Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
B3H754
|
APD3_ARATH
|
MGSIRGDLQPLFVMPPPPLDEDCDDIFNSDESSWGLLSLSCFGIIMGLWFFASVCLIFGVYGSETVWLGPNSSILVKPSSIFVKSIKVKELDFSKPGLQLYGFNGQSTPSGYFVNWTESRVLSVSQNSYKGWPYYLNRGTHMNISYNILPKGSAVRLVITEGSQVIGMPFFYRSSLKDIAFRDTAWSWNLIQGSGMIQLDISKSKGYYLTVANLKRKDIEVELDIDVKAVLYDTKQTSYNCSFSNGECSFKMNERYPVENYAVVTSPALGQGVSIDDEWYIELSYQPRLIAYGSFTGVLLSFMLVAIHFCNKLKCCGGEGFLSGDDSVRTCLLADKGDNDCCNDVEASNKSLCAICFDAPRDCCFLPCGHCVSCYQCGTKIKRTKGRCPICRKKMIHVKRIYTA
|
2.3.2.27
| null |
mitotic cell cycle [GO:0000278]; pollen development [GO:0009555]; protein ubiquitination [GO:0016567]
|
endosome [GO:0005768]; plant-type vacuole membrane [GO:0009705]
|
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
|
PF16041;PF16040;PF13920;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q0WS06}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q0WS06}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q6DBH0};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q6DBH0}.
| null | null |
FUNCTION: Involved in pollen mitosis II (PMII) regulation during male gametogenesis. {ECO:0000269|PubMed:22897245}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
B3H7A9
|
PXG7_ARATH
|
MSHQTVALASKAKSPKPKRGKLDKEKMTALEKHVSFFDRNKDGTVYPWETYQGFRALGTGRLLAAFVAIFINMGLSKKTRPGKGFSPLFPIDVKNSHLCMHGSDTDVYDDDGRFVESKFEEIFNKHARTHKDALTAEEIQKMLKTNRDPFDITGWLSDYGEWKILHTLAQDKNGLLSEKSVRAIYDGSLFHQLEKKRSSSSSRGKKQKLP
|
1.11.2.3
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
| null |
extracellular region [GO:0005576]
|
18-hydroxyoleate peroxygenase activity [GO:0102070]; calcium ion binding [GO:0005509]; lipase activity [GO:0016298]; monooxygenase activity [GO:0004497]; plant seed peroxidase activity [GO:1990137]
|
PF05042;
|
1.10.238.10;
|
Caleosin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11431566}.
|
CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
| null | null | null | null |
FUNCTION: Probable calcium-binding peroxygenase. May be involved in pollination.
|
Arabidopsis thaliana (Mouse-ear cress)
|
B3H7I1
|
SOP12_ARATH
|
MRNTISSKMGQVLIVLLLLCTVLCRTESALPSGQHSVLLTGRRLMGSGASGPVRSSQSSQAGGRFNDADPIAIDYGKY
| null | null |
cell-cell signaling involved in cell fate commitment [GO:0045168]; defense response to insect [GO:0002213]; indole glucosinolate biosynthetic process [GO:0009759]; jasmonic acid biosynthetic process [GO:0009695]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; plant-type cell wall organization [GO:0009664]; regulation of defense response to bacterium [GO:1900424]; regulation of defense response to fungus [GO:1900150]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of root development [GO:2000280]; regulation of root meristem growth [GO:0010082]; regulation of unidimensional cell growth [GO:0051510]; response to bacterium [GO:0009617]; response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to wounding [GO:0009611]
|
apoplast [GO:0048046]; plasma membrane [GO:0005886]
|
LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612]
| null | null |
Serine rich endogenous peptide (SCOOP) phytocytokine family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34535661}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:34535661}. Note=The precursor of SCOOP12, PROSCOOP12, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP12 in the apoplasm. {ECO:0000269|PubMed:34535661}.
| null | null | null | null | null |
FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including root growth prevention, phospholipid signaling pathway activation (e.g. accumulation of phosphatidic acid (PA), but transient reduction of phosphatidylinositol 4,5-bisphosphate (PIP(2)) levels) and reactive oxygen species (ROS) response regulation (PubMed:30715439, PubMed:33514716, PubMed:34535661). Moderates primary root growth, and regulates root meristems and cell elongation; this root growth regulation is associated with the modulation of ROS metabolism and alteration of cell wall structure, and depends on variations in many genes expression (PubMed:34535661, PubMed:35639812). Promotes ROS (e.g. superoxide anion O(2) and hydrogen peroxide H(2)O(2)) production and MAPK (e.g. MPK3, MPK4 and MPK6) activation in a MIK2-dependent manner, thus leading to the up-regulation of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2) (PubMed:34535661, PubMed:35639812). Involved in biotic and oxidative stress responses; acts as a negative regulator of defense against necrotrophic pathogens such as the bacteria Erwinia amylovora and the fungus Alternaria brassicicola (PubMed:30715439). Able to prime defense responses against the pathogenic bacteria Pseudomonas syringae pv. tomato DC3000 (PubMed:30715439). Contributes to the triggering of defense responses toward generalist herbivores such as Spodoptera littoralis, probably via the activation of jasmonate and indole glucosinolate biosynthesis (PubMed:35401621). Triggers the expression of several PROSCOOP genes (e.g. PROSCOOP3, PROSCOOP7, PROSCOOP12 and PROSCOOP13) (PubMed:30715439). {ECO:0000269|PubMed:30715439, ECO:0000269|PubMed:33514716, ECO:0000269|PubMed:34535661, ECO:0000269|PubMed:35401621, ECO:0000269|PubMed:35639812}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
B3KU38
|
IQIP1_HUMAN
|
MRLEELKRLQNPLEQVNDGKYSFENHQLAMDAENNIEKYPLNLQPLESKVKIIQRAWREYLQRQEPLGKRSPSPPSVSSEKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK
| null | null |
negative regulation of cytoskeleton organization [GO:0051494]; positive regulation of hippo signaling [GO:0035332]
|
axon initial segment [GO:0043194]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
| null |
PF15157;PF10148;
| null | null | null |
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:A0A088MLT8}. Cytoplasm {ECO:0000269|PubMed:17045569}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000250|UniProtKB:A0A088MLT8}.
| null | null | null | null | null |
FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25950943). May also play a role in axon outgrowth and guidance (By similarity). {ECO:0000250|UniProtKB:A0A088MLT8, ECO:0000269|PubMed:25950943}.
|
Homo sapiens (Human)
|
B3L2V1
|
PSD_PLAKH
|
MKKNGRDNNFYHLYKNKYLITGVTILSFILMFQYKYHEVLTLHDNSENAVQSSKLFWARLLFGRTRSRITGQILKMEIPNTYRLFIFNFLIKYMHINKEEIKYPIESYKSIGDFFSRYIREETRPIGDVSDYSIVSPCDSELIDYGELTSEYLENIKGVKFNVNTFLGSKFQKKHNDGSTKFFYAIFYLSPKKYHHFHAPFNFKYKIRRHISGELFPVFQGMFKFINNLFNINERVILSGEWKGGNVYYAAISAYNVGNIKIINDEELVTNNLRHQLSYMGGDINTKIFDSYKSVEVGDEIGEFRMGSSIVVIFENKKDFSWNVNQNQTVSVGQRLGGIGEPVKEENRFIKIRS
|
4.1.1.65
|
COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:25724650}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:25724650};
|
phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540]
|
endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]
|
phosphatidylserine decarboxylase activity [GO:0004609]
|
PF02666;
| null |
Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily
|
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22057268}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GPP8, ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Equally found in the membrane-bound as well as in the soluble fraction. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268, ECO:0000269|PubMed:25724650};
| null |
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:22057268}.
| null | null |
FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268}.
|
Plasmodium knowlesi (strain H)
|
B3LF48
|
EHD2_ARATH
|
METSSTISIGSCLKEHQKIYKEWFNIADSDGDGRVSGNDATKFFAMSKLSRQELKQVWAVADSKRQGFLGLSEFITAMKLVSLAQEGHEITSDLLKGSIDMKSVELPVLEGLENVVSKQKVSKTNVDVEDNVVTKPQVTAKTPWFKSKSIIKPQVNVVTIVDGLKRLYTEKLKPLEVTYRFNDFASPVLTSSDFDAKPMVMLLGQYSTGKTTFIKHLLGCDYPGAHIGPEPTTDRFVVAMSGPDERTIPGNTMAVQADMPFNGLTSFGGAFLSKFECSQMPHPVLDQITLVDTPGVLSGEKQRMQRSYDFTGVISWFASKCDMILLLFDPHKLDISDEFKRVITSLRGNEDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVLNTPEVVRVYIGSFNDKPINEVAVGPIGKELFEKEQNDLLADLMDVPKKACDRKINEFVKRARSAKINAYIMSHLKKEMPAMMGKSKAQQRLMDNLEEEFGKVQREFHLPAGDFPSVEHFREVLGGYNIDKFEKLKPKMIQAVDDMLGYDIPDLLKKFRNPYDN
|
3.6.5.2
| null |
endocytosis [GO:0006897]; endosomal transport [GO:0016197]; protein homooligomerization [GO:0051260]; regulation of actin cytoskeleton organization [GO:0032956]
|
cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
|
calcium ion binding [GO:0005509]; G protein activity [GO:0003925]; GTP binding [GO:0005525]
|
PF18150;PF00350;PF12763;PF16880;
|
1.10.268.20;1.10.238.10;3.40.50.300;
|
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, EHD subfamily
| null |
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q641Z6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q641Z6}. Cell membrane {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Peripheral membrane protein {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVK4}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}. Cytoplasm {ECO:0000269|PubMed:18547399}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00758};
| null | null | null | null |
FUNCTION: Involved in endocytosis negative regulation, probably by influencing actin organization. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Exhibits an inhibitory effect on endocytosis when over-expressed. {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
B3LGE9
|
ARO1_YEAS1
|
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGEKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFLDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETGSAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
|
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
|
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
|
PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202;
|
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
|
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
|
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
| null |
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
| null | null |
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
|
B3LV44
|
HH_DROAN
|
MDNSDCRVPWASAPSSMTCLSLDPTKCHSSSSSSKCQPDCDTPPAAEKIQRHIAYTQRCPGKITTLLAVLLLVLPLSFTPAHSCGPGRGLGRRRERNLYPLVLKQTIPNLSEYTSGASGPLEGPIRRDSPKFKDLVPNYNRDILFRDDEGTGADRLMSKRCKEKLNVLAYSVMNEWPGVRLLVAESWDEDYQHGKESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLEGGVRKPLGELSIGDRVLSMTSNGQPVYSEVILFMDRNLKQMQNFVRLHTAGGAVLTVTPAHLVSVWQPERQELTFTFADRIEERQHVLVRNEETGELRPDQVIKVESVRSMGVVAPLTREGTIVVNSVAASCYAVINSQSLAHWGLAPMRLLSTLEAWLPAKDQLRSSKDHPKDSSAERQNGIHWYAEALYKIKDYVLPKSWRHD
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila ananassae (Fruit fly)
|
B3M185
|
RAS1_DROAN
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
|
3.6.5.2
| null |
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}.
|
Drosophila ananassae (Fruit fly)
|
B3M301
|
SPAST_DROAN
|
MVRTKNQSSSSSASSSTKSPIKSGSAGSGSAAGGNSASGSRQSTHRSSSASNVASAAAAAVASSNRTRTSPGSSPDGDDDTTTTDDLTPTSCSPRSGHHHHGHPYGGSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSKDQQQQHQSQPLSYPLELSEGGNPEQQLPSQTQRYRAIQPLEMASNRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLRMQRLSLKEKQQKTLPQSDYKALKSREPMLAGMTNDPLKPRVRSSGYGPKASTSAQAAAATAASGRKLTIGTKRPGNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPLRSRTPINNNGPSTSGSGASTPVVSVKGVEPKLVQLILDEIVEGGAKVEWSDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLSRLLQKQGSPLDTEALRRLAKTTDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITESDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila ananassae (Fruit fly)
|
B3M3M6
|
UBP36_DROAN
|
MPVSVAVCETTNVVNAALRESLGVGIGSGGASSDDKSAGEDTNSLQNHIVANAKRILMTKIEYEEVPNYQEAVLENLKSKYIVIKPTNPTNGCNLNGNTANTFGNKNNAGKIVGANGHDNNGRKLSDHPNQNHNHANPNGHHANPNELPKPKRVLYPRENIRIGWKQSERKWQVGSGMINAGNTCYLNSTLQALFHIPALANWLVSEQAHMENCNVSESGSFCIICAMAKTLQATQTTQSAVRPFLIYTKLKQICKHMIVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKSDSLEEAFEGYFSREKLEDFGYKCEGCKKKVSATKQFRLERAPITLCIQLKRFSMMGNKLTKQITFKPRIDLSKFAARSPAASVQPLIYRLVSMVTHLGVSQHCGHYTAIGSTEAGSYYNFDDSYVRPIAIQSVCNTNAYIMFYELDPLQTSSPAAARANGLRLTNGHGPVPVAVPATVSSPLPSPAKFIGPQLPPGGINGYSNGHGPKTTIQFKPQHQPSHQQNGVQQSAKSPLLSTHVKVEAAAGAAALAASAAPTANGNKSSSNHSNHKSVNQQHYLPISSEDEDSEDEVKARPTVQLPSMPKMDDCMDSGKPKSPVKTPVKTPLKSLVPYESASEEEEVVPLPNPNARKRSSDSSDSEHEPTTSSVQLNGHSKTNGSLSNGSSKSTDAIDEIFKSLKGYQAKKKSADSEDDDDDEDEPNNQLTNGWHPQKQSQSQSRSGPPSPKTPPSPAVIKSKTGIWKVTRDDGDDDEDDDDDDDEVVEEARAVRTPVKNHRNPFASSKTATDSPTTPGAKRQKLLNGSAIKTQQQPRAGNGYQSEATANGGTVNELLKQSHRGYSSSVLSWNGKPAELEKEPFVLVCAKRIAGHGSLDGSGSGSNTDIIDTEIPAAAVNFPSGSCSFSLLADARDQRQRDLADDEENEMDRGRQRKVKSGSAKISNSTPGYNPFMEFENQKRWHKNGGGGGFPRFYQNQNFRQGFQQRNKFKFNRFGGPGSAKFQQQRALQRHLAAGGGFTRRQPTHSAQQQQQQQS
|
3.4.19.12
| null |
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; positive regulation of proteasomal protein catabolic process [GO:1901800]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; somatic stem cell population maintenance [GO:0035019]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]
|
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). Controls selective autophagy activation by ubiquitinated proteins. {ECO:0000250|UniProtKB:Q9VRP5}.
|
Drosophila ananassae (Fruit fly)
|
B3M6I4
|
PLK4_DROAN
|
MLSNRAFGETIEEYEVQHLLGKGGFASVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIGRPFTEAEAASILRQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHVTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQTTLNKVVLSEYIMPTHLSFEAQDLINKLLKKVPHERIALEHVLRHPFLTKRLENSSNGVYSTPGALNVFSQSLESGDSGIITFASSDSRNSQRLRSVENTAPLQGLPQIQEEYMQDKYRPTYDQPGLFKQPSSTRMEHNWLTTEKDTPFRMDVPMKEKPAPLKEERISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKYRPKFNEDRVTDICRISDDGRRIIIYQPDPGRGLPIRDHPPELQIPNEDCVYNYDSLPSKHWKKYVYADRFVGLVKSKTPKVTYFSALGKCQLMETMTDFEIRFYSGAKLTKSPSEGLKVHNANGMLLSDHVGSEARSMIDHGNECFTHCVSISNALEMAQTKDNSCFPVTIGRRPVTEVQPSQRLDGLRDTTNFAYSTPKSNQGSINFSVSTISSIRNTTDFGSNSSRTNMRASQQNIPIKRINLPDIGVATELSHGVVQVQFYDGSVVSIIPDIQGGGVTYTQSNGISTHFGKDDDLPFTVREKLSQLPHIQLKLKTAPLLSNSRKIEFNAMTPKTTTPCYNRMLL
|
2.7.11.21
| null |
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}.
|
Drosophila ananassae (Fruit fly)
|
B3MEY6
|
LIS1_DROAN
|
MKMVLSQRQREELNQAIADYLGSNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSMSGHRASITRVIFHPIFGLVVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQTYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTVKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSRDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLFTLNGHDNWVRGLAFHPAGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; iron-sulfur cluster assembly [GO:0016226]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; CIA complex [GO:0097361]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila ananassae (Fruit fly)
|
B3MH43
|
PTK7_DROAN
|
MAALRISVWILVQALMMALVSSNSSHFLQLPQSQSVVENESVDFECQASTDPSSELHYEWLHNGHRIAYDKRVYQIGSHLHIEAVQRAEDVGDYVCIATSLASGAREASPPAKLSVIYIDSASVQLLGSNRNELLLKCHVEAVSGSDDPLQIEWYRNSAKLSSWQNVQLDQHRLIIRQPSAADDGLYRCTASNAAGRVMSKQGYVYRSSLKCLPRLPRRKNQKLPESWSKEVFLCRGKRGGSGGVEALPSAPEDLRIVQGPASHAIIKEGDPAALTCLYELPAELQNQRIQLRWRKDGKLLRHVELGNSLPLPGISSDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEGYAPINSSPGTLEVIEQLKFVPQPTSKNLELDAPIAKVHCKAQGTPTPQVQWMRDDANTSLPDQVEVDANGTLIFRNVNADHRGNYTCLATNSQGQINATVAINVVVTPKFSVPPVGPIETAEQGNVVIHCQAIGDPKPTIQWDKDLTYLSENNTDRERFRFLENGTLEIRNVQAEDEGSYGCTIGNSAGLKREDVQLVVKTAGDGFPPEESGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNELSTKEAGGDQPDGAANGKGSEQEPCLSKQRNGHGGQSRSKSNGDAQKSDDTACSQQSRASKKSAHIYEQLALPRSGLTELIQIGRGEFGDVFVGKLKASLVATGSPSDKDADTEKQHSNSENGSGGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQQQSDLDQLVLVKALNKVKDEQACQEFRRQLDLLRGISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTASAAATSSPPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNTLLPIRWLAPECIQEDEYTTKSDIFAYGVVVWELFNQATKLPHEELTNEQVIQKSQAGTLEWTVAESTPDSLREILLSCWVSNPKERPSFSQLGAALSKAMQSLEK
| null | null |
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila ananassae (Fruit fly)
|
B3MPN6
|
IRS1_DROAN
|
MASISDDGMVLSGYHKKLKTMKKKFFVLYEETSINQARLEYYDTEKKFLQRAEPKRVIYLKDCFNINRRLDTKHRFVIVLSSREGGFGIVLESENDLRKWLDKLLLLQRNIANVNGQVYSAYEHVWQVIIQKKGMSEKVGITGTYHCCLSAKSLTFVCIGPEKTANGDDRISSIEILLTTIRRCGHASPQCIFYMELGRQSVLGSGELWMETDNAAIATNMHNTILSAMSAKTDSNTNLINVYQARPDISHEPMRKRSSSANEASKPINVIQNRQNSLELRNCSSPHNYGFPRERCDSLPTRNGTLSESSNQSYFGSNLGLRSNTISGIRPHSTSKHSNSPTFNMPLRCSESEDSSISIDESDDNASFGHYRLNTRSSKGAIPEENLDDFASAEYCKGSGPSGDDNYIPMTPIKPASFCEPDKVELPKPDDPNLHINFPEHTSEKLENDFDLDSDNQCGRPIRAYSIGNKVEHLKLNRRLGYLNDTGQNSNRVRAYSVGSKSKIPRCDLQRVVLVEDNRFDTNRSQNNISKEGPISGTSTNREKKSTSAPLLSLKNQINQDRMSDLMEIDFSQSSKIEPWTPAQFKRNVMDVVPKNIESVFPKSYRNDSSNLTLHATSQKDIFNGGKLNTTESSSEGGYLEMKPVGNAFSSSPVTLPSKIEKLKLKDNTELPVHELHKVSSYNIPPEKRKEQTPTQTRIEEKTLNSQLNEKLINTESANVVANITPNVPELKSDKKNNVESLIIENNNWDLGTTDEKKLVHSISSEDYTQIKDKLNDLTKNNEVGYKILQIKSDSSLISSKITLKNRLRDNLERQQRLTESVNTIPDKSPSATTKGTFYSLGNNFQTPPNNVVNNTLDNILQTKDLNFPSRPSSQASQPELHYAKLDLPNCSDQNPAKYLKRGSRESPPVATCAEDGNTYARIDFDQSDSSSSSSKIFNM
| null | null |
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; lipid homeostasis [GO:0055088]; long-term synaptic potentiation [GO:0060291]; male germ-line stem cell asymmetric division [GO:0048133]; multicellular organism growth [GO:0035264]; negative regulation of entry into reproductive diapause [GO:0061964]; negative regulation of triglyceride catabolic process [GO:0010897]; olfactory learning [GO:0008355]; positive regulation of border follicle cell migration [GO:1903688]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell size [GO:0045793]; positive regulation of immune response [GO:0050778]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primary spermatocyte growth [GO:0007285]; regulation of tube length, open tracheal system [GO:0035159]; response to anoxia [GO:0034059]; vitellogenesis [GO:0007296]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
|
PF02174;
|
2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell proliferation, cell size, and body and organ growth throughout development. Also has a role in a signaling pathway controlling the physiological response required to endure periods of low nutrient conditions. Insulin/insulin-like growth factor (IGF) signaling pathway has a role in regulating aging and is necessary in the ovary for vitellogenic maturation (By similarity). {ECO:0000250|UniProtKB:P35570, ECO:0000250|UniProtKB:Q9XTN2}.
