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
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D4A280 | PAK5_RAT | MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKSCKESSINGLLEDFDNISVTRSNSLRKESPPTPDQGAASRIQGHSEENGFITFSQYSSESDTTTDYTTEKYRDRSLYGDDLDLYYRGSHAAKQNGHAMKMKHGDAYYPEMKPLKSDLARFPVDYHTHLDSLSKASEYGDLKWDYQRASSSSPLDYSFQLTPSRTAGTSRCSKESLAYSESDWGPSFDDYDRRPKSSYLHQTSPQPAMRQRSKSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVFSPPLSGSDTYPRGPTKLPQSQSKVGYSSSSHQYPGYHKASLYHHPSLQTSSQYISTASYLSSLSISSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLDNFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLKALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSMLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH | 2.7.11.1 | null | apoptotic process [GO:0006915]; cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; learning [GO:0007612]; locomotory behavior [GO:0007626]; memory [GO:0007613]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; phosphorylation [GO:0016310]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; synapse [GO:0045202] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00786;PF00069; | 3.90.810.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated when activated by CDC42/p21. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival. {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=2.7.11.1; 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; | null | null | null | null | FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4A2H2 | SPTC1_RAT | MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSRNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAAFASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVAEGLYMNTGTICPLPELVRLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKKKCQTIHKSLQGVSGLKVVGESLCPALHLQLEESTGSRERDMKLLQEIVEQCMNKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTDEELQRAAATIREAAQAVLL | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000250|UniProtKB:O15269}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35704}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35704}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine + CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:65073; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:71007; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676; Evidence={ECO:0000250|UniProtKB:O15269}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:71008; Evidence={ECO:0000250|UniProtKB:O15269}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680; Evidence={ECO:0000250|UniProtKB:O15269}; | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:O15269}. | null | null | FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or SPTLC3 forms the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity). {ECO:0000250|UniProtKB:O15269, ECO:0000250|UniProtKB:O35704}. | Rattus norvegicus (Rat) |
D4A2Z8 | DHX36_RAT | MSYDYHQSWSRDGGPRGSGQGSGGGGGGSRGSGGGGGGRGGRGRHPAHLKGREIGLWYAKKQTQKNKEAERQERAVVHMDERREEQIVQLLNSVQAKNDKDSEAQISWFAPEDHGYGTEVSSEKKINSEKKLDNQEKKLLNQEKKTYRITDKSYIDRDSEYLLQQNEPNLGLDQQLLEDLQKKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGNGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVVEYLLEDIIEKIRYFPEQKEHRSQFKRGFMQGHVNRQEKEEKEAIYKERWPAYIKELQTRYSASTIDVLEMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDRFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFLSRLMDPPSDEAVVLSIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKETRSDHLTVVNAFEGWEEAKRRGFRYEKDYCWEYFLSSNTLQMLHNMKGQFAEHLLGAGFVSSRSPKDPKANINSDNEKIIKAVICAGLYPKVAKIRLNLGKKRKMVKVHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCLLFFGGDISIQKDKDQEIIAVDEWIVFQSPERIAHLVKGLRKELDILLQEKIECPHPVDWNDTKSRDCAVLSAILDLIKTQEKAIPRNLPPRSQDGYYS | 3.6.4.12; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q05B79}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cell differentiation [GO:0030154]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; cellular response to UV [GO:0034644]; defense response to virus [GO:0051607]; G-quadruplex DNA unwinding [GO:0044806]; innate immune response [GO:0045087]; negative regulation of translation [GO:0017148]; ossification [GO:0001503]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cardioblast differentiation [GO:0051891]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of gene expression [GO:0010628]; positive regulation of hematopoietic progenitor cell differentiation [GO:1901534]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of intracellular mRNA localization [GO:1904582]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of myeloid dendritic cell cytokine production [GO:0002735]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of telomere maintenance [GO:0032206]; positive regulation of telomere maintenance via telomere lengthening [GO:1904358]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of embryonic development [GO:0045995]; regulation of mRNA stability [GO:0043488]; regulation of transcription by RNA polymerase III [GO:0006359]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; spermatogenesis [GO:0007283]; telomerase RNA stabilization [GO:0090669] | axon [GO:0030424]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; G-quadruplex