|
Drosophila ananassae (Fruit fly)
|
B3MRI9
|
SWS_DROAN
|
MDVLELLRASATGSYTALFSDAWCQYVSKQITNSMYLYCALGVLSMVFLAWFMYFKRLARIRLRDEASRSMSAVNSSSGGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIDGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMEAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRFKSSTIMAPSTHSSQCSRQTGSQPTLGVPAPTCSNTTTTASPTTANTVHSGLAGANGVIGQSRPPISPSRHSREEHTLSDPNPNPDVINTSVGGASGTSMYAEVHGDAPNVDVFHQQQHSVGNLSTRRGSISQMAPDLGPALSQPGLGQGQGLGPGVTGAPPLMTGAPASKIDMRLVHASAVDSLRKELGLPEEDSHIIEPFVEVRELEPNVTLITEGNSDDVCVWFVMTGTLAVYQANQDAARAKQQQEKNDMLIHFVHPGEIVGGLAMLTGEASAYTIRSRNNSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDEISDSTYIVLSGRMRSVITHPGGKKEIIGEYGKGDLVGIVEMITETSRTTTVLAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGTMQTRSSSAAPGGPVEANPVTHKYSTVALVPITDEVPLTPFTYELYHSLCAIGPVLRLTSDVVRKQLGPNIFEAANEYRLTSWLAQQEDRNIITLYQCDNALSAWTQRCMRQADVILIVGLGNGSHLVGKFEREIDRLAMRTQKELVLLYPETTNSKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGQLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFENMAKAGRLGRFNQWFNKEPPKRGNHASLNEYTFIDLAQIVCRLPETNAGNSADIFSEDEDCDGYISEPTTLNTDRRRIQVPRAGNSLSFSENEMDSDVELDLQLDRKTEKSIHSAATSVARGSMRSREFHKLEQDRSVEITRLKDETERIMAPTNLDRKGDGQEQEKEPEQEQELETEEPNQENTEVEEEQRNQGEGNEDNKENKGGAYNETKN
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila ananassae (Fruit fly)
|
B3N5J3
|
FICD_DROER
|
MGTEAEPPSPPSPPAQQQEQANPPVWNAQNQKPARLYRLVLFFIAGSLTAWMFHAFSSSNLAWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASFTEAEQTSINEALVSLRMAQDMYLTGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQNLDQRRLESLDSKRDALSAIHESNAALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIEITIKDILELHRRVMGHVDPIEGGEFRRNQVYVGGHIPPGPGDLALLMQRFERWLNSEHISTLHPVNYAALAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGALP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-250 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila erecta (Fruit fly)
|
B3N946
|
IRS1_DROER
|
MASISDDGMALSGYLKKLKTMKKKFFVLYEETSNSSARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKQRFVIVLSSRDGGFGIVLESENDLRKWLDKLLVLQRNIANTNGTAYSPYDQVWQVVIQKKGISEKVGITGTYHCCLTSKSLTFVCIGPDKTPNGEERVASIEILLTTIRRCGHASPQCIFYVELGRQSVLGSGDLWMETDNAAVATNMHNTILSAMSAKTESNTNLINVYQNRPDLSHEPMRKRSSSANEASKPINVNVIQNSQNSLDLRSCSSPHNYGFGRERCDSLPTRNGTLSESSNQTYFGSNHGLRSNTISGIRPHSSNKHSNSPTFTMPLRCSASEESSISIEESDDNGSFSHYRLNTRSSETAIPEENIDDFASAEFSKVSEQNESDENYIPMTPINPTDAIHEKEKVDMQRLEDGSLHFDFPEHASEKLARDFDLDSDNQCGRPIRAYSIGNKVEHLKFNKRLGHLNDTGQNPNRVRAYSVGSKSKIPRCDLQRVVLVEDNKHEFAANRSQSSITKEGTSYSTSSNRQKKSTSAPLLSLKNHINSDRMSDLMEIDFSQATNLEKQKFIKNNEIPKYIENVFPKTPRTDSSSLTLHATSQKDIFNGTKLNNTVNASEEGYLEMKPVGNAYTPSSNCLPIKVEKLKISDYTAPLTTAAPVHDLNKISAYNISAEKWKEQSLCEEKKSNSPLNETPCSLKPTDVESNSHDEHSTNNMECEVSVQCDKQNNLDDKVAENNNLDIGGHEEKKLVHSISSEDYTQIKDKSNDFTKFNEAGYKILQIKSDSSLISLKLYQKGIHKDNLERSHRLTESVNTIPDNATASSSVTKFNINTKAADSRSTDPSTPQNILQIKDLNFPSRSSSRISQPELHYASLDLPHCSGQNPAKYLKRGSRESPPVSACPGDGNTYAKIDFDQSDSSSSSSNIFNT
| null | null |
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; lipid homeostasis [GO:0055088]; long-term synaptic potentiation [GO:0060291]; male germ-line stem cell asymmetric division [GO:0048133]; multicellular organism growth [GO:0035264]; negative regulation of entry into reproductive diapause [GO:0061964]; negative regulation of triglyceride catabolic process [GO:0010897]; olfactory learning [GO:0008355]; positive regulation of border follicle cell migration [GO:1903688]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell size [GO:0045793]; positive regulation of immune response [GO:0050778]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primary spermatocyte growth [GO:0007285]; regulation of tube length, open tracheal system [GO:0035159]; response to anoxia [GO:0034059]; vitellogenesis [GO:0007296]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
|
PF02174;
|
2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell proliferation, cell size, and body and organ growth throughout development. Also has a role in a signaling pathway controlling the physiological response required to endure periods of low nutrient conditions. Insulin/insulin-like growth factor (IGF) signaling pathway has a role in regulating aging and is necessary in the ovary for vitellogenic maturation (By similarity). {ECO:0000250|UniProtKB:P35570, ECO:0000250|UniProtKB:Q9XTN2}.
|
Drosophila erecta (Fruit fly)
|
B3NC86
|
UBP36_DROER
|
MPVSMAVCETANVVNAALRESLGGNSSAAGSSADQAKSGEESNGSLQNHIVANAKRILMAKIEYEEVPNYHESVLESLKSKYIVIKPGNPGAINGFGGKNNTGKVVGANGHDNNGARKQAEHPNNQSHHNNHNNHPHPTSNPNELPKPKRVLYPRENIRIGWKQSERKWQVGTGMINVGNTCYLNSTLQALLHIPALANWLVSEQAHLENCNVAESGGGCIVCAMAKTLLATQSNQSAVRPFLIYSKLKQICKHMVVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADTLEDAFEGHFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMIGNKLTKQISFKPRIDLSKYAARSPAAQAQPLTYRLVSMVTHLGVSQHCGHYTAIGSTDTGSYYNFDDSYVRPIAMQSVCNTNAYIMFYELDLSQTASPAANRPNGMRLTNGHSTTPVPATTVSSPSPTRFIGPQLPPGGVNGYSNGNAQKTAIQFKQHHQQSQQNGFQLGTGKFQDTAKPPLVGAHAKGEANPAPTANGNKSSSTSSNNSSSSNHKSINQQQYLPISSEDEDSEDERTSRPSTVQLPSMPKMTDDHTEKPKSPVKIQAKTPIKTPLKSLVPYESASEEEEAPLPNPRKRRSGEDSSESDQESGQTNGHSKTNGSLTNGSASSSVHVNNSKLKTDAIDEIFKSLKKSADSDDDDDEEESSIQLTNGWHPQKQSQSQSKAPPSPKTPPSPAVIKSKTGIWKVTRNDEVDDIDDDDDEEEEATVKIQTPSKTHRNPFSSSKPSTDSPATPGAKRQKLLNGSPVKSHQQPRVGNGYQSEATSNGSTINELLKQSHRGYGSSVLSWNGKPAELEKETFELVCAKRIAGHGSVDGSDIVESSVAVNASSGSDSNDVVVIAVALLVDAREQRQRDLDDDEENEMDRGRQRKVKSGSAKGNNASNSTPGYNPFQEYEGQKRWNKNGGGGGGFPRFYNQNFRQNFQQRNKFKFNRFGGPGGAKFQQQRALQRHLAAGGGFSRRQPSAQQQQQQS
|
3.4.19.12
| null |
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; positive regulation of proteasomal protein catabolic process [GO:1901800]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; somatic stem cell population maintenance [GO:0035019]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]
|
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). Controls selective autophagy activation by ubiquitinated proteins. {ECO:0000250|UniProtKB:Q9VRP5}.
|
Drosophila erecta (Fruit fly)
|
B3NE99
|
PLK4_DROER
|
MLSNRAFGETIEDYEVQHLLGKGGFAIVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSTPGALNMFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIQEEFKHHKLTYEQPGLFRQTSTGLAEPNWPGATKASSFRMEMGMVQNSKPAPVKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFFRFRPTYNEDRITDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYENLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMFLSDHSCSESRSLIEHGNECFTHCVNISNALEVAQTKENSCFPVTIGRRPLTDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSVSTISSTRNTTGFETNCSRSNMLAAHQNIPIKRISVPDVGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKDDDLPFPVRDRVGQIPNIQLKLKTAPLLESGRKIDYNAMTPKTTTPCYNRMLL
|
2.7.11.21
| null |
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}.
|
Drosophila erecta (Fruit fly)
|
B3NPW0
|
LIS1_DROER
|
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFGLMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila erecta (Fruit fly)
|
B3NS99
|
PTK7_DROER
|
MTARMISIYGLVLASMMASVWASSSRFQRLPQSQSVVENESVKFECESTDSYSELHYDWLHNGHRIAYDKRVHQIGSNLHIEAARRTEDVGSYVCIATNLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDSEPLEIEWYRNSEKLSTWKNVQLDQHRLIIRQPGSDDDGLYRCTASNAAGRVMSKQGYAYQSSVKCLPRLARRKNQKMMESWDKQTFLCRGKRGGAAGLEALPAAPEDLRIVQGPVGQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPITGHSFDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEGHLPISSTPGVLEVIEQLKFVPQPTSKNLELDAVVAKVHCKAQGTPTPQVQWVRDGENSTLPDQVEVDANGTLIFRNVNSEHRGNYTCLASNTQGQINATVAINVVVTPKFSVPPVGPIETSEQGTVVMHCQAIGDPKPTIQWDKDLKYLSENNTDRERFRFLENGTLEIRNVQVEDEGSYGCTIGNSAGLKREDVQLVVKTTGDGFAPEESGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNDLSTKEAGGDQPDAAGNGKGSEQEPCLSKQHNGHSKSRSKSSGDAQKSDDTACSQQSRASKKSAHIYEQLALPRSGLSELIQIGRGEFGDVFVGKLKATLVTSPTDKDADTEKQHSNSENGSGGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQHNQSALEQLVLVKALNKVKDEQACQEFRRQLDLLRAISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATAGSSSPPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNTLLPIRWLAPECIQEDEYTTKSDIFAYGVVVWELFNQATKLPHEELTNEQVVQRSQAGSLEWSVAEATPDSLREILLSCWVSNPKERPSFSQLGAALSKAMQSVEK
| null | null |
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila erecta (Fruit fly)
|
B3NY03
|
SWS_DROER
|
MDVLEMLRASASGSYNTIFSEAWCQYVSKQITATMYMYCALGMMGVLFLAWFMYFKRMARLRLRDEIARSISAVTNSSGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMQAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRYKSVSTMSGPINSQTSQSSRQTPNGPPMGISHPLNLMQSTASGTGSGSGSGVSVTVTRPPPSPSRHSREEHTLSDPNPNPDGSVHGTSNLFTEVHGDAPNADLFHQQQQSVGNLSTRRSSITQMTPDGSHSCPPAPGVTTSIDMRLVQSSAVESLRKELGLSEEDAHIIEPFVELRELEPNVTLITEGNADDVCVWFVMTGTLAVYQSNQDATRAKQDKSDMLIHFVHPGEIVGGLAMLTGEASAYTIRSRSNSRIAFIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGSMQTRSGSGAPGAPVEANPVTHKYSTVALVPITDEVPLTPFTYELYHSLCAIGPVLRLTSDVVRKQLGPNIFEAANEYRLTSWLAQQEDRNIITLYQCDSSLSAWTQRCMRQADVILIVGLGDRSHLVGKFEREIDRLAMRTQKELVLLYPEATNAKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPVDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFENMAKAGRLGRFNQWFNKEPPKRVNHASLNEYTFIDLAQIVCRLPETYAVNTADLFSEDEDCDGYISEPTTLNTDRRRIQVPRAGNSLSFSETEMDSDVELDLKLERKTDKSTQSSPPTSSRTSMRGKEEARHMDNWHWGAKHKNETGSGATEGIHTSTEQEQEHQQQQQQDQGVRAEQLVYKDEDKENRSSANNETKN
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila erecta (Fruit fly)
|
B3NZR4
|
RAS1_DROER
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
|
3.6.5.2
| null |
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}.
|
Drosophila erecta (Fruit fly)
|
B3P7F8
|
HH_DROER
|
MDNTSSVPWASAASVTCLSLDAKCHSSSAKSAASSISASPETQAMRHIAHTQRCLSRLTSLVALLLIVLPMTFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCREKLNLLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLENGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGEAVLTVTPAHLVSVWQAESQKLTFVFADRVEEKNQVLVRDVETGELRPQRVVKVGSVRSKGVVAPLTREGTIVVNSVAASCYAVINSQSLAHWGLAPMRLLSTLEAWLPAKEQLHSSPKVVTTAEQQNGIHWYANALYKVKDYVLPQSWRHD
|
3.1.-.-
| null |
Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm development [GO:0007506]; heart formation [GO:0060914]; hindgut morphogenesis [GO:0007442]; imaginal disc-derived wing morphogenesis [GO:0007476]; intein-mediated protein splicing [GO:0016539]; labial disc development [GO:0035217]; morphogenesis of larval imaginal disc epithelium [GO:0016335]; mucosal immune response [GO:0002385]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; negative regulation of proteolysis [GO:0045861]; pole cell migration [GO:0007280]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of protein localization to cell surface [GO:2000010]; progression of morphogenetic furrow involved in compound eye morphogenesis [GO:0007458]; protein autoprocessing [GO:0016540]; regulation of cell proliferation involved in compound eye morphogenesis [GO:2000495]; regulation of epithelial cell migration, open tracheal system [GO:2000274]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; spiracle morphogenesis, open tracheal system [GO:0035277]; terminal cell fate specification, open tracheal system [GO:0035154]; ventral midline development [GO:0007418]; wing disc pattern formation [GO:0035222]
|
cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila erecta (Fruit fly)
|
B3P8A3
|
SPAST_DROER
|
MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHTYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELSREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKPKVQAPSKPQKTREPMLAGMTNEPMKLRVRSSGYGPKATTSAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila erecta (Fruit fly)
|
B3PC73
|
AGUA_CELJU
|
MSTFARLFLCLVFFASLQPAMAQTEDGYDMWLRYQPIADQTLLKTYQKQIRHLHVAGDSPTINAAAAELQRGLSGLLNKPIVARDEKLKDYSLVIGTPDNSPLIASLNLGERLQALGAEGYLLEQTRINKRHVVIVAANSDVGVLYGSFHLLRLIQTQHALEKLSLSSAPRLQHRVVNHWDNLNRVVERGYAGLSLWDWGSLPNYLAPRYTDYARINASLGINGTVINNVNADPRVLSDQFLQKIAALADAFRPYGIKMYLSINFNSPRAFGDVDTADPLDPRVQQWWKTRAQKIYSYIPDFGGFLVKADSEGQPGPQGYGRDHAEGANMLAAALKPFGGVVFWRAFVYHPDIEDRFRGAYDEFMPLDGKFADNVILQIKNGPIDFQPREPFSALFAGMSRTNMMMEFQITQEYFGFATHLAYQGPLFEESLKTETHARGEGSTIGNILEGKVFKTRHTGMAGVINPGTDRNWTGHPFVQSSWYAFGRMAWDHQISAATAADEWLRMTFSNQPAFIEPVKQMMLVSREAGVNYRSPLGLTHLYSQGDHYGPAPWTDDLPRADWTAVYYHRASKTGIGFNRTKTGSNALAQYPEPIAKAWGDLNSVPEDLILWFHHLSWDHRMQSGRNLWQELVHKYYQGVEQVRAMQRTWDQQEAYVDAARFAQVKALLQVQEREAVRWRNSCVLYFQSVAGRPIPANYEQPEHDLEYYKMLARTTYVPEPWHPASSSRVLK
|
3.2.1.131
| null |
glucuronoxylan catabolic process [GO:2000886]
|
cell outer membrane [GO:0009279]; extracellular region [GO:0005576]
|
alpha-glucuronidase activity [GO:0046559]; xylan alpha-1,2-glucuronosidase activity [GO:0033939]
|
PF07477;PF07488;PF03648;
|
3.90.1330.10;3.30.379.10;3.20.20.80;
|
Glycosyl hydrolase 67 family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:12169619}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.; EC=3.2.1.131; Evidence={ECO:0000269|PubMed:12169619};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 mM for aldotriouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910}; KM=0.36 mM for aldotetraouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910}; KM=0.42 mM for aldopentaouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910}; KM=0.53 mM for aldobiouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910};
| null | null | null |
FUNCTION: Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-MeGlcA) side chain of short xylooligosaccharides and releases 4-O-methylglucuronic acid. It can also hydrolyze small soluble oligosaccharides such as dobiouronic acid, aldotriouronic acid, aldotetraouronic acid, and aldopentaouronic acid. {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12169619, ECO:0000269|PubMed:12654910}.
|
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
|
B3STU4
|
VCL_CARIL
|
MVTKAKIPLFLFLSALFLALVCSSLALETEDLSNELNPHHDPESHRWEFQQCQERCQHEERGQRQAQQCQRRCEEQLREREREREREEIVDPREPRKQYEQCRETCEKQDPRQQPQCERRCERQFQEQQERERRERRRGRDDDDKENPRDPREQYRQCEEHCRRQGQGQRQQQQCQSRCEERFEEEQRRQEERERRRGRDNDDEENPRDPREQYRQCQEHCRRQGQGQRQQQQCQSRCEERLEEEQRKQEERERRRGRDEDDQNPRDPEQRYEQCQQQCERQRRGQEQQLCRRRCEQQRQQEERERQRGRDRQDPQQQYHRCQRRCQTQEQSPERQRQCQQRCERQYKEQQGREWGPDQASPRRESRGREEEQQRHNPYYFHSQGLRSRHESGEGEVKYLERFTERTELLRGIENYRVVILEANPNTFVLPYHKDAESVIVVTRGRATLTFVSQERRESFNLEYGDVIRVPAGATEYVINQDSNERLEMVKLLQPVNNPGQFREYYAAGAQSTESYLRVFSNDILVAALNTPRDRLERFFDQQEQREGVIIRASQEKLRALSQHAMSAGQRPWGRRSSGGPISLKSQRSSYSNQFGQFFEACPEEHRQLQEMDVLVNYAEIKRGAMMVPHYNSKATVVVYVVEGTGRFEMACPHDVSSQSYEYKGRREQEEEESSTGQFQKVTARLARGDIFVIPAGHPIAITASQNENLRLVGFGINGKNNQRNFLAGQNNIINQLEREAKELSFNMPREEIEEIFERQVESYFVPMERQSRRGQGRDHPLASILDFAGFF
| null | null |
protein homotrimerization [GO:0070207]; seed development [GO:0048316]; seed maturation [GO:0010431]
| null |
copper ion binding [GO:0005507]; nutrient reservoir activity [GO:0045735]
|
PF00190;PF04702;
|
6.10.250.890;2.60.120.10;
|
7S seed storage protein family
| null | null | null | null | null | null | null |
FUNCTION: Seed storage protein. {ECO:0000305|PubMed:25084379, ECO:0000305|PubMed:27128197}.
|
Carya illinoinensis (Pecan)
|
B3SV56
|
NR1D1_SHEEP
|
MTTLDSNNNTGGVITYIGSSGSSPNRTSPESLYSDSSNGSFQSLTQGCPTYFPPSPTGSLTQDPARSFGSIPPSLGDDGSPSSSSSSSSSSSSSFYNGSPPGGLQVALEDGNRVSPSKSTSNITKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKRCLKNENCSIVRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQSAMNLANNQLSSQCPLETPPTQHPTPGPMGPSPPPAPAPSPLVGFSQFPQQLTPPRSPSPEPTVEDVISQVARAHREIFTYAHDKLGTSPGNFNANHASGNRPATTPHRWESQGCPPAPNDNIMAAQRHNEALNSLRQASSSYPPPWPPGATHHSCHQPNSNGHRLCPTHVYPAPEGEAPVNSPRQGNSKNVLLACPMNMYPHGRSGRTVQEIWEDFSMSFTPAVREVVEFAKHIPGFRDLSQHDQVTLLKAGTFEVLMVRFASLFNVKDQTVMFLSRTTYSLQELGAMGMGDLLNAMFDFSEKLNSLALTEEELGLFTAVVLVSADRSGMENSASVEQLQETLLRALRALVLKNRPSETSRFTKLLLKLPDLRTLNNMHSEKLLSFRVDAQ
| null | null |
cell differentiation [GO:0030154]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cholesterol homeostasis [GO:0042632]; circadian regulation of gene expression [GO:0032922]; circadian temperature homeostasis [GO:0060086]; glycogen biosynthetic process [GO:0005978]; hormone-mediated signaling pathway [GO:0009755]; intracellular glucose homeostasis [GO:0001678]; negative regulation of astrocyte activation [GO:0061889]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of inflammatory response [GO:0050728]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of neuroinflammatory response [GO:0150079]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of bile acid biosynthetic process [GO:0070859]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasomal protein catabolic process [GO:0010498]; protein destabilization [GO:0031648]; regulation of circadian rhythm [GO:0042752]; regulation of circadian sleep/wake cycle [GO:0042749]; regulation of fat cell differentiation [GO:0045598]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of lipid metabolic process [GO:0019216]; regulation of type B pancreatic cell proliferation [GO:0061469]; response to leptin [GO:0044321]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; nucleus [GO:0005634]
|
E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; transcription corepressor binding [GO:0001222]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Ubiquitinated, leading to its proteasomal degradation (By similarity). Ubiquitinated by the SCF(FBXW7) complex when phosphorylated by CDK1 leading to its proteasomal degradation (By similarity). Ubiquitinated by SIAH2; leading to its proteasomal degradation (By similarity). Rapidly ubiquitinated in response to inflammatory triggers and sumoylation is a prerequisite to its ubiquitination (By similarity). {ECO:0000250|UniProtKB:P20393, ECO:0000250|UniProtKB:Q3UV55}.; PTM: Sumoylated by UBE2I, desumoylated by SENP1, and sumoylation is a prerequisite to its ubiquitination. {ECO:0000250|UniProtKB:Q3UV55}.; PTM: Phosphorylated by CSNK1E; phosphorylation enhances its cytoplasmic localization. {ECO:0000250|UniProtKB:Q3UV55}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000250|UniProtKB:Q3UV55}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:Q3UV55}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3UV55}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q3UV55}. Note=Localizes to the cytoplasm, dendrites and dendritic spine in the presence of OPHN1. Localizes predominantly to the nucleus at ZT8 whereas it is cytoplasmic at ZT20. Phosphorylation by CSNK1E enhances its cytoplasmic localization. {ECO:0000250|UniProtKB:Q3UV55}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC1 and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner (By similarity). Represses the transcription of CYP2B10, CYP4A10 and CYP4A14 (By similarity). Represses the transcription of CES2 (By similarity). Represses and regulates the circadian expression of TSHB in a NCOR1-dependent manner (By similarity). Negatively regulates the protein stability of NR3C1 and influences the time-dependent subcellular distribution of NR3C1, thereby affecting its transcriptional regulatory activity (By similarity). Plays a critical role in the circadian control of neutrophilic inflammation in the lung; under resting, non-stress conditions, acts as a rhythmic repressor to limit inflammatory activity whereas in the presence of inflammatory triggers undergoes ubiquitin-mediated degradation thereby relieving inhibition of the inflammatory response (By similarity). Plays a key role in the circadian regulation of microglial activation and neuroinflammation; suppresses microglial activation through the NF-kappaB pathway in the central nervous system (By similarity). Plays a role in the regulation of the diurnal rhythms of lipid and protein metabolism in the skeletal muscle via transcriptional repression of genes controlling lipid and amino acid metabolism in the muscle (By similarity). {ECO:0000250|UniProtKB:Q3UV55}.
|
Ovis aries (Sheep)
|
B3TLD6
|
LNBB_BIFB1
|
MEKSSNRRFGVRTVAAIVAGLMVGGMCTAMTASAADDSAAGYSATAPVNLTRPATVPSMDGWTDGTGAWTLGEGTRVVSSDALAARAQSLASELTKFTDVDIKAATGSATGKDISLTLDASKKAELGDEGFKLNIGSKGLEVIGATDIGVFYGTRSVSQMLRQGQLTLPAGTVATKPKYKERGATLCACQINISTDWIDRFLSDMADLRLNYVLLEMKLKPEEDNTKKAATWSYYTRDDVKKFVKKANNYGIDVIPEINSPGHMNVWLENYPEYQLADNSGRKDPNKLDISNPEAVKFYKTLIDEYDGVFTTKYWHMGADEYMIGTSFDNYSKLKTFAEKQYGAGATPNDAFTGFINDIDKYVKAKGKQLRIWNDGIVNTKNVSLNKDIVIEYWYGAGRKPQELVQDGYTLMNATQALYWSRSAQVYKVNAARLYNNNWNVGTFDGGRQIDKNYDKLTGAKVSIWPDSSYFQTENEVEKEIFDGMRFISQMTWSDSRPWATWNDMKADIDKIGYPLDIREYDYTPVDAGIYDIPQLKSISKGPWELITTPDGYYQMKDTVSGKCLALFTGSKHLDVVTQVGARPELRNCADVSVGQDQRNTANERNTQKWQIRADKDGKYTISPALTQQRLAIATGNEQNIDLETHRPAAGTVAQFPADLVSDNALFTLTGHMGMSATVDSKTVNPASPSKITVKVRAASNANTGDVTVTPVVPEGWEIKPGSVSLKSIPAGKAAIAYFNVVNTTGTGDATVQFKLTNTKTGEELGTTSVALTGSLTKDVEASDYAASSQETTGEHAPVGNAFDKNANTFWHSKYSNPSANLPHWLAFKASPGEGNKIAAITHLYRQDKLNGPAKNVAVYVVAASDANSVADVTNWGEPVATAEFPYTKELQTIALPNTIPSGDVYVKFQINDAWGLTETSAGVTWAAVAELAATAKATPVELTEPEQPKDNPEVTETPEATGVTVSGDGVANGALSLKKGTTAQLTAKVAPDDADQAVTWASSDDKVVTVDKTGKVTAVAKGVAKVTATTANGKSASVTVTVTEDSEVPGPTGPTEPTKPGTEKPTTKPTTKPNDGKLSATGADTAVLATIAALFALAGGAVVAVRRRSVR
|
3.2.1.140
| null |
carbohydrate metabolic process [GO:0005975]
|
plasma membrane [GO:0005886]
|
beta-N-acetylhexosaminidase activity [GO:0004563]; lacto-N-biosidase activity [GO:0047403]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]
|
PF02368;PF00754;PF00728;PF02838;PF14200;
|
2.60.40.1080;2.80.10.50;3.30.379.10;2.60.120.260;3.20.20.80;
|
Glycosyl hydrolase 20 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:18469123}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H2O = beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + lactose; Xref=Rhea:RHEA:21568, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:27707, ChEBI:CHEBI:30248; EC=3.2.1.140; Evidence={ECO:0000269|PubMed:18469123, ECO:0000269|PubMed:23479733}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21569; Evidence={ECO:0000305|PubMed:18469123, ECO:0000305|PubMed:23479733};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=626 uM for lacto-N-tetraose {ECO:0000269|PubMed:23479733}; KM=68 uM for chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) {ECO:0000269|PubMed:18469123}; Note=kcat is 41.1 sec(-1) with lacto-N-tetraose as substrate (PubMed:23479733). kcat is 89 sec(-1) with chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as substrate (PubMed:18469123). {ECO:0000269|PubMed:18469123, ECO:0000269|PubMed:23479733};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 with LNB-beta-pNP as substrate and pH 6.0 with PA-lacto-N-tetraose. {ECO:0000269|PubMed:18469123};
| null |
FUNCTION: Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose (PubMed:18469123, PubMed:23479733). Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro (PubMed:18469123). {ECO:0000269|PubMed:18469123, ECO:0000269|PubMed:23479733, ECO:0000305|PubMed:23479733}.
|
Bifidobacterium bifidum (strain DSM 20082 / JCM 1254 / BCRC 11844 / KCTC 3440 / E319f (Variant a))
|
B3TMR8
|
KIJDR_ACTKI
|
MENPANANPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGGEPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTDRPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAASFTIPPKPQGDIRYQADVGGGALLDIGVYPIRAAGLFLGADLEFVGAVLRHERDRDVVVGGNALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNRVFTPPATYQPVVHIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPREWSEDSLRQASLVDAVRTGARDIYFP
|
1.1.1.384
| null |
antibiotic biosynthetic process [GO:0017000]; D-xylose catabolic process [GO:0042843]
| null |
D-xylose 1-dehydrogenase (NADP+) activity [GO:0047837]; nucleotide binding [GO:0000166]
|
PF01408;PF02894;
|
3.40.50.720;
|
Gfo/Idh/MocA family
| null | null |
CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:44624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84537, ChEBI:CHEBI:84540; EC=1.1.1.384; Evidence={ECO:0000269|PubMed:21598943};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=116.4 uM for dTDP-glucose {ECO:0000269|PubMed:21598943}; KM=6.31 mM for NADPH {ECO:0000269|PubMed:21598943}; Vmax=0.01 mmol/min/mg enzyme {ECO:0000269|PubMed:21598943}; Note=kcat is 6.24 sec(-1) for dTDP-glucose as substrate. {ECO:0000269|PubMed:21598943};
|
PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:21598943}.
| null | null |
FUNCTION: Involved in the biosynthesis of L-digitoxose, an unusual dideoxysugar attached to various pharmacologically active natural products, including the antitumor antibiotic tetrocarcin A, and the antibiotics kijanimicin and jadomycin B. Catalyzes the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,6-dideoxy-alpha-D-glucose. Also able to reduce dTDP-3-keto-6-deoxy-D-galactose and dTDP-3-keto-6-deoxy-D-glucose to yield dTDP-fucose and dTDP-quinovose, respectively. {ECO:0000269|PubMed:21598943}.
|
Actinomadura kijaniata
|
B3TP03
|
CTR2_CHICK
|
MLPCGPALTFVRCLVRKKNIKGEGLEDSLCRCLSTLDLIALGVGSTLGAGVYVLAGEVAKSDSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVAVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLGKQISHFFKTYFKMNYPGLAEYPDFFAVFLILLLSGLLSFGVKESAWVNKIFTAINILVLLFVMISGFVKGDVDNWRISEEYLINLSEIAENFSSYKNVTSIYGSGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVVSLLVCFMAYFGVSAALTLMMPYYLLDEKSPLPVAFAYVGWGPAKYVVAVGSLCALSTSLLGSMFPLPRIVFAMARDGLLFSFLAKVSKRQAPLLATLTAGVISAIMAFLFDLKALVDIMSIGTLLAYSLVATCVLILRYQPSLTYEQPKYSPEKATLAASKRESAVSESQINMIQESHFSLQTLINPSSLPTEQTATTVNCFVGLLAFLVCGLSALTTYGTHFIANLEPWSICLLATLVVSFIVTILLIQRQPQNQQKVAFMVPLLPFLPSLSILVNIYLMVQLSADTWIRFSIWMALGFIIYFTYGIRHSLEGRHSDGDGDSCSENSGLQEKNPVEEVDEPENANESDKFLARERTSEC
| null | null |
L-arginine import across plasma membrane [GO:0097638]; L-lysine import across plasma membrane [GO:0097639]; L-ornithine transmembrane transport [GO:1903352]
|
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
|
L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]
|
PF13520;PF13906;
|
1.20.1740.10;
|
Amino acid-polyamine-organocation (APC) superfamily, Cationic amino acid transporter (CAT) (TC 2.A.3.3) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18581}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18581}.
|
CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199, ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-homoarginine(in) = L-homoarginine(out); Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006; Evidence={ECO:0000250|UniProtKB:P52569};
| null | null | null | null |
FUNCTION: Low-affinity, high capacity permease involved in the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine). {ECO:0000250|UniProtKB:P18581, ECO:0000250|UniProtKB:P52569}.
|
Gallus gallus (Chicken)
|
B3VI55
|
LGK_LIPST
|
MPIATSTGDNVLDFTVLGLNSGTSMDGIDCALCHFYQKTPDAPMEFELLEYGEVPLAQPIKQRVMRMILEDTTSPSELSEVNVILGEHFADAVRQFAAERNVDLSTIDAIASHGQTIWLLSMPEEGQVKSALTMAEGAILASRTGITSITDFRISDQAAGRQGAPLIAFFDALLLHHPTKLRACQNIGGIANVCFIPPDVDGRRTDEYYDFDTGPGNVFIDAVVRHFTNGEQEYDKDGAMGKRGKVDQELVDDFLKMPYFQLDPPKTTGREVFRDTLAHDLIRRAEAKGLSPDDIVATTTRITAQAIVDHYRRYAPSQEIDEIFMCGGGAYNPNIVEFIQQSYPNTKIMMLDEAGVPAGAKEAITFAWQGMEALVGRSIPVPTRVETRQHYVLGKVSPGLNYRSVMKKGMAFGGDAQQLPWVSEMIVKKKGKVITNNWA
|
2.7.1.232
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26354439, ECO:0000269|PubMed:28196882}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:26354439, ECO:0000269|PubMed:28196882};
|
amino sugar metabolic process [GO:0006040]; peptidoglycan turnover [GO:0009254]; phosphorylation [GO:0016310]
| null |
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]
|
PF03702;
|
3.30.420.40;
|
Anhydro-N-acetylmuramic acid kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H2O + levoglucosan = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:63428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:30997, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.232; Evidence={ECO:0000269|PubMed:21719279, ECO:0000269|PubMed:26354439, ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63429; Evidence={ECO:0000269|PubMed:21719279, ECO:0000269|PubMed:26354439, ECO:0000269|Ref.1};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=105.3 mM for levoglucosan {ECO:0000269|PubMed:26354439, ECO:0000269|Ref.1}; KM=0.2 mM for ATP {ECO:0000269|Ref.1};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|Ref.1};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|Ref.1};
|
FUNCTION: Levoglucosan kinase that catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP (PubMed:21719279, PubMed:26354439, Ref.1). In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom (PubMed:21719279, PubMed:26354439, Ref.1). {ECO:0000269|PubMed:21719279, ECO:0000269|PubMed:26354439, ECO:0000269|Ref.1}.
|
Lipomyces starkeyi (Oleaginous yeast)
|
B3WFY8
|
DYF5_CAEEL
|
MSSAVKLADRYLMTKRLGDGTFGEVMLAKKIDTGDRVAIKRMKKKFYSWEEAMSLREVKSLKKLNHPNIIKLREVIRENDILYFVFEFMQENLYELMKDRDRYFPESVIRNIIYQVLQGLAFMHKNGFFHRDMKPENIMCNGTELVKIADFGLAREIRSKPPYTDYVSTRWYRAPEILLRSTSYNSPIDMWALGCIMAELYILRPLFPGTSEMDQLFKIISILGTPNKDEWPEGYQLASAMNFRFQQVVATPMEQVVNTISKEGMKLMMDMMLWNPEKRPNANQSLRYKYFQVAEKLGAPVVSQPAPGSIRKTSAASVKSDTKAMTAKAAKKDYIGSENVSPQQPAKVIDRHINRNLPLNKETLFEKSDNKPLGPTKSNEAKPTAKEIYLSKSKYVPGQVSKDTHQNQIMTTNGLTGTTKTTTFSAKKEGRTAVQTRFEYAYGYIPSFGARQTGPTVSNQTNNHSANNSHSPNKMSNTGRVDWAAKYVK
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9JKV2};
|
cilium assembly [GO:0060271]; intracellular signal transduction [GO:0035556]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; negative regulation of non-motile cilium assembly [GO:1902856]; non-motile cilium assembly [GO:1905515]; phosphorylation [GO:0016310]; positive regulation of non-motile cilium assembly [GO:1902857]; protein localization [GO:0008104]
|
axon [GO:0030424]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; nucleus [GO:0005634]; perikaryon [GO:0043204]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, RCK subfamily
| null |
SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17420466}. Cell projection, dendrite {ECO:0000269|PubMed:17420466}. Cell projection, axon {ECO:0000269|PubMed:17420466}. Cell projection, cilium {ECO:0000269|PubMed:17420466}. Note=Enriched at the transition zone between the base of the cilia and the dendrites and to a lesser extent in the cilia. {ECO:0000269|PubMed:17420466}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9JKV2}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9JKV2};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is required for ciliogenesis. Regulates the length and the morphology of sensory neuron cilia. In addition, plays a role in the anterograde intraflagellar transport (IFT) in the cilia by regulating the undocking of kinesin-II motor complex (composed of klp-11, klp-20 and kap-1) before reaching the distal segment and the docking of kinesin motor osm-3 onto IFT cargos. {ECO:0000269|PubMed:17420466}.
|
Caenorhabditis elegans
|
B3Y613
|
TLR2_PANTR
|
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFRFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLIVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNVDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS
| null | null |
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
|
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
|
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
|
PF00560;PF13855;PF01463;PF01582;
|
3.80.10.10;3.40.50.10140;
|
Toll-like receptor family
|
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}.