DNA binding [GO:0051880]; G-quadruplex RNA binding [GO:0002151]; histone deacetylase binding [GO:0042826]; magnesium ion binding [GO:0000287]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; pre-miRNA binding [GO:0070883]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; single-stranded DNA binding [GO:0003697]; telomerase RNA binding [GO:0070034]; transcription cis-regulatory region binding [GO:0000976] | PF00270;PF21010;PF04408;PF00271;PF07717; | 1.20.120.1080;3.40.50.300; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion {ECO:0000250|UniProtKB:Q8VHK9}. Perikaryon {ECO:0000269|PubMed:23651854}. Cell projection, dendrite {ECO:0000269|PubMed:23651854}. Cell projection, axon {ECO:0000269|PubMed:23651854}. Note=Predominantly localized in the nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with DDX5 in nucleolar caps upon transcription inhibition. Accumulates and colocalized with TIA1 in cytoplasmic stress granules (SGs) in an arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into and out of SGs in an ATPase-dependent manner (By similarity). Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that translocates to the mitochondria upon poly(I:C) stimulation (By similarity). {ECO:0000250|UniProtKB:Q8VHK9, ECO:0000250|UniProtKB:Q9H2U1}. | 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=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9H2U1}; 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; Evidence={ECO:0000250|UniProtKB:Q9H2U1}; | null | null | null | null | FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (By similarity). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:23651854). G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA) (By similarity). Plays a role in genomic integrity. Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (By similarity). Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (By similarity). Plays a role in post-transcriptional regulation. Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment (PubMed:23651854). Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size (PubMed:23651854). Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability. Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression. Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively. Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation. Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Required for the early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification (By similarity). {ECO:0000250|UniProtKB:Q05B79, ECO:0000250|UniProtKB:Q8VHK9, ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:23651854}. | Rattus norvegicus (Rat) |
D4A3K5 | H11_RAT | MSETAPVPQPASVAPEKPAATKKTRKPAKAAVPRKKPAGPSVSELIVQAVSSSKERSGVSLAALKKSLAAAGYDVEKNNSRIKLGLKSLVNKGTLVQTKGTGAAGSFKLNKKAESKASTTKVTVKAKASGAAKKPKKTAGAAAKKTVKTPKKPKKPAVSKKTSSKSPKKPKVVKAKKVAKSPAKAKAVKPKAAKVKVTKPKTPAKPKKAAPKKK | null | null | chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; positive regulation of receptor-mediated endocytosis [GO:0048260]; spermatogenesis [GO:0007283] | cell surface [GO:0009986]; chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634]; vesicle [GO:0031982] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; heparin binding [GO:0008201]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000250|UniProtKB:P43275}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}. Note=Mainly localizes in euchromatin. {ECO:0000250}. | null | null | null | null | null | FUNCTION: H1 histones bind to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. H1 histones are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4A4D7 | E2F7_RAT | MEVNCLTLKDLISPRQTRLDFAVEDAETAQKENIFVDRSRMTPKTPMKNEPIDLSKQRIFTPERSPITPVKLVDRQPQVEPWTPTANLKMLISAASPDIRDREKKKELFRPIENKGDAFVNSLQLDVVGDSAVDDYEKRRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRTLQRLGEEQKYEEQMACLQQKELDLMEYRFGERRKDGSPDPRDQHLLDFSESDYPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDTPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSIDEELLDVSASVLPELKKETYGQIRVCAKERLARYGSFNTVQTSEKIQRKVNSEPSSPQGGKQGPAYSLEIGSLAAIYRQKVEDSSQGEAFVNKRAAPPASVLDPTLPVDSEYCVKPLAQPVFSVAQTDLQAFSAQNGLNGQVGVPVPSAASDAETLKSALLASQPLVYVPSTSLFMLYGSVQEALSPESRSEEDGSGSDVPADLSLAPTAQKRLCEERNPLEDDEPAVKRQSREFEDSPLSLVMPKKPSNSTDLAFPVTTGNGRATPLEDACVKGQLPAAEDASGRAVPNGFIASECGNPSRNPDTEKSSNDNEITKDPSLLQYLYVQSPAGLNGFNMLLPGGQTPHAVAPSSAAMPSFGVPCMFLPSPGLGPFPVLYSPAIPGPISSAPGTLPNTGPMNFGLSTLASASHLLISPAAMVNPKSSTLPSADPQLRCQPPLNPNPVMPGSHGVIHPESPGYMRHPVSMVKAEQSPAPATPKSIQRRHRETFFKTPGSLGDPAFRRERNQSRNTSSAQRRLEISSSGPD | null | null | chorionic trophoblast cell differentiation [GO:0060718]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; hepatocyte differentiation [GO:0070365]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cytokinesis [GO:0032466]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of transcription by RNA polymerase II [GO:0000122]; placenta development [GO:0001890]; positive regulation of DNA endoreduplication [GO:0032877]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; sprouting angiogenesis [GO:0002040]; trophoblast giant cell differentiation [GO:0060707] | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837] | PF02319; | 