| null | null | null | null | null |
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
|
Pan troglodytes (Chimpanzee)
|
B3Y614
|
TLR2_PANPA
|
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYESKSLKSIQNVSHLILHMKQHILLLEIFVDVSSSVECLELRDTDLDTFRFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLIVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNVDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS
| null | null |
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
|
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
|
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
|
PF00560;PF13855;PF01463;PF01582;
|
3.80.10.10;3.40.50.10140;
|
Toll-like receptor family
|
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}.
| null | null | null | null | null |
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
|
Pan paniscus (Pygmy chimpanzee) (Bonobo)
|
B3Y615
|
TLR2_GORGO
|
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNVDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS
| null | null |
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; detection of diacyl bacterial lipopeptide [GO:0042496]; detection of triacyl bacterial lipopeptide [GO:0042495]; inflammatory response [GO:0006954]; positive regulation of cellular response to macrophage colony-stimulating factor stimulus [GO:1903974]; positive regulation of chemokine production [GO:0032722]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of matrix metallopeptidase secretion [GO:1904466]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of Wnt signaling pathway [GO:0030177]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]
|
cell surface [GO:0009986]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]; Toll-like receptor 1-Toll-like receptor 2 protein complex [GO:0035354]; Toll-like receptor 2-Toll-like receptor 6 protein complex [GO:0035355]
|
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; pattern recognition receptor activity [GO:0038187]; peptidoglycan binding [GO:0042834]; protein-containing complex binding [GO:0044877]; signaling receptor activity [GO:0038023]; Toll-like receptor binding [GO:0035325]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
|
PF00560;PF13855;PF01463;PF01582;
|
3.80.10.10;3.40.50.10140;
|
Toll-like receptor family
|
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}.
| null | null | null | null | null |
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
|
Gorilla gorilla gorilla (Western lowland gorilla)
|
B3Y618
|
TLR2_MACMU
|
MPHTLWMVWVLGVIISLSKEESSNQASLSCDHNGICKGSSGSLNSIPSVLTEAVKCLDLSNNRITYISNSDLQRYVNLQALVLTSNGINTIEEDSFSSLGRLEHLDLSYNYLSNLSSSWFKPLSSLKFLNLLGNPYKTLGETSLFSHLTKLRILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDLTSSVECLELRDTDLNTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLSQISGLLELEFDDCTLNGVGDFRGSDNDRVIDPGKVETLTIRRLHIPQFYSFNDLSTLYPLTERVKRITVENSKVFLVPCLLSRHLKSLEYLDLSENLMVEEYLKNSACEDAWPSLQTLILRQNHLASLGKIGETLLTLKNLTNLDISKNTFHYMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDISNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNTITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLVDWPANYLCDSPSHVRGQRVQDVRLSVSECHRAALVSGMCCALFLLILLMGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPNRDICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILVLLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEARQEGFWVNLRAAIKS
| null | null |
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
|
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
|
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
|
PF13855;PF01463;PF01582;
|
3.80.10.10;3.40.50.10140;
|
Toll-like receptor family
|
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}.
| null | null | null | null | null |
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
|
Macaca mulatta (Rhesus macaque)
|
B4EUF7
|
ENO_PROMH
|
MSKIVKVLGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVLKAVEAVNGPIAKALLGQDAKDQANIDKIMIDLDGTENKSNFGANAILAVSLANAKAAAAAKGMPLYEHISDLNGTHGQYSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAPTLKEAVRMGSEIFHHLAKVLKAKGMNTAVGDEGGYAPNLESNAAALAAIKEAVEAAGYVLGKDVTLAMDCAASEFYNNETGNYELKGEGKTFTSQEFTHYLEELTKQYLIVSIEDGLNESDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIDKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAIISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGSKAPFNGLKEVKGQA
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
|
glycolytic process [GO:0006096]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015]
|
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
|
PTM: Acetylated and 2-hydroxyisobutyrylated at Lys-326 and Lys-343, respectively, reducing the enolase activity (PubMed:31328167). Deacetylated and de-2-hydroxyisobutyrylated by NpdA/CobB, increasing the enolase activity (PubMed:31328167). {ECO:0000269|PubMed:31328167}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:31328167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000269|PubMed:31328167};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
| null | null |
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:31328167). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:31328167}.
|
Proteus mirabilis (strain HI4320)
|
B4EY22
|
CAIT_PROMH
|
MSKDNKKAGIEPKVFFPPLIIVGILCWLTVRDLDASNEVINAVFSYVTNVWGWAFEWYMVIMFGGWFWLVFGRYAKKRLGDEKPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISSPPFGMEGYSAPAKEIGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMEVIRPSSTLTPLVGEKHVNGLFGTVVDNFYLVALILAMGTSLGLATPLVTECIQYLFGIPHTLQLDAIIISCWILLNAICVAFGLQKGVKIASDVRTYLSFLMLGWVFIVGGASFIVNYFTDSVGTLLMYMPRMLFYTDPIGKGGFPQAWTVFYWAWWVIYAIQMSIFLARISKGRTVRELCLGMVSGLTAGTWLIWTILGGNTLQLIDQNILNIPQLIDQYGVPRAIIETWAALPLSTATMWGFFILCFIATVTLINACSYTLAMSTCRSMKEGAEPPLLVRIGWSVLVGIIGIILLALGGLKPIQTAIIAGGCPLFFVNIMVTLSFIKDAKVHWKDCSPYTQKMTH
| null | null |
4-(trimethylammonio)butanoate transport [GO:1900751]; carnitine metabolic process [GO:0009437]
|
plasma membrane [GO:0005886]
|
(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity [GO:0044667]
|
PF02028;
| null |
BCCT transporter (TC 2.A.15) family, CaiT subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}.
|
CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + 4-(trimethylamino)butanoate(in) = (R)-carnitine(in) + 4-(trimethylamino)butanoate(out); Xref=Rhea:RHEA:29427, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347; Evidence={ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for L-carnitine {ECO:0000269|PubMed:20829798}; KM=8.5 uM for L-carnitine {ECO:0000269|PubMed:24101465}; Vmax=4672 nmol/min/mg enzyme {ECO:0000269|PubMed:20829798}; Vmax=5172 nmol/min/mg enzyme {ECO:0000269|PubMed:24101465}; Note=kcat is 263 min(-1) with L-carnitine as substrate (PubMed:20829798). kcat is 4.9 sec(-1) with L-carnitine as substrate (PubMed:24101465). {ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465};
|
PATHWAY: Amine and polyamine metabolism; carnitine metabolism. {ECO:0000255|HAMAP-Rule:MF_01049}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:24101465};
| null |
FUNCTION: Catalyzes the exchange of L-carnitine for gamma-butyrobetaine. {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}.
|
Proteus mirabilis (strain HI4320)
|
B4EZY7
|
SIAT_PROMH
|
MQLHDFGFINYAVLFGYLAAMLLVGVYFSKRQKTADDYFRGGGRVPGWAAGVSVFATTLSSITFMSIPAKAYTSDWTFIIGQYLAIAILPLVFYFYIPFFRKLKITSAYEYLEARFDVRSRLFASLSFMLFHIGRVAIITYLTVLALRPFMGIDPVVLIVLISLLCIIYTWMGGIEGVIWTDVIQGLLLSGGAVLIFIMICFKVDGGISEIFTTTAQADKFFPTTQWRWSWTDSTIPVLMIGFLFANIQQFTASQDVVQRYIVTDSIKETKRTLITNAKLVAIIPIFFFAIGSALFVYYQQNPSLLPAGFNTGGILPLFIVTEMPIGIAGLIIAAIFAAAQSSISSSLNSISSCFNSDIYTRLSKSSPSPEQKMKVAKLVIIVAGIFSSLAAIWLVLSDEAEIWDAFNSLIGLMGGPMTGLFMLGIFVKRANAGSAVVGIIVSIIAVLAARYGSDLNFFFYGVIGSMSVVIAGTITAPLFAPAKQLSLDDSETSEN
| null | null |
sodium ion transport [GO:0006814]
|
extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
|
symporter activity [GO:0015293]
|
PF00474;
|
1.20.1730.10;
|
Sodium:solute symporter (SSF) (TC 2.A.21) family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:29717135}; Multi-pass membrane protein {ECO:0000269|PubMed:29717135}.
|
CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-neuraminate(out) + 2 Na(+)(out) = N-acetyl-alpha-neuraminate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:78535, ChEBI:CHEBI:29101, ChEBI:CHEBI:58770; Evidence={ECO:0000269|PubMed:29717135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78536; Evidence={ECO:0000269|PubMed:29717135};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for Neu5Ac {ECO:0000269|PubMed:29717135}; Vmax=187 nmol/min/mg enzyme {ECO:0000269|PubMed:29717135};
| null | null | null |
FUNCTION: Symporter that uses the Na(+) gradient as the driving force for the uptake of the sialic acid N-acetylneuraminic acid (Neu5Ac) (PubMed:29717135). It allows the use of host-derived Neu5Ac as an energy source by P.mirabilis (PubMed:29717135). Also binds N-glycolylneuraminic acid (Neu5Gc) and ketodeoxynonulosonic acid (KDN) (PubMed:29717135). Shows the highest affinity for Neu5Ac and Neu5Gc, which commonly occupy the terminal non-reducing position of mammalian cell surface glycoconjugates (PubMed:29717135). {ECO:0000269|PubMed:29717135}.
|
Proteus mirabilis (strain HI4320)
|
B4F6I3
|
FSP1_XENTR
|
MGSKVSVEESVRVVIVGGGFAGIAAATQLKSFGIPFVLVDLKDAFHHNVAALRASVESGFARKTFISYKDTFQDNFIQGKVVGINLQTQRVILESNEELQFSHLIIATGSNGPFPGKINNVISKDQAIQVYEDLVKEIQKAKHVVVVGGGSAGVEMAAEVKTDYPEKEVTLVHSKVALADVQLQPKVRRTVKEILLSKGVRLILAQKVTNLDQVTSNVAQENTVLQLDKNSEVVTCDLVLCCTGYKISSSSYSSAFGDKLAEDGALIVNDYLQVQGHANVYAVGDCAYINEPKMAYYAGIHARVAATNVRNSLIGKSLKTYKPGALSMLLSMGRNDGVGQFNGCYLGRFFVTMAKSRDIFVSKSWKEMGQTMPR
|
1.6.5.-
|
COFACTOR: Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; Note=Binds 6-hydroxy-FAD non-covalently. {ECO:0000250|UniProtKB:Q9BRQ8};
|
apoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]; vitamin K metabolic process [GO:0042373]
|
lipid droplet [GO:0005811]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]
|
PF07992;
|
3.50.50.100;
|
FAD-dependent oxidoreductase family
|
PTM: N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane. {ECO:0000250|UniProtKB:Q9BRQ8}.
|
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9BRQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BRQ8}. Nucleus {ECO:0000250|UniProtKB:Q9BRQ8}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + phylloquinone = NAD(+) + phylloquinol; Xref=Rhea:RHEA:74075, ChEBI:CHEBI:15378, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74076; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menaquinone-4 + NADH = menaquinol-4 + NAD(+); Xref=Rhea:RHEA:74079, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78277, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74080; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADH = menadiol + NAD(+); Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378, ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696; Evidence={ECO:0000250|UniProtKB:Q9BRQ8};
| null | null | null | null |
FUNCTION: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death. {ECO:0000250|UniProtKB:Q9BRQ8}.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
B4F6I5
|
FICD_XENTR
|
MAVTECEWASLGSRIGLRAALVLLSGSLLVVLFPLSGLEHQYRTALNILLQCNLWGGDDRHTFTGQTRGLAVASTAIELLVLKQKPTSDVKFEAKAALNQALEMKRQGKKEKAHKLLHHALKMDPDHVDALNELGILLEEEKDIIQADYLYSKALTISPHNEKALINRDRTLPLVEEIDQRYFSLIDSKVKKLMSIPKGNPALRRVMEESYYHHIYHTVAIEGNTLSLSEIRHIIETRYAVPGKSLEEQNEVIGMHAAMKYVNATLVSRIGSVTIDNILEIHRRILGYVDPVEAGRFRRNQVFVGHHIPPHPRDVEKLMQEFVQWLNSEEAMSLHPVEFAALAHYKLVYIHPFVDGNGRTSRLLMNLILMQAGYPPITVRKEQRSEYYHVLEIANEGDVRPFIRFIAKCTESTLDLLLIATAEHPVGLPEPNHGFSECKQTITIKT
|
2.7.7.108; 3.1.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6};
|
protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]
|
endoplasmic reticulum membrane [GO:0005789]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:A0A061I403}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-222 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (By similarity). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q9BVA6}.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
B4F6N6
|
LOXL2_XENTR
|
MLVTHIFLLTLSLSVPTLGQYEHWLYYPEYQASQAPEPLPTPARNVPQIHVRLAGEKRKHNEGRVEVYYEGEWGTVCDDDFSMYAAHIVCRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDCKHSEDVGVQCSDRRIPGFKVSNELPGQLEGLNIQVEEVRIRAILSAYRKRVPVTEGFVEVKVQGSWRQVCNAEWSSKNSRVVCGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTCSDGSPAVVSCTPGRAFAPSPGTGFGKAFRQEQPLVRLRGGANTGEGRVEVLKNGEWGTICDDKWNLVTASVVCRELGFGSAKEALAGAQMGQGMGHIHMSEIQCNGFEKSLIDCKFNVHSQGCNHEEDAAVRCNVPAMGFENQVRLSGGRHPTEGRVEVLMERNGTLRWGTVCSDTWGTMEAMIVCRQLGLGFASHAFQETWYWQGDINADDVVMSGVKCSGTEMSLAHCRHDGANINCPRGGGRFAAGVSCVETAPDLVLNAALVEQTTYLEDRPMFMLQCAHEEQCLSSSADRTSPTTGYRRLLRFSSQIHNNGQADFRPKTGRHSWIWHDCHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDSECETDVQKQYACANFGEQGITVGCWDVYRHDIDCQWVDITDVAPGDYFFQVIINPNQEVAESDYTNNIMKCRCRYDGHRIWMYNCHIGGSYSTETEEKFEHFSGLMNNQLSTR
|
1.4.3.13
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0};
|
collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein modification process [GO:0036211]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]
|
basement membrane [GO:0005604]; chromatin [GO:0000785]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720]
|
PF01186;PF00530;
|
3.10.250.10;
|
Lysyl oxidase family
|
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0};
| null | null | null | null |
FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency. Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0}.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
B4F753
|
ABD12_XENTR
|
MRKRAEPVPPEHESFGRAPLDRECSIKQKLRIPGTKGHYPHDSDCDSKGMKRFGRRYGLWSRLRMFLIFLLGLYIAIPFLVKICPAIQTQLVFLNLVRFPYFIDLKRPEDQGLNHTCNFYLQPEEDVSIGVWHTVPAVLWKDAQGKDLEWYEEVLSTSYPVILYLHGNAGTRGGDHRVQLYKVLSSMGYHVISFDYRGWGDSVGSPSESGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDSLILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITASGIKFANDDNVKYISCPLLILHAEDDPVIPFHLGKKLYNIAAPARSLRDYKVQFVPFHKDLGYRHKYIYRSPELRQILRDFLGNTEQQ
|
3.1.-.-; 3.1.1.23
| null |
acylglycerol catabolic process [GO:0046464]; monoacylglycerol catabolic process [GO:0052651]; phosphatidylserine catabolic process [GO:0006660]; phospholipid catabolic process [GO:0009395]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
acylglycerol lipase activity [GO:0047372]; lysophospholipase activity [GO:0004622]; phospholipase activity [GO:0004620]
|
PF00561;
|
3.40.50.1820;
|
Serine esterase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717, ChEBI:CHEBI:72828; Evidence={ECO:0000250|UniProtKB:Q99LR1}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo-inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762; Evidence={ECO:0000250|UniProtKB:Q99LR1}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:Q99LR1}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q99LR1}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) + hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64765, ChEBI:CHEBI:75020; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:69081; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629, ChEBI:CHEBI:75555; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, ChEBI:CHEBI:85195, ChEBI:CHEBI:143087; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, ChEBI:CHEBI:143088, ChEBI:CHEBI:143089; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020, ChEBI:CHEBI:143089, ChEBI:CHEBI:143094; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
| null | null | null | null |
FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity). {ECO:0000250|UniProtKB:Q8N2K0, ECO:0000250|UniProtKB:Q99LR1}.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
B4F769
|
SMAL1_RAT
|
MSLPLTEEQRKKIEENRQKALARRAEKLWAEQPQSTASGSSAARPSQCKQNSLLNLPAEPSKPEGHATISKGQNLNNSLPAAQRPHSSPCFQPSTAEEAKGLWKSEGKMSAACPNPSPPEVSNQQLLGSKSSEGHPQATQDTAASCPRPFPRDPKLEAKAGRPSTSGQSISDTFYALGEKTPKTDGRPAKALQTSPQKASCLRGMCLRTGDRFRVKIGYNKELIEVFKSLPSRRYDSFTKTWDFSMSDYRALMKAVERLSTVSLQPLEEVDGTGGQTSLPSAPSLTFVTGRCMLISRARFEVDIGYSEVVIALFKQMESRNYDPKTRKWNFLLEEHNKLIARSRELKQVQLDPLPKTLTLAFASQLEKTSLQSKADVPEADLSGVDAKLVSNLMPFQREGVSFAISKRGRLLLADDMGLGKTIQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPEDINVVVTGKGRLTAGLVNIVSFDLLSKLEKQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKRLPWGWDYSGSSNLGELKLLLEEAVMLRRLKSDVLSQLPAKQRKMVVVNPGRISTRAKAALDAAAKEMTKDKTKQQQKEALLVFFNRTAEAKIPCVIEYILDLLESGREKFLVFAHHKVLLDAIAKELERKNVQHIRIDGSTPSADREDLCQQFQLSKGHTVAVLSITAANMGLTFSSADLVVFAELFWNPGVLIQAEDRVHRIGQTNSVGIHYLVAKGTADDYLWPLIQEKIKVLGEAGLSETNFSEMTEATDYLYKDPKQKTIYSLFQQSFEDDGNDMEFLEAAESFELGSTSGTSGNSSQELGDITDENALADSPPKKRRFEFFDNWDSFTSPF
|
3.6.4.-
| null |
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; regulation of transcription by RNA polymerase II [GO:0006357]; replication fork processing [GO:0031297]
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DNA replication factor A complex [GO:0005662]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
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ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; ATP-dependent DNA/DNA annealing activity [GO:0036310]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]
|
PF07443;PF00271;PF00176;
|
3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family, SMARCAL1 subfamily
|
PTM: DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC. {ECO:0000250}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to damaged DNA regions. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks (By similarity). {ECO:0000250}.