1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4A4K3 | BAKOR_RAT | MASPSGKGSWTPEAPGFGPRALAPDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLHILELTSVIFPMDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFCGENLSKQRLTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVSPHSEHLGRSGPFEVRADLEESMEFVDPGVAGESDVSGDERVSDEETDLGTDWENLPSPRFCDIPSQPVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR | null | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; autophagosome membrane docking [GO:0016240]; autophagy [GO:0006914]; cellular response to glucose starvation [GO:0042149]; cellular response to starvation [GO:0009267]; early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; negative regulation of protein phosphorylation [GO:0001933]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; positive regulation of protein phosphorylation [GO:0001934]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of macroautophagy [GO:0016241]; regulation of protein phosphorylation [GO:0001932]; regulation of triglyceride metabolic process [GO:0090207]; response to mitochondrial depolarisation [GO:0098780] | autophagosome [GO:0005776]; axoneme [GO:0005930]; endoplasmic reticulum membrane [GO:0005789]; extrinsic component of omegasome membrane [GO:0097629]; extrinsic component of phagophore assembly site membrane [GO:0097632]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; phosphatidylinositol 3-kinase complex, class III [GO:0035032] | GTPase binding [GO:0051020]; phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; protein-membrane adaptor activity [GO:0043495] | PF10186; | null | ATG14 family | PTM: Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14 aggregation and loss of interaction with STX17. {ECO:0000250|UniProtKB:Q6ZNE5}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZNE5}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions (By similarity). Following autophagy stimuli, such as starvation or rapamycin induction, predominantly detected in cytoplasmic foci, identified as isolation membranes and autophagosomes (By similarity). Accumulates on highly curved PtdIns(3)P enriched autophagic membrane via its BATS domain to sense and maintain membrane curvature (By similarity). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000250|UniProtKB:Q8CDJ3}. | null | null | null | null | null | FUNCTION: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Modulates the hepatic lipid metabolism (By similarity). {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000250|UniProtKB:Q8CDJ3}. | Rattus norvegicus (Rat) |
D4A523 | NLRP3_RAT | MKMMSVRCKLAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKKDQPEWNDACTSNLSMVCQEDSLEEEWIGLLGYLSRISICKKKKDYCKIYRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRTKMWDRPMSSLKLELLFEPEDEHLEPVHTVVFQGAAGIGKTILARKIMLDWALGKLFKDKFDYLFFIHCREVSLRAPKSLADLIISCWPDPNPPVCKILCKPSRILFLMDGFDELQGAFDEHIEEVCTDWQKAVRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQTSKTTTAVYVFFLSSLLQSRGGIEEHLFSAYLPGLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSFSHMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSDLLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQEEDFVQSAMGHFPKIEINLSTRMDHVVSSFCIKNCHRVKTLSLGFLHNSPKEEEEEKRGSQPLDQVQCVFPDPHVACSSRLVNCCLTSSFCRGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFGVRLLCVGLKHLLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNSGLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCSLTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLCEVLKQQGCLLQSLQLGEMYLNCETKRTLEALQEEKPELTVVFEISW | 3.6.4.- | null | acute inflammatory response [GO:0002526]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to peptidoglycan [GO:0071224]; cellular response to virus [GO:0098586]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; detection of biotic stimulus [GO:0009595]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; leukocyte migration involved in inflammatory response [GO:0002523]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; NLRP3 inflammasome complex assembly [GO:0044546]; positive regulation of cytokine production involved in immune response [GO:0002720]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of interleukin-5 production [GO:0032754]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of T-helper 17 cell differentiation [GO:2000321]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; positive regulation of T-helper 2 cell differentiation [GO:0045630]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type 2 immune response [GO:0002830]; protein homooligomerization [GO:0051260]; protein maturation [GO:0051604]; regulation of inflammatory response [GO:0050727]; response to ethanol [GO:0045471]; response to organic cyclic compound [GO:0014070] | canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; interphase microtubule organizing center [GO:0031021]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; molecular condensate scaffold activity [GO:0140693]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sequence-specific DNA binding [GO:0043565]; signaling adaptor activity [GO:0035591]; small molecule sensor activity [GO:0140299] | PF14484;PF13516;PF05729;PF17776;PF17779;PF02758; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: Phosphorylation by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-805 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation at Ser-5 in the pyrin domain inhibits homomultimerization of NLRP3 and activation of the NLRP3 inflammasome: dephosphorylation by protein phosphatase 2A (PP2A) promotes assembly of the NLRP3 inflammasome. Phosphorylation at Ser-293 by PKD/PRKD1 promotes NLRP3 inflammasome assembly (By similarity). Phosphorylation by ERK1/MAPK3 promotes NLRP3 inflammasome assembly (By similarity). Phosphorylation by BTK (at Tyr-134, Tyr-138 and Tyr-166) in the region that mediates binding to phosphatidylinositol phosphate, promotes relocalization of NLRP3 and assembly of the NLRP3 inflammasome. Phosphorylation at Tyr-860 inhibits NLRP3 inflammasome assembly: dephosphorylation by PTPN22 promotes inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Ubiquitination does not lead to degradation, but inhibits inflammasome activation. Deubiquitination is catalyzed by BRCC3 and associated with NLRP3 activation and inflammasome assembly. This process can be induced by the activation of Toll-like receptors (by LPS), through a non-transcriptional pathway dependent on the mitochondrial production of reactive oxygen species, and by ATP. Ubiquitinated by TRIM31 via 'Lys-48'-linked ubiquitination, leading to its degradation by the proteasome (By similarity). Ubiquitinated at Lys-689 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). Ubiquitinated by TRIM35 via 'lys-48' and 'Lys-63'-linked ubiquitination leading to inhibition of NLRP3 inflammasome activation (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; PTM: The disulfide bond in the pyrin domain might play a role in reactive oxygen species-mediated activation. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Palmitoylation by ZDHHC12 inhibits the NLRP3 inflammasome by promoting NLRP3 degradation by the chaperone-mediated autophagy pathway. Following palmitoylation, HSPA8/HSC70 recognizes and binds the KFERQ-like motifs on NLRP3 and promotes NLRP3 recruitment to lysosomes, where it is degraded via the chaperone-mediated autophagy pathway in a LAMP2-dependent process. Palmitoylation by ZDHHC5 enhances its binding to NEK7 leading to inflammasome assembly and activation. Depalmitoylated by ABHD17A. {ECO:0000250|UniProtKB:Q96P20}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes NLRP3 recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagy-dependent degradation. {ECO:0000250|UniProtKB:Q96P20}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome {ECO:0000250|UniProtKB:Q8R4B8}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8R4B8}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R4B8}. Mitochondrion {ECO:0000250|UniProtKB:Q8R4B8}. Secreted {ECO:0000250|UniProtKB:Q8R4B8}. Nucleus {ECO:0000250|UniProtKB:Q8R4B8}. Note=In macrophages, under resting conditions, mainly located in the cytosol and on membranes of various organelles, such as endoplasmic reticulum, mitochondria and Golgi: forms an inactive double-ring cage that is primarily localized on membranes. Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes for the formation of an active inflammasome complex. Recruited to dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). After the induction of pyroptosis, inflammasome specks are released into the extracellular space where they can further promote IL1B processing and where they can be engulfed by macrophages. Phagocytosis induces lysosomal damage and inflammasome activation in the recipient cells. In the Th2 subset of CD4(+) helper T-cells, mainly located in the nucleus. Nuclear localization depends upon KPNA2. In the Th1 subset of CD4(+) helper T-cells, mainly cytoplasmic. {ECO:0000250|UniProtKB:Q8R4B8}. | 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; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8R4B8}; | null | null | null | null | FUNCTION: Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.; FUNCTION: Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF. {ECO:0000250|UniProtKB:Q8R4B8}. | Rattus norvegicus (Rat) |
D4A612 | ELOV2_RAT | MFGPRDSRVRGWFLLDSYLPTFTLTIVYLLSIWLGNKYMKNRPALSLRGILTLYNLGITLLSAYMLVELVLSSWEGGYNLQCQNLDSAGEGDIRVAKVLWWYYFSKLVEFLDTIFFVLRKKTSQITFLHVYHHASMFNIWWCVLNWIPCGQSFFGPTLNSFIHILMYSYYGLSVFPSMHRYLWWKKYLTQAQLVQFVLTITHTLSAVVKPCGFPFGCLIFQSSYMMTLVILFLNFYIQTYRKKPMKKEMPEGAAGKEVKNGFPKAHSIAANGVTDKKVQ | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]; very long-chain fatty acid metabolic process [GO:0000038] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL2 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728; Evidence={ECO:0000305|PubMed:22216341}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + H(+) + malonyl-CoA = (9Z,12Z,15Z,18Z,21Z)-3-oxotetracosapentaenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36491, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73870, ChEBI:CHEBI:73871; Evidence={ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36492; Evidence={ECO:0000305|PubMed:22216341}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862, ChEBI:CHEBI:73863; Evidence={ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484; Evidence={ECO:0000305|PubMed:22216341}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000269|PubMed:22216341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000305|PubMed:22216341}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + H(+) + malonyl-CoA = (9Z,12Z,15Z,18Z)-3-oxotetracosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73856, ChEBI:CHEBI:73857; Evidence={ECO:0000269|PubMed:22216341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36480; Evidence={ECO:0000305|PubMed:22216341}; | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}. | Rattus norvegicus (Rat) |