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Rattus norvegicus (Rat)
|
B4F779
|
DP13B_RAT
|
MPAVDKLLLEEALQDSPQTRSLLSVFEEDAGTLTDYTNQLLQAMQRVYGAQNEMCLATQQLSRQLLAYEKQNFALGKGDEEVISTLHYFSKVMDELNGLHSELAKQLADTMVLPVIQFREKDLTEVSTLKDLFGLASNEHDLSMAKYSRLPKRKENERVKTDVAKEVAAARRKQHLSSLQYYCALNALQYRKRAAMMEPLIGFAHGQINFFKKGAEMFSKSMDGFLSSVTDMVQSIQVELEAEADKMRVSQQELLSVSESVYTPDIDVATPQINRNLIQKTGYLNLRNKTGLVTTTWERLYFFTQGGNLMCQPRGAVAGGLIQDLDNCSVMAVDCEDRRYCFQISTPSGKPGIILQAESRKEYEEWICAINNISRQIYLTDNPEAVAIKLNQTALQAVTPITSFGKKQESFYFSQNIKNSDTGYVKIVPKAAASIPETEELIAPGTPIQFDIVLPATEFLDQNRGSRRINPFGETEDDSFPDAEDSLLQQMFIVRFLGSMAVKTDSTTEVIYEAMRQVLAARAIHNIFRTTESHLMVTSQTLRLIDPQTQVSRACFELTSVTQFAAHQENKRLVGFVIRVPESTGEESLSTYIFESNSEGEKICYAINLGKEIIEVQKDPEALARLMLSVPLTNDGKYVLLNDQADDTGGSPSDHRGAESEA
| null | null |
adiponectin-activated signaling pathway [GO:0033211]; cell cycle [GO:0007049]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cold acclimation [GO:0009631]; diet induced thermogenesis [GO:0002024]; glucose homeostasis [GO:0042593]; negative regulation of cellular response to insulin stimulus [GO:1900077]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of glucose import [GO:0046325]; negative regulation of neural precursor cell proliferation [GO:2000178]; negative regulation of neurogenesis [GO:0050768]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis [GO:1905451]; positive regulation of macropinocytosis [GO:1905303]; positive regulation of phagocytosis, engulfment [GO:0060100]; protein homotetramerization [GO:0051289]; protein import into nucleus [GO:0006606]; regulation of fibroblast migration [GO:0010762]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of innate immune response [GO:0045088]; regulation of toll-like receptor 4 signaling pathway [GO:0034143]; signaling [GO:0023052]; transforming growth factor beta receptor signaling pathway [GO:0007179]
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cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; early phagosome membrane [GO:0036186]; endosome [GO:0005768]; endosome membrane [GO:0010008]; macropinosome [GO:0044354]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; vesicle [GO:0031982]
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identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF16746;PF00169;PF00640;
|
1.20.1270.60;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q8NEU8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NEU8}. Nucleus {ECO:0000250|UniProtKB:Q8NEU8}. Cell membrane {ECO:0000250|UniProtKB:Q8NEU8}. Endosome membrane {ECO:0000250|UniProtKB:Q8NEU8}. Cytoplasm {ECO:0000250|UniProtKB:Q8K3G9}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q8K3G9}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q8K3G9}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8K3G9}. Cell membrane {ECO:0000250|UniProtKB:Q8K3G9}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q8K3G9}. Note=Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF. Associates dynamically with cytoplasmic membrane structures that undergo changes in shape, movement, fusion and fission events. PI(4,5)P2 levels are important for membrane association of APPL2 (By similarity). Absent of endosome in macrophage. Colocalized with RAB31 at early-stage phagosome. Localized on macropinosomes in LPS-activated macrophages. Associated with membrane domains in contact with pathogens and pathogen-derived ligands like LPS. First recruited to the ruffles, and accumulates on macropinosomes (By similarity). {ECO:0000250|UniProtKB:Q8K3G9, ECO:0000250|UniProtKB:Q8NEU8}.
| null | null | null | null | null |
FUNCTION: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism. Regulates signaling pathway leading to cell proliferation through interaction with RAB5A and subunits of the NuRD/MeCP1 complex (By similarity). Plays a role in immune response by modulating phagocytosis, inflammatory and innate immune responses. In macrophages, enhances Fc-gamma receptor-mediated phagocytosis through interaction with RAB31 leading to activation of PI3K/Akt signaling. In response to LPS, modulates inflammatory responses by playing a key role on the regulation of TLR4 signaling and in the nuclear translocation of RELA/NF-kappa-B p65 and the secretion of pro- and anti-inflammatory cytokines. Also functions as a negative regulator of innate immune response via inhibition of AKT1 signaling pathway by forming a complex with APPL1 and PIK3R1 (By similarity). Plays a role in endosomal trafficking of TGFBR1 from the endosomes to the nucleus (By similarity). Plays a role in cell metabolism by regulating adiponecting ans insulin signaling pathways and adaptative thermogenesis (By similarity). In muscle, negatively regulates adiponectin-simulated glucose uptake and fatty acid oyidation by inhibiting adiponectin signaling pathway through APPL1 sequestration thereby antagonizing APPL1 action (By similarity). In muscles, negatively regulates insulin-induced plasma membrane recruitment of GLUT4 and glucose uptake through interaction with TBC1D1 (By similarity). Plays a role in cold and diet-induced adaptive thermogenesis by activating ventromedial hypothalamus (VMH) neurons throught AMPK inhibition which enhances sympathetic outflow to subcutaneous white adipose tissue (sWAT), sWAT beiging and cold tolerance (By similarity). Also plays a role in other signaling pathways namely Wnt/beta-catenin, HGF and glucocorticoid receptor signaling (By similarity). Positive regulator of beta-catenin/TCF-dependent transcription through direct interaction with RUVBL2/reptin resulting in the relief of RUVBL2-mediated repression of beta-catenin/TCF target genes by modulating the interactions within the beta-catenin-reptin-HDAC complex (By similarity). May affect adult neurogenesis in hippocampus and olfactory system via regulating the sensitivity of glucocorticoid receptor. Required for fibroblast migration through HGF cell signaling (By similarity). {ECO:0000250|UniProtKB:Q8K3G9, ECO:0000250|UniProtKB:Q8NEU8}.
|
Rattus norvegicus (Rat)
|
B4F795
|
CTL2_RAT
|
MGKDSQHYYGKHGTPQKYDPTFKGPIYNRGCTDIICCVLLFLAIVGYVAVGIIAWTHGDPRKVIYPTDSRGEFCGQKGTKNADKPFLFYFNIVKCASPLVLLEFHCPTPQICVKQCPDRYLTFLSARNSRDFDYYKQFCVPGFKNNKGVAEVLRDGECPAVIIPSKPLAQRCFPAIHASKGVLMVGNETTYEDGHGTRKNVTDLVEGAKKANKVLEARQLAMQIFEDYTVSWYWIVIGLVIAMLLSLMFIVLLRFLAGVMVWVMIVMVILVLGYGIFHCYAEYSRLRGEAGSDVSLVDLGFQTDLRVYLHLRQTWMAFMIILSILEVVIILLLIFLRKRILIAIALIKEASRAVGHVMCSMLYPLVTFFLLCLCIAYWASTSVFLSTSNVAVYKIVDDTPCPLLGKTCNPETFPLNESRQCPNGRCQFAFYGGESTYHRALLGLQIFNAFMFFWLANFVLALGQVTLAGAFASYYWAMRKPDDMPAFPLFSAFGRALRYHTGSLAFGSLILAIVQIIRVMLEYLDQRLKAAQNKFAKFLMVCLKCCFWCLEKFIKFLNRNAYIMIAIYGTNFCTSARNAFFLLMRNIIRVAVLDKVTDFLFLLGKLLIVGSVGILAFFFFTHRIRIVQDTAPPLNYYWVPILTVIIGSYLIAHGFFSVYGMCVDTLFLCFLEDLERNDGSAERPYFMSSTLKKLLNKTNKKVAES
| null | null |
choline transport [GO:0015871]; ethanolamine transport [GO:0034229]; transmembrane transport [GO:0055085]
|
membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
antiporter activity [GO:0015297]; choline transmembrane transporter activity [GO:0015220]; ethanolamine transmembrane transporter activity [GO:0034228]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; salt transmembrane transporter activity [GO:1901702]; transmembrane transporter activity [GO:0022857]
|
PF04515;
| null |
CTL (choline transporter-like) family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19236841}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:19236841}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly expressed in mitochondria. {ECO:0000269|PubMed:19236841}.
|
CATALYTIC ACTIVITY: Reaction=choline(out) + n H(+)(in) = choline(in) + n H(+)(out); Xref=Rhea:RHEA:75463, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:19236841}; CATALYTIC ACTIVITY: Reaction=ethanolamine(out) + n H(+)(in) = ethanolamine(in) + n H(+)(out); Xref=Rhea:RHEA:75467, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603; Evidence={ECO:0000250|UniProtKB:Q8IWA5};
| null | null | null | null |
FUNCTION: Exhibits choline transporter activity, as choline/H+ antiporter (PubMed:19236841). Also acts as a low-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy pathway (By similarity). {ECO:0000250|UniProtKB:Q8IWA5, ECO:0000269|PubMed:19236841}.
|
Rattus norvegicus (Rat)
|
B4F7B7
|
DUS15_RAT
|
MGNGMTKVLPGLYLGNFIDAKDPDQLGRNKITHIVSIHESPQPLLQDITYLRISVSDTPEVPIKKHFKECVHFIHSCRLNGGNCLVHCFAGISRSTTVVIAYVMTVTGLGWQEVLEAIKASRPIANPNPGFRQQLEEFGWANSQKLRRQLEERFGEIPFRDEEDLRALLPLCRRCRQGPGTSAPSATTASSAASEGTLQRLVPRSPRESHRPLPLLARVKQTFFCLPRCLSRKGGK
|
3.1.3.16; 3.1.3.48
| null |
dephosphorylation [GO:0016311]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of oligodendrocyte differentiation [GO:0048713]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
|
PF00782;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H1R2}; Lipid-anchor; Cytoplasmic side.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q9H1R2, ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: May play a role in the regulation of oligodendrocyte differentiation. May play a role in the regulation of myelin formation (PubMed:27532821). Involved in the regulation of Erk1/2 phosphorylation in Schwann cells; the signaling may be linked to the regulation of myelination (PubMed:27891578). May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6 (By similarity). {ECO:0000250|UniProtKB:Q9H1R2, ECO:0000269|PubMed:27532821, ECO:0000269|PubMed:27891578}.
|
Rattus norvegicus (Rat)
|
B4F7C5
|
LRRT4_RAT
|
MGFRLITQLKGMSVLLVLFPTLLLVMLTGAQRACPKNCRCDGKIVYCESHAFADIPENISGGSQGLSLRFNSIQKLKSNQFAGLNQLIWLYLDHNYISSVDEDAFQGIRRLKELILSSNKITYLHNKTFHPVPNLRNLDLSYNKLQTLQSEQFKGLRKLIILHLRSNSLKTVPIRVFQDCRNLDFLDLGYNRLRSLSRNAFAGLLKLKELHLEHNQFSKINFAHFPRLFNLRSIYLQWNRIRSVSQGLTWTWSSLHTLDLSGNDIQAIEPGTFKCLPNLQKLNLDSNKLTNVSQETVNAWISLISITLSGNMWECSRSICPLFYWLKNFKGNKESTMICAGPKHIQGEKVSDAVETYNICSDVQVVNTERSHLAPQTPQKPPFFPKPTIFKSDAIPATLEAVSPSPGFQIPGTDHEYEHVSFHKIIAGSVALFLSVAMILLVIYVSWKRYPASMKQLQQHSLMKRRRKKARESERQMNSPLQEYYVDYKPTNSETMDISVNGSGPCTYTISGSRECEMPHHVKPLPYYSYDQPVIGYCQAHQPLHINKAYEAVSIEQDDSPSLELGRDHSFIATIARSAAPAIYLERITN
| null | null |
AMPA glutamate receptor clustering [GO:0097113]; neurotransmitter-gated ion channel clustering [GO:0072578]; positive regulation of synapse assembly [GO:0051965]; regulation of presynaptic membrane organization [GO:1901629]; regulation of synapse assembly [GO:0051963]; synapse organization [GO:0050808]
|
AMPA glutamate receptor complex [GO:0032281]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; photoreceptor ribbon synapse [GO:0098684]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
heparan sulfate proteoglycan binding [GO:0043395]
|
PF13855;
|
3.80.10.10;
|
LRRTM family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in the development and maintenance of the nervous system (By similarity). Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation. {ECO:0000250, ECO:0000269|PubMed:19285470}.
|
Rattus norvegicus (Rat)
|
B4F7E7
|
PALS1_RAT
|
MTTSYMNGHVTEESDSGIKNLGLASPEEHPKHREMAVDCPGDLGTRLMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVKILEVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNRDFQNAFKIHNAVTVHMNKASPPFPLIANVQDLVQEVQTVLKPVHQKEGQELTALLNAPHIQALLLAHDKVAEQEMQLEPITDERVYESIGHYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRNRRDHEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRAQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR
| null | null |
central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; establishment or maintenance of polarity of embryonic epithelium [GO:0016332]; gene expression [GO:0010467]; generation of neurons [GO:0048699]; morphogenesis of an epithelial sheet [GO:0002011]; myelin assembly [GO:0032288]; peripheral nervous system myelin maintenance [GO:0032287]; phosphorylation [GO:0016310]; plasma membrane organization [GO:0007009]; protein localization [GO:0008104]; protein localization to myelin sheath abaxonal region [GO:0035750]; protein localization to plasma membrane [GO:0072659]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]
|
adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; bicellular tight junction [GO:0005923]; Golgi apparatus [GO:0005794]; lateral loop [GO:0043219]; myelin sheath adaxonal region [GO:0035749]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; Schmidt-Lanterman incisure [GO:0043220]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; protein domain specific binding [GO:0019904]
|
PF00625;PF02828;PF09060;PF00595;PF07653;
|
2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40;
|
MAGUK family
| null |
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}. Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8N3R9}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8N3R9}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JLB2}. Perikaryon {ECO:0000250|UniProtKB:Q9JLB2}. Apical cell membrane {ECO:0000250|UniProtKB:Q8N3R9}. Note=Localized to the tight junctions of epithelial cells (By similarity). Localized to the Golgi apparatus in T lymphocytes (By similarity). Localized to a subset of intracellular vesicles (By similarity). Localized to the Purkinje cell body and axon (By similarity). Localized to intercellular junctions in vascular endothelial cells (By similarity). Localized to Schmidt-Lanterman incisures, the adaxonal domain, and the inner part of paranodal loops in myelinating Schwann cells of the sciatic nerve (By similarity). Localized to apical membrane domains of the outer limiting membrane (OLM) junctions in the retina (By similarity). Colocalizes with CRB1 at the OLM, apical to the adherens junction (By similarity). Colocalizes with MPP1 in the retina at the OLM (By similarity). Colocalizes with MPP3 to the subapical region of adherens junctions in the retina OLM (By similarity). {ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2}.
| null | null | null | null | null |
FUNCTION: Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (By similarity). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface (By similarity). Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (By similarity). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing premature differentiation, and is required for cerebellar histogenesis, fissure formation, cerebellar layer organization and cortical development (By similarity). Plays a role in neuronal progenitor cell survival, potentially via promotion of mTOR signaling (By similarity). Plays a role in the radial and longitudinal extension of the myelin sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter (By similarity). May play a role in the T-cell receptor-mediated activation of NF-kappa-B (By similarity). Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). Required for the normal polarized localization of the vesicular marker STX4 (By similarity). Required for the correct trafficking of the myelin proteins PMP22 and MAG (PubMed:20237282). Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity). {ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:20237282}.
|
Rattus norvegicus (Rat)
|
B4FK49
|
NDK1_MAIZE
|
MESTFIMIKPDGVQRGLIGEIISRFEKKGFYLKALKLVNVERSFAEKHYADLASKPFFQGLVDYIISGPVVAMVWEGKSVVTTGRKIIGATNPLASEPGTIRGDFAVDIGRNVIHGSDSIESANKEIALWFPEGPADWQSSQHPWIYEK
|
2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P22392};
|
CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]; protein hexamerization [GO:0034214]; UTP biosynthetic process [GO:0006228]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; nucleoside diphosphate kinase activity [GO:0004550]
|
PF00334;
|
3.30.70.141;
|
NDK family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|RuleBase:RU004013, ECO:0000269|PubMed:25679041}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|RuleBase:RU004013, ECO:0000269|PubMed:25679041};
| null | null | null | null |
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Involved in transcription regulation (Probable). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds folded G4 with low nanomolar affinity and corresponding unfolded G-rich DNA more weakly. Stabilizes folded G4s regardless of whether they are prefolded or not (PubMed:25679041). {ECO:0000250|UniProtKB:P36010, ECO:0000269|PubMed:25679041, ECO:0000305}.
|
Zea mays (Maize)
|
B4FZ81
|
PTA12_MAIZE
|
MASCYNPWRLFPGMSTAVPAGPVTAPAHSRTCKSSKVFSALPHRRGLLFLGTRRARIKCVKDDSLHFDPSKIEPPPYSSYFDSTSGQLEPASGARASIPGKEYWPEGTAARVRAARAPAPVGESAGMPSFGTKPGSRRRGYKEQVTSASGTEGAQTDDRKDGDEPDVAIIGSGDDALEEIKDSVDEYVIYETPEEEELSEYDMDKMMGRPHPFIDPAKAMSLGEPKTSEELWWHWRRKSQEEEMWSRWQRRRPDVDTVFAKAMAETGQIKIFGDHPSRTEAALAKTRRHLYKEERLEAEQRRLEEIGPIAYYSEWVEAYKNKDTSREAIQKHFEETGEDENVQLIKMFQHQTAGEYRIMMGTDVRIQRDPLAMRMREDQIKQIWGGDPVYPTINYVQDPDEVIDYRGPEFHEPTPEVVPYLMEHGIMITKEELYARLNEEREDVNQDITYIPEAKDPMATAIDIGEHSYNEDSDDEDEDVDKAAAQPQSLEDEEDDRDDVAEVEEKVNQNWSALKSTGQAEKPKEKSKKDEMTLKEAIDDSENLTDFLMDFEETE
| null | null |
plastid transcription [GO:0042793]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of red or far-red light signaling pathway [GO:0090228]; positive regulation of thermomorphogenesis [GO:0140922]; protein catabolic process [GO:0030163]; regulation of gene expression [GO:0010468]; regulation of plant organ morphogenesis [GO:1905421]; regulation of transcription by RNA polymerase II [GO:0006357]; response to blue light [GO:0009637]; response to cytokinin [GO:0009735]; response to far red light [GO:0010218]; response to red light [GO:0010114]; response to temperature stimulus [GO:0009266]; UV protection [GO:0009650]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; nucleus [GO:0005634]; plastid-encoded plastid RNA polymerase complex [GO:0000427]
|
single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; transcription regulator activator activity [GO:0140537]
| null | null | null | null |
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:25599833}. Nucleus {ECO:0000269|PubMed:25599833}.
| null | null | null | null | null |
FUNCTION: Required for the activity of the plastid-encoded RNA polymerase (PEP) and full expression of genes transcribed by PEP (PubMed:24246379, PubMed:25599833). Required for the proper build-up and formation of the PEP-complex. Binds single-stranded (ss) DNA and RNA, but not double-stranded (ds) DNA (PubMed:25599833). {ECO:0000269|PubMed:24246379, ECO:0000269|PubMed:25599833}.
|
Zea mays (Maize)
|
B4G2I8
|
HH_DROPE
|
MDNHNEVPMSMSAPWASAARVTCLSLDAKCHRPCPSSISASASASGCASDSAAIATTKLRHIAYTQRCSSRLTMLMTVLLLLLPLSFTPAHSCGPGRGLGRRRERNLYPLVLKQTIPNLSEYQSGASGPLEGEIKRDSPKFKDLVPNYNRDILFRDEEGTGADRLMTKRCKEKLNVLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDREPSRYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGITKPLSEIAIGDRVLSMGSNGQPVYSEVILFMDRNLEQMQNFVELHTDGGAVLTVTPAHLISVWHPERQQLDYVFADRVEELNYVLVRDPQTGELRPQRVVRVGSVRSKGVVAPLTREGTIVVNSVAASCYAVIDSQSLAHWGLAPMRILAMLQSWMPAKDQLRSSQTEGVVSRAEQQNGIHWYANALYKVKDYVLPKSWRHD
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila persimilis (Fruit fly)
|
B4G437
|
SPAST_DROPE
|
MVRTKNQSSSSSASSSSHKSPIKSHGGSGSAAAGTAGHPVSRSSSSHRTSIDDRKSATNVSSSSNRRTTPGSSPDGDGDDDTTTTDDLTPTSTSAPRSAGGPSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNNSNNKDQKHQQLTSSQSLNYPLEVTSGEAASEQQVQQPLPQQRYRALQPLEMAGANRSGSGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDFQMHRLSLKEKQKANESREQQQKPQKAREAADKPMLTNLTNDPAKLKTRSSGYGPKNGLTTPRIFATATTPTSSSSLASGRKLTIGTKRPGNLAVAANKSQTLPRNLGSKTSVGAVRQPGKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGASGSGSGASTPVVTVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHLQPSIIFIDEVDSLLSERSSGEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTDALRRLSKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDINAMRHITEKDFHNSLKRIRRSVAPQSLSLYEKWSSDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila persimilis (Fruit fly)
|
B4GAJ1
|
LIS1_DROPE
|
MKMVLSQRQREELNQAIADYLGSNGYGDSLETFRKEADVSTESEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDSQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLMNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLNGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila persimilis (Fruit fly)
|
B4GBH0
|
PTK7_DROPE
|
MDMDVMMISMCILASTLMAPGWASTSGFLRVPQSQSIVENEAADFGCEATDPASYLHYEWLHNGREISYDKRVYRIGSHLHIEAVQREEDVGDYVCIATSLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDEPLQIEWYRDSARLASWGNVHLEEHRLLVRQPSPSDDGLYRCTASNAAGRVMSKQGYVYQANIKCLPRLLKKNQKLPESWGKQTFLCRGKRGGSGGLDQALSPAPEDLRIVQGPAGQLLIKEGDSAALSCLYELPAELQNQRIQLRWRKDGKLLRHVELGGAIPIPGHAHDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEGHAPLNSSPGLLEVIEQLKFVPQPTSKNLELDAAVAKVHCKAQGTPSPQVQWLREGSLNSSLPDQVEVDINGTLIFRNVRAEHRGNYTCQARSSQGQISATVSINVVVTPKFSVPPVGPIETTEQGTVVMHCQAIGDPKPTIQWDKDLKYLSENNTDRERFSFLENGTLEIRNVQVEDEGSYGCTIGNSAGLKREDVQLVVRSTGDGFAPEETGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNELSIKEAGGDQPDASVTNGKGSEQEPCLSKQRNGASGKPKSKSNGDAQKSDDTACSQQSRSSKKSVYEQLVLPRSGLSELLQIGRGEFGDVFVGKLKASLVAASAQSDKDADTEKQHSNSENGSGGSGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEPEQSALEQLVLVKALNKVKDEQACQEFRRQLDLLRGISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATATSSPPALTTSQVLAVAYQIARGMDAIYRSRCTHRDLATRNCVISSEFVVKVSYPALCKDKYSREYHKHRNTLLPVRWLAPECIQEDEYTTKSDIFAYGVLVWELFNQATKLPHEELTSEQVIQRSQAGTLEWTVAEATPDSLKEILLSCWLANPKERPSFSQLGSALSKAMQSVAEK
| null | null |
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila persimilis (Fruit fly)
|
B4GFJ8
|
RAS1_DROPE
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLTTWNVKNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKLNKPNRRFKCKIL
|
3.6.5.2
| null |
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}.
|
Drosophila persimilis (Fruit fly)
|
B4GJC1
|
FICD_DROPE
|
MAMTILHASEKVNAEAEATTCPPTEKVKEEQQQQEQLQHSKTSKRVQFYRFALFFIAGSFAAFSFHALTSSSSWRLRQLHHLPNAHYLQTREEFAVYSVEELNAFKEFYDKSISDSVGASYSEAEQTNIKEALGALRLAQDMHLSGKDDKASRLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALTLCPSNSEALANRQRTAEVVQTLDERRLQSLDSKRDALSAIHESSSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHVPPGPGDLALLMQRFERWLNSEHSSSLHPVNYAAYAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGEQLAQMRSPHISAQSASIPEFYEFSGSGFQP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-261 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila persimilis (Fruit fly)
|
B4GZN1
|
WLS_DROPE
|
MSGTILENLSGRKLSILVGSLLLCQVLCFLLGGLYAPVPAGHTNVLGSLCRENHARQNDTSFFLYSRGEGSCTQVTREEVEQDSMKLANQIVHVFQMPLPRDSRVLDYSRWQQNLIGVLQVEFGYDSSSELREPPKELQLTIDMRLAYRNKGDPDHAWKLYAHGVEHRYLDCVAAHIGSSETLYTCDMIPLFELGALHHSFYLLNLRFPLDTPKQMNLQFGHMHDLTLTAIHQNGGFTHVWLMLKTLLFPFVVGIMVWFWRRVHLLQRSPALLEYMLLYLGGALTFLNLPLEYLSLTIEMPYMLLLSDIRQGIFYAMLLSFWLVFAGEHMLIQDSHNKSTIRSRYWKHLSAVVVGCISLFVFDISERGVQLRNPFYSIWTTPLGAKVAMSFILLAGVSAAVYFLFLCYMISKVFKNIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAALTVTGFIMGQMAEGQWKWNDDVEIQLTSAFLTGVYGMWNIYIFALLILYAPSHKQWPTMHHSDETTQSNENIVASAASEEIEFSNLPSDSNPSEISSLTSFTRKVAFE
| null | null |
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; positive regulation of Wnt protein secretion [GO:0061357]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of intracellular protein transport [GO:0033157]; segment polarity determination [GO:0007367]; trans-synaptic signaling via exosome [GO:0099157]; Wnt protein secretion [GO:0061355]; Wnt signaling pathway [GO:0016055]
|
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
Wnt-protein binding [GO:0017147]
|
PF06664;
| null |
Wntless family
| null |
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). {ECO:0000250}.
|
Drosophila persimilis (Fruit fly)
|
B4H3U8
|
SWS_DROPE
|
MDVLELLRVSGSNMYYSTFLADAWCYYISNQITMTMYLYCALGVLSMLFIGWFVYFKRLARLRLRHEIARSLSAVTMASGGDLRGPRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVIRFARRILQLRRENMPLEVRTVEPPAEYLEETMEGSDRVPPDALYMLQSIRIFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRFKGSSQGAGPSVYCSQTTRQATGSASATATAAAASGTAGSTHTAVPRPASSLSRYSQDEQHTLSDPNPGIPNLELSGDSVNTLFGEVNGGARLNSYPPLYHQRESDGNLSTRRGSITQQEQPEVGPVPSIDMRLVKSSAVDSLRKELGLPEQDAHIIDPFVEVREMEPNVTLITEGNADDVCVWFVMTGTLAVYQGNADATRIKQDKTDLLIHYVHPGEIVGGLAMLTGEASAYTIRSRNHSRVAFIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRALYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGSMQTRTTTGAPGAPVEANPVTHKYSTVALVPITDDVPLTPFTYELYHSLCAIGPVLRLTSDLARKQLGMNIFDASNEYRLTSWLAQQEDRNIITLYQCDNALSPWTQRCMRQADVVLIVGLGDHSHLVGKFEREIDRLALRTQKELVLLYPETASSKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHETFGDVNIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTAPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPLINKYQTLSCAGCPETYGLNPSDLFSEDEDCDGYISEPTTLNTDVRRYQVPRGGNSLSLSETEMDMDSDVEMDLKMERKMDKATQSTPPLQSKAQILRRKHSKEEARHEWEIKREQKQELAREQELERERELSQKGTTAGATGYTPNAVIATQTSLIFMDEEDEMDKKKTKDNDRDEVRGSAEDTGKEKEEDKENRSNTNNETKNYL
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila persimilis (Fruit fly)
|
B4HBU3
|
PLK4_DROPE
|
MMSTRTFGETIEEYEVQHLLGKGGFASVYKARCLHSHQDVAIKMIDKKLIQGTGLTSRVRQEVEIHSRLKHPSVLQLYTFFQDVNYVYLVLELAHNGELQRYMKQHLLRPFTESEGATILRQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHIKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRLSHGLPADVWSVGCMLYTLLVGRPPFETEGVESTLNKVVMSEFMMPSHLSFEAQDLIHKLLKKSPHERITLEQVLRHPFLKRTVGGSSYSTTPGALNEFSQSLASSDSGIVTFASSDSRKSHRLRSVDNSSGQSMPQIMEEYLPSSNLGYDSKEHRPIYEQHGSYLPTPGDQLENRDAKWPGTNNLAPFTSDSDMIPSPVGEKRLLMPPLETKRLQPTRYKTKNAIMSILRTGEVVLEFVKFKVKYNEDRITDICRISEDGRRIIIYQPDPGRGLPIREHPPDPLIPSENCVYNYENLPNKHWKKYVYAARFVGLVKSKTPKITFFSSLGKCQLMETMTDFEVRFYSGAKLLKSSTDGVKVFNSNGAVLSDNGCAEARNLIDHGNECFSHCVNISNALELAQTKENTCFPVTIGRRPAADMHAGQRFDGLRDTTNFAYSTPKSNQGSINFSVSTISTTRSASDYNSNTPRLNMLAAHQNVPIKRITVPEIGIVTELSHGVVQVQFYDGSMVSVIPKVQGGGITYTQANGLSTHFGNNDDLPFAVRDRINQMPQLQMKLKCAPLLGNARSVDCHLMTPKTTTPFYNRMII
|
2.7.11.21
| null |
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}.
|
Drosophila persimilis (Fruit fly)
|
B4HFB7
|
HH_DROSE
|
MDNHSSVPWASAASVTCLSLDAKCHSSSSKSAASSISASPETQTMRHIAHTQRCLSRLTSLVALLLIVLPMMFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCKEKLNVLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGGAVLTVTPAHLVSVWQPESQKLTFVFADRIEEKNQVLVRDVETGELRPQRVVKVGSVRSKGVVAPLTREGTIVVNSVAASCYAVINSQSLAHWGLAPMRLLSTLEAWLPAKEQLHSSPKVVSSAQQQNGIHWYANALYKVKDYVLPQSWRHD
|
3.1.-.-
| null |
Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm development [GO:0007506]; heart formation [GO:0060914]; hindgut morphogenesis [GO:0007442]; imaginal disc-derived wing morphogenesis [GO:0007476]; intein-mediated protein splicing [GO:0016539]; labial disc development [GO:0035217]; morphogenesis of larval imaginal disc epithelium [GO:0016335]; mucosal immune response [GO:0002385]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; negative regulation of proteolysis [GO:0045861]; pole cell migration [GO:0007280]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of protein localization to cell surface [GO:2000010]; progression of morphogenetic furrow involved in compound eye morphogenesis [GO:0007458]; protein autoprocessing [GO:0016540]; regulation of cell proliferation involved in compound eye morphogenesis [GO:2000495]; regulation of epithelial cell migration, open tracheal system [GO:2000274]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; spiracle morphogenesis, open tracheal system [GO:0035277]; terminal cell fate specification, open tracheal system [GO:0035154]; ventral midline development [GO:0007418]; wing disc pattern formation [GO:0035222]
|
cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
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Drosophila sechellia (Fruit fly)
|
B4HGG6
|
SPAST_DROSE
|
MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHSYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKQKEEARSKPQKTREPMLAGMTNEPMKLRVRSSGYGPKATTSAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila sechellia (Fruit fly)
|
B4HKC7
|
RAS1_DROSE
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
|
3.6.5.2
| null |
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313]
|
plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}.
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Drosophila sechellia (Fruit fly)
|
B4HNW4
|
PTK7_DROSE
|
MISIYGLVMALMMASVLASSSRFQRVPQSQSVVENESVKFECESTDSYSELHYDWLHNAHRIAYDKRVHQIGSNLHIEAVRRTEDVGNYVCIATNLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDLEPLEIEWYRNSEKLSTWKNVQLDQHRLIIRQPGSEDDGLYRCTASNAAGRVMSKQGYVYQSSVKCLPRLPRRKNQKMMESWDKQTFLCRGKRGGAAGLESLPAAPEDLRIVQGPVGQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPIIGHSFDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEAHAPISSSPGILEVIEQLKFVPQPTSKNLELDAVVAKVHCKAQGTPTPQVQWIRDGENTTLPDQVEVDANGTLIFRNVNSEHRGNYTCLATNTQGQINATVAINVVVTPKFSVPPVGPIETSEQGTAVMHCQAIGDPKPTIQWDKDLKYLSENNTDRERFRFLENGTLEIRNVQVEDEGSYGCTIGNSAGLKREDVQLVVKTTGDGFAPEESGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNDLSTKEAGGEQPDAAGNGKGSEQEPCLSKQHNGHSKSRSKSSGDAQKSDDTACSQQSRASKKSAHIYEQLALPRSGLSELIQIGRGEFGDVFVGKLKATLVTSPSDKDADTEKQHSNSENGSGGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQHNQSGLDQLVLVKALNKVKDEQACQEFRRQLDLLRAISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATAGSSSPPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNTLLPIRWLAPECIQEDEYTTKSDIFAYGVVVWELFNQATKLPHEELTNEQVVQRSQAGSLEWSVAEATPDSLREILLSCWVSNPKERPSFSQLGAALSKAMQIAEK
| null | null |
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila sechellia (Fruit fly)
|
B4HSL3
|
LIS1_DROSE
|
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila sechellia (Fruit fly)
|
B4HWI2
|
IRS1_DROSE
|
MASISDDGMALSGNLKKLKTMKKKFFVLYEETSTSSARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKHRFVIVLSSRDGGFGIVLENENDLRKWLDKLLVLQRNIANSNGTAHSPYDQVWQVVIQKKGISEKVGITGTYHCCLTSKSLTFVCIGPEKTPNGEDRVASIEILLTTIRRCGHASPQCIFYVELGRQSVLGSGDLWMETDNAAVATNMHNMILSAMSAKTESNTNLINVYQNRPDLSHEPMRKRSSSANEASKPINVNVIQNSQNSLELRSCSSPHNYGFSRERCDSLPTRNGTLSESSNQTYFGSNHGLRFNTISGIRPHSTNKHSNSPTFTMPLRCSESEDSSISVDESDDNGSFSHYRLNTRTSETAIPEENIDDFASAEFSKVTEPNESDENYIPMNPVNPTDAIHEKEKADLQRLEDASLHFNFPEHASEKLAKDFDLDSDNQCCRPIRAYSIGNKVEHLKFNKRLGHLNDTGQNPNRVRAYSVGSKSKIPRCDLQRVVLVEDNKHEFASNRSQSSIGKEGSSYGSSANRQKKSTSAPLLSLKNQINSDRMSDLMEIDFSQATNLEKQKFIKNNEIPKYIENVFPKAPRTDSSSLTLHATSQKDIFNGSKLNNTAITSEDGYLEMKPVGNGYTPSSNCLPIKVEKLKLSDYQTTAPPLLTATAAPVQDLNKISTYNISAEKWREQPSRSEEKKSNSPLNDNPFSLKPTNVESKSKSHDVHSANQIDCEKVCVQSDKLNNLTDKIVENNNLDIGGHEEKKLVHSISSEDYTQIKDKANDFTKFNEAGYKILQIKSDSSLISSKLYQKGMHKDNLERTHRLTESVNTIPDNATATVGSSSLTKFNINSVKPAADSRSTGTDPSTAQNILQIKDLNFPSRSSSRISQPELHYASLDLPHCSGQNPAKYLKRGSRESPPVSACPEDGNTYARIDFDQSDSSSSSSNIFNT
| null | null |
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; lipid homeostasis [GO:0055088]; long-term synaptic potentiation [GO:0060291]; male germ-line stem cell asymmetric division [GO:0048133]; multicellular organism growth [GO:0035264]; negative regulation of entry into reproductive diapause [GO:0061964]; negative regulation of triglyceride catabolic process [GO:0010897]; olfactory learning [GO:0008355]; positive regulation of border follicle cell migration [GO:1903688]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell size [GO:0045793]; positive regulation of immune response [GO:0050778]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primary spermatocyte growth [GO:0007285]; regulation of tube length, open tracheal system [GO:0035159]; response to anoxia [GO:0034059]; vitellogenesis [GO:0007296]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
|
PF02174;
|
2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell proliferation, cell size, and body and organ growth throughout development. Also has a role in a signaling pathway controlling the physiological response required to endure periods of low nutrient conditions. Insulin/insulin-like growth factor (IGF) signaling pathway has a role in regulating aging and is necessary in the ovary for vitellogenic maturation (By similarity). {ECO:0000250|UniProtKB:P35570, ECO:0000250|UniProtKB:Q9XTN2}.
|
Drosophila sechellia (Fruit fly)
|
B4I1V5
|
FICD_DROSE
|
MCTEAEQPSPPAQQQEQGNPPLCKAQNPKPARLYRLVLLFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHIPPGPGDLALLMQRFERWLNSEHSSTLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGDIP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila sechellia (Fruit fly)
|
B4IAQ8
|
PLK4_DROSE
|
MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTSRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARHFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNMFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQPGLFGQASTGLAEPNWTGAAKTSAFRMETGMVPNSKPASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPNKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDSEIRFYSGAKLLKAPTEGLKVYDRNGMLLSDHSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNITFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPDIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKDDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL
|
2.7.11.21
| null |
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}.
|
Drosophila sechellia (Fruit fly)
|
B4IL64
|
SWS_DROSE
|
MDVLEMLRASASGSYNTIFSDAWCQYVSKQITATVYMYCALVMMSLLFIAWFLYFKRMARLRLRDELARSISTATNSSGDLRGLRFRKRDKMLFYGRRMLRKVKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMQAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRYKSVSTMSGPINSQTSQSSRQAPNGPPMVINQLNLMQSAASGTGSGVSVTVTRPPSSPSRHSREEHTLSDPNPNPDGSFHGTTNLFTEVHGDAPNADLFQQQQQPSVGNLSTRRSSITLMTPDGSHSCVQTPGVTTSIDMRLVQSSAVDSLRKELGLSEEDSHIIEPFVELRELEPNVTLITEGNADDVCVWFVMTGTLAVYQSNQDATRAKQDKSDMLIHFVHPGEIVGGLAMLTGEASAYTIRSRSYARIAFIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGSMQTRSGSGAPGAPVEANPVTHKYSTVALVPITDEVPLTPFTYELYHSLCAIGPVLRLTSDVVRKQLGSNIFEAANEYRLTSWLAQQEDRNIITLYQCDSSLSAWTQRCMRQADVILIVGLGDRSHLVGKFEREIDRLAMRTQKELVLLYPEATNAKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPVDMVGGVSIGALMGALWCSDRNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFENMAKAGRLGRFNQWFNKEPPKRVNHASLNEYTFIDLAQIVCRLPETYAVNTAELFSEDEDCDGYISEPTTLNTDRRRIQVSRAGNSLSFSETEMDSDVELDLKLERKMDKSTQSSPPTSSRTDMRGKEEAKHMANWHWGVKHKDETGSGATVATHTQTGQEQELQQQQKLQQLQQDQGARAEQLVDKDKEEDKENRSSPNNETKN
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila sechellia (Fruit fly)
|
B4J2W3
|
WLS_DROGR
|
MSGTILENLSGRKLSILVSSLMLCQVVCFLMGGLFAPVPAGHQTVLGSKCRDVPGRQNDTSFFLYSRGNGACKSLQDIDIEQDELKMANQLVYVFQMPLPRDNNTLQYSRWQQNLIGVLQVDIAYDSASELREPPKELQLTIDTRLAYRNQKDADTDWKLYAHSVEQRYLDCHASHVGRLETLYTCDIIPLFELGALHHNFYLLNLRFPMDTPKQMNLQFGHMHDLTLTAIHQNGGFTQVWLVLKTLLFPFVIGIMMWFWRRVHILQRSPALLEYMLFYLGGALSFLNLPLELLTLGVEMPYMLLLSDVRQGIFYAMLLSFWLVFAGEHMLIQDSPSKSTIRSRYWKHLSAVVVGCISLFVFDICERGVQMRNPFYSIWTTPLGAKVAMSFIVLAGVSAAIYFLFLCFMVWKVFKDIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAGLTVAGFIMGQMAEGHWKWNENIEIQLTSAFLTGVYGMWNIYIFALIILYAPSHKQWPTMRHSDETTQSNENIVASAASEEIEFSNLPSDSNPSEISSLTSFTRKVAFD
| null | null |
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; positive regulation of Wnt protein secretion [GO:0061357]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of intracellular protein transport [GO:0033157]; segment polarity determination [GO:0007367]; trans-synaptic signaling via exosome [GO:0099157]; Wnt protein secretion [GO:0061355]; Wnt signaling pathway [GO:0016055]
|
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
Wnt-protein binding [GO:0017147]
|
PF06664;
| null |
Wntless family
| null |
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). {ECO:0000250}.