D4A631 | BIG1_RAT | MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGSAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQHHLLQSPVSHHEPESPHLRYLPPQTVDHIAQEQEGDLDPQTHDVDKSLQDDIEPENGSDISSAENEQTEADQATAAETLSKDDVLCDGECEEKPQDIVQSIVEEMVDIIVGDMGEGTAVSASADGNAGAVEDGSDSENVQANGIPGTPISAAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQAGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTDVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTSGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCVINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAAPPSPSAMSEKQLDAISQKSVDIHDSAQPRSSDNRQQAPLVSVSPASEEVSKGRPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINKQ | null | null | endomembrane system organization [GO:0010256]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; neuron projection development [GO:0031175]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of wound healing [GO:0090303]; protein glycosylation [GO:0006486]; protein transport [GO:0015031]; regulation of ARF protein signal transduction [GO:0032012]; regulation of establishment of cell polarity [GO:2000114] | cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802] | guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11; | null | PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11809827}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11809827}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment (By similarity). PRKAR1B. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250|UniProtKB:Q9Y6D6}. | Rattus norvegicus (Rat) |
D4A693 | AZIN2_RAT | MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLAELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDALGLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVDGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQACRVTYAMSRLAWEALQGQLLPAEEDQDAEGVCKPLSCGWEITDSLCVGPVFTPASIM | null | null | negative regulation of protein catabolic process [GO:0042177]; ornithine metabolic process [GO:0006591]; positive regulation of catalytic activity [GO:0043085]; positive regulation of polyamine transmembrane transport [GO:1902269]; putrescine biosynthetic process from ornithine [GO:0033387]; trans-Golgi network membrane organization [GO:0098629] | axon [GO:0030424]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; granular vesicle [GO:1990005]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; trans-Golgi network [GO:0005802]; transport vesicle [GO:0030133] | catalytic activity [GO:0003824]; ornithine decarboxylase activator activity [GO:0042978] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, ODC antizyme inhibitor subfamily | PTM: Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizymes. May also be degraded through the lysosomal degradative pathway in a proteasomal-independent manner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19718454}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic granule {ECO:0000269|PubMed:19718454}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN) (By similarity). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking. {ECO:0000250|UniProtKB:Q8BVM4, ECO:0000250|UniProtKB:Q96A70}. | Rattus norvegicus (Rat) |
D4A6D8 | LRRT1_RAT | MDFLLLGLCLHWLLRRPSGVVLCLLGACFQMLPAAPSGCPGQCRCEGRLLYCEALNLTEAPHNLSGLLGLSLRYNSLSELRAGQFTGLMQLTWLYLDHNHICSVQGDAFQKLRRVKELTLSSNQITELANTTFRPMPNLRSVDLSYNKLQALAPDLFHGLRKLTTLHMRANAIQFVPVRIFQDCRSLKFLDIGYNQLKSLARNSFAGLFKLTELHLEHNDLIKVNFAHFPRLISLNSLCLRRNKVAIVVSSLDWVWNLEKMDLSGNEIEYMEPHVFETVPYLQSLQLDSNRLTYIEPRILNSWKSLTSITLAGNLWDCGRNVCALASWLSNFQGRYDANLQCASPEYAQGEDVLDAVYAFHLCEDGAEPTSGHLLSAAVTNRSDLAPPESSATTLVDGGEGLHDSTLEPITVAIPGGEHAENAVQIHKVVTGTMALIFSFLIVVLVLYVSWKCFPASLRQLRQCFVTQRRKQKQKQTMHQMAAMSAQEYYVDYKPNHIEGALVIINEYGSCTCHQQPARECEV | null | null | establishment of localization in cell [GO:0051649]; exploration behavior [GO:0035640]; locomotory behavior [GO:0007626]; long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; protein localization to synapse [GO:0035418]; receptor internalization [GO:0031623]; regulation of postsynaptic density assembly [GO:0099151]; regulation of presynapse assembly [GO:1905606]; synapse organization [GO:0050808] | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634] | null | PF13855; | 3.80.10.10; | LRRTM family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19285470}; Single-pass type I membrane protein {ECO:0000269|PubMed:19285470}. Postsynaptic cell membrane {ECO:0000269|PubMed:19285470}; Single-pass type I membrane protein {ECO:0000269|PubMed:19285470}. | null | null | null | null | null | FUNCTION: Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level. {ECO:0000269|PubMed:19285470}. | Rattus norvegicus (Rat) |