|
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
|
B4JBN5
|
FICD_DROGR
|
METGKVTQEPKQMKFTYRFAFFFIAGSLATFVFHALTSSSSVSLFGWRLQLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGAMRLALDMHISGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALSISPSNSEAFANRQRTANVVQTLDERRLVSLDEKRDALSAIHEANAALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITLKDILELHRRVLGHVDPIEGGEFRRTQVYVGGHVPPGPGDLALLMQRFEHWLNSEQSNSLHPVNYAALAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSQYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEGGVLAQLQSHIAQSAPEPYESGSGLDSGVNGMP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-236 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
|
B4JII0
|
SPAST_DROGR
|
MVRTKNQSSSSSASSSTKSPVKISGGTTNRSRSCSDALIDDGNSKSSSKPTSNNRQRTTTNNNTTAITTTPGSSPDNDDDDTTTTDADLTPTSGNAPRGGNSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRSPNRRDCNIEIVVQNSKEQQQQHQHQQAIIHCPLERRGNISGIEQTLAQALPQRQRAIQPLEMAGNRAGGNYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLQLQRLSLKEQQQKKKSPQQQPQQQQQHTFKQPMLVGQTNSSGGSGSTKVPLRSSGYGLKPSATNISRAMPAASGRKLTIGNKRPGNLPVVNKSQTLPRNLGSKTSSTSVGAALQRQPGKTAATPPAVRRQFSSGRNTPPQRSRTPINNNAAGGSGSGASTPMVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDVQTRELLLNRLLQKQGSPLDSDALGRLAKITEGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRQITEKDFHNSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
|
B4JTF5
|
HH_DROGR
|
MDNEAVSALWSCASATCLSLDVKRHCSDANVDSQARTQSQATPMTNETDPRKLRHIAHTPRGSCFMTLLLLLLLALNFRHAHSCGPGRGLGRRRDRNLYPLVLKQTVPNLSEYQSGASGPLEGVIDRKSPKFKDLVPLYNSDILFRDEEGTGADRMMTKRCKEKLVMLATSVMNEWPGVKLLVTESWDEDHHHGEQSLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSSSISHVHGCFTPESTAQLESGAKKPLGELAIGDRVLSMDAKGQAVYSEVILFMDRNLEQMETFVQLHTDGGAVLTVTPAHLITVWQPERQTLDFVFADHVEELNYVLVVDDATGGELRPQRVLRVSSVRRRGVVAPLTREGTIVVNSVAASCYAVISSQSLAHWGLAPMRLWSTLQSWLPAKDKLRSSKVQEKSTPKVNSTAQLQNGLHWYANALYKVKDYVLPQSWRHD
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
|
B4JWA1
|
LIS1_DROGR
|
MKMVLSQRQREELNQAIADYLGTNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERTLKGHTDSVQDVAFDAQGKLLVSCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGQCLLTLNGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
|
B4K4M0
|
HH_DROMO
|
MDNNQAVSALWSCASATCLSLDAKRHSLEPSSPDGQASLDVNNKSAPVDAHARKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYHNGASGPLEGVIHRDSPKFKNLVLNYNKDILFRDEEGTGADRVMSKRCREKLNMLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPSISHVHGCFTPESTALLESGAEKALSELAIGDRVLSMDTKGQPVYSEVILFMDRNLEQVQNFVQLHTDGGAVLTVTPAHLIAVWQAERQTLEFVFADRVEELSQVLVHDATGELRPQRVLRVDSVQSRGVVAPLTREGTIVVNSVAASCYAVISSQSLAHWGLAPMRLWSTLQSWMPAKGQLRSAQDKPTPKDATAQQQNGIHWYANALYKVKDYVLPQSWRHD
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila mojavensis (Fruit fly)
|
B4K799
|
SPAST_DROMO
|
MVRTKNQSSSSSASSSTKSPVKISGGGSSGANRSRSCSEALIDDGKTSSKLSSNRQRATITTTTTSTTPGSSPDDDTTDADLTPTSGYGPRGGTSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYCASTKVIYRSPHRRDCNIEIVVQNSKEQQSIICPLERNTSDGIEKAQQLLPQRQRALLPLEMATNRGGSGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHEKMQTNLSMARDRLHFLALREEDLQMQRLSLMDPPKNKQQVTSKFKQPMLVGQTNSKAAAVEPSKITMRSSGYGPKPVSGTGSSAGTSKALQAASGRKLTIGNKRPGNLAVANKSQTLPRNLGSKTTSTSVGAALQRQPGKTAATPPAVRRQFSSGRNTPPQRSRTPINNNAASGSGSGSGASTPMISVKGVEQKLVQLIMDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHLQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPEVQTRELLLSRLLQKQGSPLDTEALARLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRPITEKDFHNSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila mojavensis (Fruit fly)
|
B4KFW6
|
FICD_DROMO
|
MAMATGKATEEEQPEQGQQQQQLQQQQKQTTLQSTYRFALFFIAGCLAAFGFHALTSSSGSLLGWRLRLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSVSDSVGASLSEAEETNIKEAMGALRLAQEMYMTGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALSINPSNTEALANRQRTADVVQLLDERRLSSLDEKRDALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLYITLKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHIPPGPGDLAILMQRFEHWLNSEQSNSLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSQYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESDGNVLAQLQSHTSSPELYESGSGSGAGAGAGSGQKGMP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;PF13428;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-251 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila mojavensis (Fruit fly)
|
B4KPU0
|
PTK7_DROMO
|
MPIVMDMNMLLMLSLAFTVMAPASASSSRFTQPPQSQAIVENDAADFSCEATGPSGDLHYEWLHNGQQIGYDSRVLQIGSNLRIESVQREDAGDYVCIAASAASGARQASPPAKLSVIFLDAVTVQLLGSNRNELLLKCHVEGASGDEPLQIEWYRDSAKLSSWQNVELQQHRLLVRQPSSADDGLYRCIASNAAARVMSKQGYVYEHLASVAPGSTKCLPKLKRNQKMPESWGKQVFLCRGKRGGSTGMDQSQSLPPSPEGLRIVQGPNDKLIIKEGEPTTLSCLYELPAELQNQRIQLRWRKDGKILRHVELGDAVVPGLALDHGKDALVREDGRLVLHKQNGTLSFNSIIASDAGQYMCQIQLEGHAPVNSAPGALEVIEQLKFMPQPTSKNLELGALGKLHCKAQGTPTPQVQWLRDAANGSLPEHVDDINGTLIFRNVSAEHRGNYTCVASNSQGQINATVAINVVVAPRFSVAPEGPIESSEQGVAVIHCQAIGDPKPTIQWDKDLKYLSENNTDRQRFSFLENGTLEIRNVQAEDEGKYGCTIGNSAGLKREEVRLLVRGNGDGFITEESAGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNELSIKEAGGDQAESGKNTEQEPCLSKQRNGHGKSRTAANGDAQKSDDTACSQQSKASKKSAHIYEQLALPRSGLSELIQIGRGEFGDVFVGKLKASLVAAASPSDKDADTEKQHSNSENGSGASGASGCGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQPQEQAQSESTADLLVMVKALNKVKDEQACQEFRRQLDLLRAISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATATSSPPPLTTSQLLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVAYPALCKDKYSREYHKHRNTLLPVRWLAPECIQEDEYTTKSDIFAFAVVVWELFNQATKLPHEDLSNEQVVQRSLANTLEWSVAEGTPDGLKEILLSCWLTNPKERPSFSQLGAALSKAMQAAEK
| null | null |
cell adhesion [GO:0007155]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]
|
axon [GO:0030424]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; cell-cell adhesion mediator activity [GO:0098632]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila mojavensis (Fruit fly)
|
B4KT48
|
LIS1_DROMO
|
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTESEKKYGGLLEKKWTSVIRLQKKVMDLEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLNGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQSVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; iron-sulfur cluster assembly [GO:0016226]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; CIA complex [GO:0097361]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila mojavensis (Fruit fly)
|
B4L184
|
WLS_DROMO
|
MSGTILENLSGRKLSILVSSLLLCQVACFLIGGLYAPVPAGHQIVMGIKCRDVAGRQNDTSFFLYSRGNGACDSVQDIDIEQDPLKMANQLVYVFQMPLPRDNRTLDYSRWQQNLIGVLQMDIAYDSSSELREPPKELQLTIDTRLAYRNKNDEDADWKPYAHSIEKRFLDCRAAHVGLQEILYTCDIIPLFELGALHHSFYLLNLRFPMDTPKRLNLQFGHMHDIILTAIHQNGGFTQVWLLLKSVLFPFIIGIMVWFWRRVHILQRSPALLEYMLLYLGGALSFLNLPLEYLTLSFEMPYMLLLSDVRQGIFYAMLLSFWLVFAGEHMLIQDSPNKSTIRSRYWKHLSAVVVGCISLFVFDICERGMQLRNPFYSIWTTPLGAKVAMSFIVLAGVSAGIYFLFLCYMVWKVFKDIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAGLTVAGFIMGQMAEGHWKWNEDIEIQLTSAFLTGVYGMWNIYIFALLILYAPSHKQWPTMRHSDETTQSNENIVASAASEEIEFSNLPSDSNPSEISSLTSFTRKVAFD
| null | null |
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; positive regulation of Wnt protein secretion [GO:0061357]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of intracellular protein transport [GO:0033157]; segment polarity determination [GO:0007367]; trans-synaptic signaling via exosome [GO:0099157]; Wnt protein secretion [GO:0061355]; Wnt signaling pathway [GO:0016055]
|
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
Wnt-protein binding [GO:0017147]
|
PF06664;
| null |
Wntless family
| null |
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). {ECO:0000250}.
|
Drosophila mojavensis (Fruit fly)
|
B4L535
|
SWS_DROMO
|
MDVLELLRASVNGCYNTLFSDAWSQYVSKQIATTTYWYGALLAIGALFIAWFLYFKRLASLRLRDESARTLSALTAASGGDHRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLQRENRPLEMKTVEPPAEYLEETIDGSDRVPPDALYMLQSIRIFGHFEKPIFLKLCKHTQLLQLMAGDYLFKITDPDDSVYIVQSGMINVYICNADGSTLSLKTVRKGESVTSLLSFIDVLSGNSSYYKTVTAKAMEKSVVIRLPMQAFEEVFNENPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRIKGSNPVPVTVPGPVLSQASQASRAMASRPATSPVTRMSREEHTLSDPDPNPNASAMLFAEVHGDAPYIDLYHHQQQQSSGVSVGGTHRSSGACTPTGSGGESPDGTGNATITNIDQRLVQSSAVDSLRRELGLSEEDTSIIEPFVEVRELEPNVTLITEGNAEDVCIWFVMTGTLAVYQSNADATRAAKQDSKNDMLIHFVHPGEIVGGLAMLTGEASAYTIRARSNSRIAYIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVLAVRDSELAKLPEGLFNAIKLRYPIVVTRLISFLSHRFLGSMQTRGANASSAPVEANPVTHKYSTVALVPITDDVPITPFTYELYHSLCAIGPVLRLTSEVVRKQLGNNIFEAANEYRLTSWLAQQEDRNIITLYQCDSALSPWTQRCMRQADVVLIVGLGERSHMVGKFEREIDKLAMRTQKELVLLYPETTNARPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPQDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFDNMAKAGRLGRFNQWFNKEPPKRGNHASLNEYTFIDLAQIVCKLPETYALNAVDIFSEDEDFDGYISEPTTLNMDRHRIQVPRAGNSLSFSETELDSDVEIDLELERKVDKSTQSTPPTPNKKHPSTPTSSQGNLMHLPLSMKAKDKMQILDKLEREHKRRQKSKHKRDRSMQRDSKATLHPAPMAEATTQTPSSDVDIDAKLDQLRKLQQELEQGNESEQEQEQEQEQEQGHIQEPENVTEADTKN
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila mojavensis (Fruit fly)
|
B4LC58
|
WLS_DROVI
|
MSGTILENLSGRKLSILVSSLMLCQVACFLMGGLYAPVPAGHQTVVGIKCRDVPGRQNDTNFFLYSRGNGACKSLQDMDIEQDPLKMANQLVYVFQMPLPRDNRTLDYSRWQQNLIGVLQVDIAYDSSSELREPPKELQLTIDTRLAYRNKKDADTDWKLYAHSVEQRYLDCHAAHVGLLETLYTCDIIPLFELGALHHNFYLLNLRFPIDTPKRMNLQFGHMHDLTLTAIHQNGGFTQVWLLLKTLLFPFVVGIMIWFWRRVHILQRSPALLEYMLLYLGGALSFLNLPLEYLTLSIEMPYMLLLSDVRQGIFYAMLLSFWLVFAGEHMLIQDTPNKSTIRSRYWKHLSAVVVGCISLFVFDICERGVQLRNPFYSIWTTPLGAKVAMSFIVLAGVSAAIYFLFLCFMVWKVFKDIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAGLTVAGFIMGQMAEGHWKWNEDIEIQLTSAFLTGVYGMWNIYIFALIILYAPSHKQWPTMRHSDETTQSNENIVASAASEEIEFSNLPSDSNPSEISSLTSFTRKVAFD
| null | null |
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; positive regulation of Wnt protein secretion [GO:0061357]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of intracellular protein transport [GO:0033157]; segment polarity determination [GO:0007367]; trans-synaptic signaling via exosome [GO:0099157]; Wnt protein secretion [GO:0061355]; Wnt signaling pathway [GO:0016055]
|
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
Wnt-protein binding [GO:0017147]
|
PF06664;
| null |
Wntless family
| null |
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). {ECO:0000250}.
|
Drosophila virilis (Fruit fly)
|
B4LG38
|
UBP36_DROVI
|
MPVSLAVCETANVVNAALRESLGSGIGGGGGCVAAAASRSSAGSGSGSVAGVDEAKIGDVSGTDNLQSQIVANAKRVLLAKIEYEEVENYHESVLAKLKSKYIVIKPDNNNGAANCNYKTNGKAVGSNGHDNNTVNGGTVNGNRKQTVDSGQSNQNSSANPNELPKPKRVLYPRENIRIGWKQSERKWQVGAGMLNVGNTCYLNSTLQALFHIPALANWLVSETSHVENCNISESCGSGGCIICAMAKTLQTTQSNQSAVRPFLIYTKLRQICKHMVVGRQEDAHEFLRFLVEAMEKAYLMRFRNFKELDQLVKETTPISQIFGGYLRSEVRCLSCNHVSITFQHFQDLLLDIRKADTLEEAFDGYFSRERLEDMGYKCEGCKKKVSATKQFSLERAPITLCIQLKRFSMMGNKLTKQISFKPRIDLSRFAARSPTAAAQPLSYRLVSMVTHLGVSQHCGHYTAIGLTEAGSYYNFDDSYVKPIAMQSVCNTNAYIMFYELDVANSSSSSTINNNSSSSSNNSVAPKLNGLRLSNGAHSPAAATVAVAATATSTSASAVSPRFIGPQLPNGYANSNGHALGGAKTTIQFKTTPQKQLQQQQQQQNGLLMGANKFQESSQSKHSLAGTLHKGEAAPNANTNANANKSSCNNNITSQHQQQHILPISSDEDEDEDDSDDDDDDDDDDVKANTAPQLPSMPKMFEDSESVAQTAKLKPKTPLKSLVPYESASEEEQEQQQQQQQQQLLQTPQQLAANPRKRRSGSDSSESEEEAPPPLPSILRNGHAKTNGSVSNTSNSSHSKAKSASNASSANVNSSKQKTDAIDEIFKSLNNYKNKHRIAADDDEDGDGDGDGHGNEQVQTEQGTKKLNSASSASASKSNGWQSQNGKAPSSPKTPPSPAVIKSKTGIWQITRTNDDDDEEDEEEDDVEADADQEDDDDEVVVVEEPQVSVTPKNPKNPFAASKSAEANATIAGAKRQKLLNGSAKSAATTRPGNGYQSESVANGSAVSELLKQNHRGYGTSVLSWNGKPSELDKESFDLVCAKRIAGHGDTDVHSDVNSSSNNSSNINSNSNSNSNGNGKRKNSTLLAEAREQRKRDAEDEEENEMDRGRQRKVKSASVKSNNSTPGYNPFQEFENQKRWHSNKSGTFPRFYHQNNRPNFQQRNKFKFNRFGGGAKFQQQRALQRHLAAGGGFTRRQQQSTGQQQQQQQQQQQS
|
3.4.19.12
| null |
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; positive regulation of proteasomal protein catabolic process [GO:1901800]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; somatic stem cell population maintenance [GO:0035019]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]
|
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby preventing histone H3 'Lys-4' trimethylation (H3K4). Controls selective autophagy activation by ubiquitinated proteins. {ECO:0000250|UniProtKB:Q9VRP5}.
|
Drosophila virilis (Fruit fly)
|
B4LQ21
|
LIS1_DROVI
|
MKMVLSQRQREELNQAIADYLGSNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGQCLLTLNGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
| null | null |
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616]
|
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat LIS1/nudF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
| null | null | null | null | null |
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
|
Drosophila virilis (Fruit fly)
|
B4LQT7
|
FICD_DROVI
|
MAKAKAKQEPQQQRQTLQATYRFVLFFIAGSLAAFAFHALTSSTGSLMGWRLRLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSISDSVGASFTEAEQTNIKEAMGALRLAQEMYMAGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALCISPSNSEALANRQRTADVVQTLDERRLISLDEKRDALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITLKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHVPPGPGDLAILMQRFEHWLNSEHSSSLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTENEGHVLAQLQPHIAQSIPELHESGSGSGSGADPIRVP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;PF13428;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-236 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila virilis (Fruit fly)
|
B4LX81
|
SPNE_DROVI
|
MDSDLMDFFDFSKQFKRGTALKGCITGDPNALTTESRDSKPIKREKIGTDYVNEIVEKEKQLMNKLVDGQSVAKRNRTLDELDSDDEEENMQEQPSVRSDEAYYEKYRFDLNRNKNLPIYAQREQIMKAIRENPVVILKGETGCGKTTQVPQYILDEACKRREFCNIVVTQPRRIAAISIANRVCQERQWQPGTVCSYQVGLHRQSNVEDTRLLYCTTGVLLNNLIRLKTLTHYTHIVLDEVHERDQDMDFLLIVVRRLLALNSRHVKVILMSATIDTREFSKYFATSSAFPPVVTASHGRKYPLVKYYRDQLKNIHWKDEPQERAPGIGPEGYADAIKILLVIDNMERKAVGQSLQSYEEAKRTGSVLIFLPGINEIDTMADHITSVMEENPTMIITIVRCHSLMSPDSQEEVFQPPLPGHRKIILTTNIAESSITVPDVSYVIDFCLTKVLHTDTATNYSCLRLEWASKVNCRQRAGRVGRLRSGRVYRMVSKAFYLEEMKEFGIPEMLRSPLQNSVLKAKELEMGRPSEILALAMSPPNLSDIQNTVLLLKEVGALYTTVDGVYEELDGDLTYWGTIMSRFPLDVRLSRLIILGYVFNCLEEVIVIAAGMTVRSLYLTGKRRQVNDAFWMHYIFADGSGSDMVAIWRVYRIYLNMCQDRMLKESAEQWARRFNVNLRSLKEMHLMVQELRQRCASVNLQPLPYGTCQMWDDREKSIILKVIIAGAFYPNYFMRSNKSNADYDRSLFQSICGNDPCRTVFFTHYEPRYMGELYTRRIKELFLEVKIPPENMDVTFLHGSEKVFVTFKSDDEDMDTAKVVQVPGRVMTEVYKAVRMRLENQNRPLRVMDQNSALRYVQDRKIGVVTEGTWFPPSNQWNVELLTLPSVFAKNITGLVTYIVSCGKFYFQPRALAESIASMSEIFNGPQQLSCHVRNASAVTKGLQLLAKRGHLFQRAVVLRIETQTNGHPRFRVRFIDYGDMAVLPMDQLRLMPHELKRDFDQLPPRMFECRLALVQPSMVTSSYNRWPKAANDMLISVAQCGRLELEVYSLVNNVAAVLIHMRDGVLNDRLVERQLARRADEDYMSRKDHDLRIRKQEAKRNISVAEQERINEEYLRFAQLPKDMDLEPPPLDKCNLSIRLRGPFSPLESSMNSMLRIGMYKSVTIDKDSVNAVLLDTDPQDRHDQMVVAASVTETDNTERLTARGTTLMPNIHGFGALMAMLFCPTMQIKCNKDRTKYVCLLAGLGFDPETLEPYFAEHDMVINLDVTILRDDIRIINQMRYNIDSMFYNFDANEMPSVGTEDRVVIFNQLRSLLTRLLGKDRSFIERHVSNSEYLWEDMSDLEPPSEPYGKRAIFPMHSSYDLENDNLSNLLELQANCKQLYDWRNFEGNLQTQVCRLCNESLESVAELRLHLLTQLHRDREKQVGYKQQ
|
3.6.4.13
| null |
dorsal appendage formation [GO:0046843]; germarium-derived oocyte fate determination [GO:0007294]; global gene silencing by mRNA cleavage [GO:0098795]; heterochromatin formation [GO:0031507]; intracellular mRNA localization [GO:0008298]; mitotic chromosome condensation [GO:0007076]; oocyte karyosome formation [GO:0030717]; oocyte localization involved in germarium-derived egg chamber formation [GO:0030720]; oocyte maturation [GO:0001556]; polarity specification of anterior/posterior axis [GO:0009949]; polarity specification of dorsal/ventral axis [GO:0009951]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; regulation of pole plasm oskar mRNA localization [GO:0007317]; retrotransposon silencing [GO:0010526]; secondary piRNA processing [GO:0140965]; spermatogenesis [GO:0007283]
|
nucleus [GO:0005634]; P granule [GO:0043186]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF00270;PF21010;PF00271;PF00567;
|
1.20.120.1080;2.30.30.140;2.40.50.90;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the nuage, also named P granule, a germ-cell-specific organelle required to repress transposon during meiosis. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: Probable ATP-binding RNA helicase which plays a central role during spermatogenesis and oogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi and govern the methylation and subsequent repression of transposons. Involved in the repression of LTR retrotransposon copia. Also involved in telomere regulation by repressing specialized telomeric retroelements HeT-A, TAHRE, and TART; Drosophila telomeres being maintained by transposition of specialized telomeric retroelements. Involved in telomeric trans-silencing, a repression mechanism by which a transposon or a transgene inserted in subtelomeric heterochromatin has the capacity to repress in trans in the female germline, a homologous transposon, or transgene located in euchromatin. Involved in the repression of testis-expressed Stellate genes by the homologous Su(Ste) repeats. Required for anteroposterior and dorsoventral axis formation during oogenesis (By similarity). {ECO:0000250}.
|
Drosophila virilis (Fruit fly)
|
B4LY29
|
RAS1_DROVI
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVQNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRKGRKTNKPNRRFKCKML
|
3.6.5.2
| null |
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}.
|
Drosophila virilis (Fruit fly)
|
B4LZT9
|
HH_DROVI
|
MDNQTVAAIWSCASATCLSLDAKRHSVETNTNDRQAPPGLSNSNNNNNNNKSTAVDADPRKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYMSGASGPIEGVIQRDSPNFKDLVPNYNRDIIFRDEEGTGADRLMSKRCREKLNTLSYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPFISHVHGCFTPESTALLESGAKKPLSELAIGDRVLSMNGKGQAVYSEVILFMDRNLEQMQNFVQLHTDSGAVLTVTPAHLITVWQPEREALDFVFADRVEELNYVLVHDATGELRPHRVIRVSSVRSRGVVAPLTREGTIVVDSVAASCYAVISSQSLAHWGLAPMRLLYTLQSWMPAKGQLRTAQDKSTPKDATAQQQNGLHWYANALYKVKDYVLPQSWRHD
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila virilis (Fruit fly)
|
B4M0H8
|
SPAST_DROVI
|
MVRTKNQSSSSSASSSTKSPVKISGGGGGGGGSSSSTNRSRSCSEALIDDGKSSSKLSSNRQRTTTTITTTTTTPGSSPDDDTTDADLTPTSGNVPRGGQSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRSPHRRDCNIEIVVQNSKEQQAIICPLEGSGVNIEQAQILPQRQRALQTLEMAASRGGTGAGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHEKMQTNLSMARDRLHFLALREEDLQMQRLSLKEQPKKQLPHKFKQPMLVGQTTTSSGSSSSSRASAEPPKITLRSSGYGPKTGGATTSKAVPAASGRKLTIGNKRPGNLAVANKSQTLPRNLGSKTTSTSVGAALQRQPGKTAATPPAVRRQFSSGRNTPPQRSRTPINNNAASGSGSGASTPLISVKGVEQKLVQLILDEIVEGGAKVEWSDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPEGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPGVQTRELLLSRLLQKQGSPLDTEALARLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRPITEKDFHNSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila virilis (Fruit fly)
|
B4M709
|
SWS_DROVI
|
MDVLELLRASANGCYNTLFSDAWFQYVSKQIATTMYWYGALLVIGVLFIAWFLYFKRLARLRLRDEIARSLSAVTSSGGDHRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLQRENRPLEMKTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPIFLKLCKHTQLLQLMAGDYLFKITDPDDSVYIVQSGMINVYICNADGSTLSLKTVRKGESVTSLLSFIDVLSGNSSYYKTVTAKAMEKSVVIRLPMQAFEEVFEENPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRTKGSSVVPNAVGGAVLAQASQASRPVVRAPTSPNSRLSREEHTLSDPDPNPNANALLFAEVHGDAPYIDLYHHQQQQSSAVSVNQAGTRRSSTTYGPSGESPNGNANTAPGTSIDQRLVQSSAVDSLRRELGLSEDDAQIIEPFVEVRELEPNVTLITEGNAEDVCVWFVMTGTLAVYQSNADATRATKQDSKNDVLIHFVHPGEIVGGLAMLTGEASAYTIRARSNSRVAYIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITHPGGKKEIIGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTRLISFLSHRFLGSMQTRGSNAAGGPVEANPVTHKYSTVALVPITDDVPLTPFTYELYHSLCAIGPVLRLTSEVVRKQLGINIFEAANEYRLTSWLAQQEDRNIITLYQCDSSLSPWTQRCMRQADVVLIVGLGERSHLVGKFEREIDKLAMRTQKELVLLYPETTNAKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPQDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFDNMAKAGRLGRFNQWFNKEPPKRGNHASLNEYTFIDLAQIVCKLPETYALNTADIFSEDEDFDGYISEPTTLNMDRRRIQVPRAGNSLSFSETEMDSDVEIDLELERKVDKATQSTPPTPNKQHALSPTSSQTNLLPLPPNSKPKEKQPSYDKLDREHKRRQKSKQKQQQERSSMQQRDSMVTLHPATMAEATTQTAPHSSEEDELNKPEQQPEQKPVPETEEQQQKQQDQQQQENLTKTDTKN
|
3.1.1.5
| null |
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
|
PF00027;PF01734;
|
3.40.1090.10;2.60.120.10;
|
NTE family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
|
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
| null | null | null | null |
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
|
Drosophila virilis (Fruit fly)
|
B4MR28
|
PTK7_DROWI
|
MDMLMMWSICLFVCIFMAPFSCGSGSSSRFIQVPESQSIVENDSVDFNCEATTDPSTDLHYEWLHNGHQIVYDKRVYQIGANLHIESVQRGEDVGDYVCIAMSLSSGAREASPTAKLSVIFLDSASVQLLGSNRNELLLKCHVEGASGNEALQIEWYRNSAKLSSWQNIELDEHRLLVRQPTGSDDGLYRCIASNAAGRVMSKQGFVYQHQQQQQAGAKCLPRLKKNQKFLPESWGKQIFLCRGKRGGNVEAGLAPSPEGLRLVQGPDDQITIKEGEPATLSCLYEIPAELQNQRIQLRWRKDGKLLRQVELGASLPRGMGNPHNGHSLDGKDALLREDARLVLHKANGTLSFGTVIASDAGQYQCQLQMEGHLAINSSPGILEVIEQLKFMPQPTSKNLELDAAVAKVHCKAQGTPTPQVQWFRDGVNTTLPDQVEVDLNGTLIFRNVNADHRGNYTCLATNLQGQINATVSINVVVAPKFSVPPNVPMEIAEQSTVVIHCQAIGDPKPTIQWDKDLLYLSENNTDRQRFSFLENGTLEIRNVQAEDEGRYGCTIGNSAGLKREEAVLTVKTSSTGGGGYVTEESSGDGGFLATRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNELSIKEAGGEQAGGEGSTSGNPKASEQEPCLGKQQRNGRNGKSKSNGDPQKSDDTACSQQSRASKKSAHIYEQLALPRSGLSELIQIGRGDFGDVFVGKLKASLVNNAQANDKDSDNDKQHSNSENGSGGSSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQQQSQQQQQQDQLVMVKALNKVKDEQACQEFRRQLDLLRALSHKGIVRLYGLCREKDPHYLVLEYTDWGDLKQFLLATAGKVNTATTATSSTTPLPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNSLLPIRWLAPECIQEDEYTTKSDIFSYGVVVWELFNQATKLPHEDLTNEQVIEKSQDGTLKWTVAESTPESLKEILLSCWSVNPKQRPSFSQLGAALSKAMQNSE
| null | null |
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]
|
axon [GO:0030424]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]
|
PF07679;PF13927;PF07714;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
| null | null | null | null | null |
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}.
|
Drosophila willistoni (Fruit fly)
|
B4MUQ2
|
FICD_DROWI
|
MPWEFLKKCDRQKAEVRGEKEEQEPVPGNPHFQVQFHVTSCRFAFLAFLAGSFLAFSLHALISSNLFWRLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSTADSVGATYTEAEETNIKEALSSLRLAQDMYMAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTINPSHSEALANRQRTADVVQTLDERRLASLDAKRAALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHVPPGPGDLAVLMQRFEDWLNSEYSSSLHPVNYAALAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTETEAGEQLVKLQSPQMASIPESFYESGSGALP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-255 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila willistoni (Fruit fly)
|
B4MXR8
|
PLK4_DROWI
|
MLPVRNYGETIEEYEVQHLLGKGGFASVYKARCRRTYQDVAIKMIDKKLIHGTGLSSRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNQQMSHPFTEADAATILQQVVAGLLYLHSHNIMHRDISLSNLLLSKDMHVKIADFGLATQLKRPDEKHMTMCGTPNFISPEVVSRLSHGLAADVWSVGCLLYTLVVGRPPFDTDAVQSTLNKVVMSEFIMPTHLSFEACDLIEKLLKKNPHERISLEQVLRHPFMSKRSAGAEEPQYNSSKPGACDFYMEAQGQSVASGDSGIVTFASNESRSSQRLRSIEKSAQSSSNPQMLPQIQEEYGYWQPSTEHKPYPMPLSSDNAEWERLGSKGNQPHTAASVITEEQQMRVPPLNTIRLQPTRYKTKNAIMSILRHGEVVLEFVKFRSKLNEDRVTDICRISGDGRRIIIYQPDPGRGLPIREQPPPPESHIAGDKSVYNYDSLPSKHWKKYLYAARFVGLVKSKTPKITYFSSLAKCHLMENMIDFEMSYYSGAKYVKTSPGEELKLYNNYGMLLSDLACPEAKKMIEHGNECFSHCINICNALELAQQSADSRNTCFPVTIGRRPLTDVSHSQRFDGLRDTTNIAYSTPKSHQGSINFSMSTISSVQNGSESVSSTHSHASRAQIQASQQNVPIKRINIPDVGIATELSHGIVQVQFYDGSMISLIPEIQGGGLTYTQCNGVSTYFPKYDGDLPLAVRDRLAQIPQVKLRLKCAPLLSNHRKADNIAMTPKSTTPSTPCYNRIVL
|
2.7.11.21
| null |
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}.
|
Drosophila willistoni (Fruit fly)
|
B4N5D3
|
WLS_DROWI
|
MSGTILENLSGRKLSILVSILLLCQVLCFLLGGIFAPVPAGHLTILGSLCRENHARQNDTNFFLYSRGDGACKQVTSEEVDADALKLANQIVHVFQLPLPRENKILEYTRWQQNLIGVLQVEFGYDSSPELHEPAKELQLTIDMRLAYRNNDDADNDWKLYAHSVEHRYLDCDTSHIGPTETLYTCDMIPLFELGALHHSFYLLNLRFPLDSPKQMNLQFGHMHDLTLTAIHQNGGFTKVWLFLKSVLFPFVVGIMVWFWRRVHLLQRSPALLEYMLIYLGGALTFLNLPLEYLTLGLEMPYMLLLSDIRQGIFYAMLLSFWLIFAGEHMLIQDSGNKSTIRSRYWKHLSAVVVGCISLFIFDISERGVQLRNPFYSIWTTPLGAKVAMGFIFLAGVSAAIYFLFLCFMIWKVFKNIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAALTVAGFIMGQMAEGHWKWNEHIEIQLTSAFLTGVYGMWNIYIFALLILYAPSHKQWPSMHHSDETTQSNENIVASAASEEIEFSHLPSDSNPSEISSLTSFTRKVAFD
| null | null |
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; positive regulation of Wnt protein secretion [GO:0061357]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of intracellular protein transport [GO:0033157]; segment polarity determination [GO:0007367]; trans-synaptic signaling via exosome [GO:0099157]; Wnt protein secretion [GO:0061355]; Wnt signaling pathway [GO:0016055]
|
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
Wnt-protein binding [GO:0017147]
|
PF06664;
| null |
Wntless family
| null |
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Endosome membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). {ECO:0000250}.
|
Drosophila willistoni (Fruit fly)
|
B4NBP4
|
SPAST_DROWI
|
MVRTKSSSSSASSSSQKSPIKSNNGAGGGGSSSSHRQSHRTSIDERKSSSHAHSNNSNVSSSSRRAATATSGSSSPEGDDDTTTDDLTPTGSSPRSCNGRGHSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVLYRPHRRDCNIEIVVQNSKEQQLQLQQHQHNQTLSYSLETGGVSGGSGGEQQVQVQPQRIRALQPLEMATNRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWNGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLQMQRLSLKEKQPAPKQPQRSQTKDPVKQPMLTSLNADPVKMKVRSSGYGPKQNGTSSSRPAPSGQTATGASGRKLTVGTKRPGNLPVTNKSQTLPRNLGSKTTVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNASSGSGASTPMVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSNEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITEGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRPITEKDFHNSLKRIRRSVAPQSLNSYEKWSQDYGDITI
|
5.6.1.1
| null |
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331]
|
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Drosophila willistoni (Fruit fly)
|
B4NJP3
|
HH_DROWI
|
MDSQSNQTPWASASVTCLSLDAKRHSQCLDDAIKSGHQVNYSPARSLRYIAYTQRCGIRLTMLMLIMCLTFMPAHSCGPGRGLGRRRVQNLYPLVLKQTVPNLSEHQLGASGPLEGEIPRDSPKFKDLVPNYNRDIVFKDEEGTGADRLMTKRCREKLNALAYSVMNEWPGVRLLVIESWDEDHDHGQESLHYEGRAVTIGTNDRDLSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSTISHVHGCFTPESTAQMENGEKKPLSQLSIGDRVLSMGSNGQPVYSEVILFMDRNLEQLENFVQLHTDGGAVLTVTPAHLISVWQPDSQQLNYVFADRVEEMNYVLVNDVVTGELLPQRVIKVTSVHSKGVVAPLTREGTIVVNSVVASCYAVINSQSLAHWGLAPMRLLSSLQSLMPAKGQLRTTSSATQPTKEVSRAEQQNGIHWYANALYKVKDYVLPKSWRHE
|
3.1.-.-
| null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; system development [GO:0048731]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}.
|
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}.
|
Drosophila willistoni (Fruit fly)
|
B4NZY8
|
IHOG_DROYA
|
MTLLTSSLLFFSLLTSRLEAIPVLEKSPAHPAHSAHPAHPSHPSPGVRILRAPESLVAPLGDEVVLECETSLQPERFEWSHRSSRSSGAGFKYLRTGTAKANVSQEAAISRLKVLVRQDTLGEYRCVGWFGPLVVTSTIARLELASTSLLGGQESESPLQWRVSAGNSVLWPCGKQVKSNPSASWSYYRNGVEIKPEFIGTNGNIFLSNVSSESSGSYSCQATNPASGERIQLTGSLQLQVTPEQRSQSKSPHLLNGQPNSQEITIREGSSLLLLCPGVGSPPPTVVWSSPDVVGAVKNKRSKVIGHALEISNTRVQDAGTYICFQDNGVRPVLEHYIKVHVEQPPQIVRPPWADLTNEGDRLKLECEATGVPTPEIYWLLNGHSSLDDTEAELSNNFLILHSVLKRHAGYVQCFARNRLGEHSAGTLLQVNPKQIQEPRESGGTHRPKPNQGSKQKQMYPPTPPNVTRLSDESVMLRWMVPRNDGLPIVIFKVQYRMVGKRKNWQTTNDNIPYGKPKWNSELGKSFTASVTDLKPQHTYRFRILAVYSNNDNKESNTSAKFYLQPGAALDPMPVPELLEIEEYSETAVVLHWSLASDADEHLITGYYAYYRPSSSAGEYFKATIEGAHARSFKIAPLETATMYEFKLQSFSAVSASEFSALKQGRTQRPKTSTTEEPTLQMGDRDTTTPSHNETFNMSPMLTGTIGGGAVLILLLISTCLCVCRRRSSRSRGNNPNKPRMAELRDDFVPLGNCSPTKQRQRTRHIHITLNPLAQQQQQALEEKNDTDQDAPYYQRPSSYDYDPGLRRMSSSSLRRSQRTLERAGGSNGSNNGNNNNLNQSAEAGPVENPGKPGRVLMKRPRLSSRSENLSSGSLNSVGV
| null | null |
compound eye development [GO:0048749]; cuticle pattern formation [GO:0035017]; homotypic cell-cell adhesion [GO:0034109]; maintenance of protein location in extracellular region [GO:0071694]; segment specification [GO:0007379]; smoothened signaling pathway [GO:0007224]; wing disc anterior/posterior pattern formation [GO:0048100]
|
cell surface [GO:0009986]; cytoneme [GO:0035230]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
coreceptor activity [GO:0015026]; hedgehog family protein binding [GO:0097108]; heparin binding [GO:0008201]; patched binding [GO:0005113]; protein homodimerization activity [GO:0042803]
|
PF00041;PF13895;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, IHOG family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9VM64, ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc). {ECO:0000250|UniProtKB:Q9VM64}.
|
Drosophila yakuba (Fruit fly)
|
B4P0E1
|
FICD_DROYA
|
MGTEAEQPSPPSPPAQQQEQTNPPLWNAQNQKPARLYRLVLFFIAGSLAAWTIHALSNSNLVWKLRQLHHLPTAHYLQTRDEFAVYSVEELNAFKEIYDKSVSDSVGASYTKDEQTSINEALVSLRMAQDMYLAGKDDKASRLFEHALALAPRHPEVLLRYGEFLEHSQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQTLDERRLQSLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHVPPGPGDLALLMQRFERWLNSEHSSTLHPVNYAALAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRNKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGALP
|
2.7.7.108; 3.1.4.-
| null |
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
|
plasma membrane [GO:0005886]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
|
PF02661;
|
1.10.3290.10;1.25.40.10;
|
Fic family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6};
| null | null | null | null |
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-250 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}.
|
Drosophila yakuba (Fruit fly)
|
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