D4A6L0 | MGLYR_RAT | MGAMAYSLLLCLLLAHLGLGEVGASLDPSERPDSSRERTSRGKQHGQQLPRASAPDPSIPWSRSTDGTILAQKLAEEVPMDVASYLYTGDFHQLKRANCSGRYELAGLPGKSPSLASSHPSLHGALDTLTHATNFLNMMLQSNKSREQTVQDDLQWYQALVRSLLEGEPSISRAAITFSTESLSTPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRPHLHRRGSNQGPRGLGHSWRRRDGLGGDRSHVKWSPPFLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYQCVCKAGFYHPRVFSVNNFQRRGPDHHFSGSTKDVSEEAHVCLPCREGCPFCADDRPCFVQEDKYLRLAIISFQALCMLLDFVSMLVVYHFRKAKSIRASGLILLETILFGSLLLYFPVVILYFEPSTFRCILLRWVRLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVIVLVVFWFLVGWTSSMCQNLERDILLVGQGQTSDNLTFNMCLIDRWDYMTAVAEFLFLLWGIYLCYAVRTVPSAFHEPRYMAVAVHNELIITAIFHTIRFVLASRLQPDWMLMLYFAHTHLTVTVTIGLLLIPKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKEGTDHSAAKGTGLVRKNPTESSGNTGRPKEESLKNRVFSLKKSHSTYDHVRDQTDESSSLPTESQEEEVTENSTLESLSSKKLTQKVKEDSEAESTESVPLVCKSASAHNLSSEKKPGHPRTSMLQKSLSVIASAKEKTLGLAGKTQTLVMEDRAKSQKPQPKDRETNRKYSNSDNTETNPNSNHTEELRKPQKSGIMKQQRVNLPTANPDASSSTTQIKDNFDIGEVCPWEVYDLTPGPVPSEPKAQKHVSIAASEVEQNPASFSKEKSHHKPKAAEGLYQANHKSIDKTEVCPWESHGQSPLEDENRLISKTPVLPGRAREENGSQLYTTNMCAGQYEELPPKAVASKVENENLNQMGDQEKQTSSSVDIIPGSCISSNNSPQPLTSRAEVCPWEFEPLEQPNAERIVALPASSALSASKIPGPRK | null | null | brain development [GO:0007420]; cognition [GO:0050890]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of neurotransmitter secretion [GO:0001956]; protein localization to plasma membrane [GO:0072659]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of synapse organization [GO:0050807] | cell projection [GO:0042995]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] | enzyme activator activity [GO:0008047]; G protein-coupled glycine receptor activity [GO:0160079]; transmembrane signaling receptor activity [GO:0004888] | PF00003; | 3.30.450.20; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T848}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Nucleus {ECO:0000250|UniProtKB:Q5T848}. Note=Mainly localizes to the postsynaptic membrane, with a small portion to the presynaptic membrane (By similarity). Trafficks between the nucleus and the cell membrane; it is unclear how a multi-pass membrane protein can traffick between the nucleus and the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q5T848, ECO:0000250|UniProtKB:Q8C419}. | null | null | null | null | null | FUNCTION: Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Glycine-binding changes the conformation of the intracellular surface, inhibiting the GTPase activator activity of the RGS7-GNB5 complex, promoting G protein alpha subunits into their active GTP-bound form and regulating cAMP levels. Also able to bind taurine, a compound closely related to glycine, but with a two-fold lower affinity. Glycine receptor-dependent regulation of cAMP controls key ion channels, kinases and neurotrophic factors involved in neuronal excitability and synaptic transmission (By similarity). Plays a pivotal role in regulating mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Also involved in spatial learning by regulating hippocampal CA1 neuronal excitability. Acts as a synaptic organizer in the hippocampus, required for proper mossy fiber-CA3 neurocircuitry establishment, structure and function: induces presynaptic differentiation in contacting axons via its interaction with GPC4. In addition to glycine, may also act as a receptor for osteocalcin (BGLAP) hormone: osteocalcin-binding initiates a signaling response that prevents neuronal apoptosis in the hippocampus and regulates the synthesis of neurotransmitters (By similarity). {ECO:0000250|UniProtKB:Q5T848, ECO:0000250|UniProtKB:Q8C419}. | Rattus norvegicus (Rat) |
D4A702 | SYNP2_RAT | MGTGDFICISMTGGAPWGFRLQGGKEEKQPLQVAKIRSQSKASDSGLCVGDEVVSINGNPCADLTYPEVIKLMESITDSLHLLIKRPTSGTSEALDSETENTNHQHLPHGGPMESTTLQIQHAAKTQGKDFLLASVQTSAPRTEDQGNAWGYAECTTEDQVSQMPGSQEGHLVEEVILRKKPEAGQPGHVVELQLSLSKERQRCTSDPIVTLLGNEKFKSPDPDWGTQHGRTVHINSIPAPEKADTSLTSGTTVQTSSGRELTVIQGRDPGGTGLPQVEVILDCSDRLKAEECRLQAGRGCVASPVEGGRSEAPPSLVSFAVSSEGTEQGEDQRSGKDQGRPHKHRARHARLRRSESLSEKQVKEAKSKCKSIALLLTDAPNPNSKGVLMFKKRRRRARKYTLVSYGTGELEREEEEEDQEAGDKDEISDLAFLGTSESEVDEELLSDVDDNTQVVNFDWDSGLVDIEKRLNRGDKMEMLPDTTGKGALMFAKRRERMEQFTAQNEEEKTGGLAGGGSDALQTDGLRTMTSYQRKEESVRMQSSVSESSFQMGRSLGSVPQQNGFSGVSETAGPQRMIPMNRTAKPFLGSVNQTAAPFSPTQSVTSPIPDFPAPPPYSAVSPPPEAFSRGISSPVAGPAQPPPWPQPAPWSQPAFYDSSEQIASRDERIAVPAKRTGILQEAKRRGTTKPMFTFKETKVSPNPELLSLLQNAEGKRGTGAGGDSGPEEDYLSLGAEACNFMQSSAKQKTPPPVAPKPAVKTSSSSQPVAPVSPVWSPGVAPAQGPAFSTTNPPNPPQVTAVSSIKIAQPTCPPARPASALNLAGPFKGPQAAVVSHNYTPKPSAPTPLVNAAPAGAGGPSNELPGMSGKGAQLFAKRQSRMEKYVVDSDTVQAHTVRAQSPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPLAAIKSQPPGAQASKTSKKKGKKPLNTLDVMKHQPYQLNASLFTFQPPDSKDGLPQKSTVKVSSVAPAMKQALPPRQADIGSPTNAKASSVYSVPAYTSQPNFFAEATSPVSASPVPVSVPTSPKQETTSTSYFVAPRPKFSAKKSGVTVQENWRSLSLPGRAAPPIMSAPPWLCQPAYSYSSKPTLEQEKANKRPTPWEAAAKSPLGLVDEAFRPRNIEESIVANVVSAARRKVFAGSQEDWKERLSFVPQTQKTSMSFSERREYNVPSPVNSHVSSHSLYSSQLPYVCYRKESRNDLKAMSMDTRSEYCLPLGGYDYNPHPRGWRHQP | null | null | autophagosome assembly [GO:0000045]; chaperone-mediated autophagy [GO:0061684]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of cell migration [GO:0030335] | actin cytoskeleton [GO:0015629]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; stress fiber [GO:0001725]; Z disc [GO:0030018] | 14-3-3 protein binding [GO:0071889]; actin binding [GO:0003779]; alpha-actinin binding [GO:0051393]; filamin binding [GO:0031005]; muscle alpha-actinin binding [GO:0051371]; protein-macromolecule adaptor activity [GO:0030674] | PF00595; | 2.30.42.10; | Synaptopodin family | PTM: Phosphorylated by PKA, and by CaMK2 at multiple sites. Dephosphorylated by calcineurin at Ser-558 and Thr-605; abrogating interaction with YWHAB and impairing nuclear import. {ECO:0000250|UniProtKB:Q91YE8}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm {ECO:0000250|UniProtKB:Q91YE8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UMS6}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11673475}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UMS6}. Note=Shuttles between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. In undifferentiated myoblasts strongly expressed in the nucleus, after induction of myotube differentiation is located to both nucleus and cytoplasm along acting filaments, and in differentiated myotubes is located at the Z lines. Upon stress redistributes from cytoplasm of myoblasts and myotubes to the nucleus. Nuclear import is KPNA2-dependent and promoted by phosphorylation by PKA and/or CaMK2, and inhibition of calcineurin. The nuclear export is XPO1-dependent. Localized in a fiber-like pattern, partly overlapping with filamentous actin (By similarity). {ECO:0000250|UniProtKB:Q91YE8, ECO:0000250|UniProtKB:Q9UMS6}. | null | null | null | null | null | FUNCTION: Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks. At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines (By similarity). Involved in autophagosome formation. May play a role in chaperone-assisted selective autophagy (CASA) involved in Z lines maintenance in striated muscle under mechanical tension; may link the client-processing CASA chaperone machinery to a membrane-tethering and fusion complex providing autophagosome membranes (PubMed:23434281). Involved in regulation of cell migration. May be a tumor suppressor (By similarity). {ECO:0000250|UniProtKB:Q91YE8, ECO:0000250|UniProtKB:Q9UMS6, ECO:0000269|PubMed:23434281}. | Rattus norvegicus (Rat) |
D4A734 | MOT12_RAT | MTKITRVGSASPPDGGWGWMIVAGCFLVTICTRAVTRCISIFFVEFQTYFAQDYSQTAWIHSIVDCMTMLCAPLGSVVSNQLSCQAGIMLGGLLASTGLILGSFATSLKHLYLSLGVLTGLGFALCYSPAIAMVGKYFSRRKAFAYGIAMSGSGIGTFILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRPITLKEDPSGPEKSHDRDAQREDCKQASPYSPLTKEWTETRLCCSLQQGYGFLLMSDFVVLAVSVLFMAYGCSPLFVYLVPYALSVGVSHHQAAFLMSILGVIDIVGNITFGWLTDRRCLKNYRYVCYLFAVALDGLCYLCLPMLQSFPLLVPFSCTFGYFDGAYVTLIPVVTAEIVGTTSLSSALGVVYFLHAVPYLVSPPIAGWLVDTTGSYTAAFLLCGFAMIFSSILLGFAKIAKRMKRTQVPFLVKDSDPKLHLWTNGSVAYSIAKELDQKDEESLAKARTGCNLT | null | null | creatine transmembrane transport [GO:0015881]; creatinine metabolic process [GO:0046449] | basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | creatine transmembrane transporter activity [GO:0005308]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; uniporter activity [GO:0015292] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6ZSM3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:34075817}; Multi-pass membrane protein {ECO:0000255}. Note=Localized on the sinusoidal membrane of the hepatocyte. Colocalized with SLC6A13 in hepatocytes around the portal vein, (PubMed:34075817). Interaction with isoform 2 of BSG is required for its localization to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q6ZSM3, ECO:0000269|PubMed:34075817}. | CATALYTIC ACTIVITY: Reaction=creatine(in) = creatine(out); Xref=Rhea:RHEA:73043, ChEBI:CHEBI:57947; Evidence={ECO:0000269|PubMed:32781157, ECO:0000269|PubMed:34075817}; CATALYTIC ACTIVITY: Reaction=guanidinoacetate(in) = guanidinoacetate(out); Xref=Rhea:RHEA:73047, ChEBI:CHEBI:57742; Evidence={ECO:0000269|PubMed:32781157}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.38 mM for guanidinoacetate {ECO:0000269|PubMed:32781157}; KM=240 uM for creatinine {ECO:0000269|PubMed:32781157}; | null | null | null | FUNCTION: Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na(+), Cl(-), or pH. Contributes to the process of creatine biosynthesis and distribution. {ECO:0000269|PubMed:32781157, ECO:0000269|PubMed:34075817}. | Rattus norvegicus (Rat) |
D4A7E1 | BATF_RAT | MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP | null | null | defense response to protozoan [GO:0042832]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; hematopoietic stem cell differentiation [GO:0060218]; isotype switching [GO:0045190]; lymphoid progenitor cell differentiation [GO:0002320]; myeloid dendritic cell differentiation [GO:0043011]; positive regulation of cytokine production [GO:0001819]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; T-helper 17 cell differentiation [GO:0072539]; T-helper 17 cell lineage commitment [GO:0072540]; T-helper 2 cell differentiation [GO:0045064] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00170; | 1.20.5.170; | BZIP family | PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4A7H1 | SL9A9_RAT | MAGQLRLTSGKDEDHFQHQGAVELLAFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIDSGTVYNCGKLLFSPSTLLVNITDQVYEYKYQREINQHNISPHQGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCVVIGLIMYGFVKAMVHAGQLKSGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDTAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLREFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSSDSKLRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKQKIPWNFQHMMMFSGLRGAIAFALAIRNTESQPKQMMFTTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDESLKEEPSSQQEANKVDKDMTKTESAQLFRMWYGFDHKYLKPILTHSGPPLTTTLPAWCGPVSRLLTSPQAYGEQLKEDDVECIVNQDELAMNYQEQSPTSSSPATKLALDQKSSGLTLGKENIYEGDLGLGGYELKLEQTRGQPQMD | null | null | defense response to bacterium [GO:0042742]; phagosome maturation [GO:0090382]; potassium ion transmembrane transport [GO:0071805]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725] | early endosome [GO:0005769]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; late endosome membrane [GO:0031902]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038] | potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Cell membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F7B113}. Note=Localized to the plasma membrane in inner ear hair cell bundle. {ECO:0000250|UniProtKB:Q8BZ00}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q8BZ00}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q8BZ00}; | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (By similarity). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (By similarity). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity). {ECO:0000250|UniProtKB:Q8BZ00, ECO:0000250|UniProtKB:Q8IVB4}. | Rattus norvegicus (Rat) |
D4A7K7 | GP183_RAT | MANNFTTPLAASHGNNCDLYAHHSTARILMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSMNLVISDILFTTALPTRIVYYALGFDWRIGDALCRITALLFYINTYAGVNFMTCLSIDRFFAVVHPLRYNKIKRIEYAKGICVFVWILVFAQTLPLLLKPMSKQEADKTTCMEYPNFEGTASLPWILLGACLLGYVLPLAIILLCYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIGVFVLCFTPYHVAIMQHMVKTLYAPGALGCGVRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMKMLKRQVSVSISSAVRSAPEENSREMTESQMMIHSKASNGR | null | null | adaptive immune response [GO:0002250]; B cell activation involved in immune response [GO:0002312]; cell chemotaxis [GO:0060326]; dendritic cell chemotaxis [GO:0002407]; dendritic cell homeostasis [GO:0036145]; G protein-coupled receptor signaling pathway [GO:0007186]; humoral immune response [GO:0006959]; leukocyte chemotaxis [GO:0030595]; mature B cell differentiation involved in immune response [GO:0002313]; osteoclast differentiation [GO:0030316]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of astrocyte chemotaxis [GO:2000458]; T cell chemotaxis [GO:0010818]; T follicular helper cell differentiation [GO:0061470] | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; oxysterol binding [GO:0008142] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32249}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (By similarity). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity). Guides B-cell movement along the B-cell zone-T-cell zone boundary and later to interfollicular and outer follicular regions (By similarity). Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses (By similarity). Collaborates with CXCR5 to mediate B-cell migration; probably by forming a heterodimer with CXCR5 that affects the interaction between of CXCL13 and CXCR5 (By similarity). Also acts as a chemotactic receptor for some T-cells upon binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular helper T (Tfh) cells differentiation by positioning activated T-cells at the follicle-T-zone interface, promoting contact of newly activated CD4 T-cells with activated dendritic cells and exposing them to Tfh-cell-promoting inducible costimulator (ICOS) ligand (By similarity). Expression in splenic dendritic cells is required for their homeostasis, localization and ability to induce B- and T-cell responses: GPR183 acts as a chemotactic receptor in dendritic cells that mediates the accumulation of CD4(+) dendritic cells in bridging channels (By similarity). Regulates migration of astrocytes and is involved in communication between astrocytes and macrophages (By similarity). Promotes osteoclast precursor migration to bone surfaces (By similarity). Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha (By similarity). Signals constitutively also via MAPK1/3 (ERK1/2) (By similarity). {ECO:0000250|UniProtKB:P32249, ECO:0000250|UniProtKB:Q3U6B2}. | Rattus norvegicus (Rat) |
D4A7P2 | LRRT2_RAT | MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILSSLRSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQGPYSEYEPTHEGPFIIINGYGQCKCQQLPYKECEV | null | null | long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; synapse organization [GO:0050808] | excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; Schaffer collateral - CA1 synapse [GO:0098685] | neurexin family protein binding [GO:0042043] | PF13855; | 3.80.10.10; | LRRTM family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane; Single-pass type I membrane protein. Note=Localized to excitatory synapses. | null | null | null | null | null | FUNCTION: Involved in the development and maintenance of excitatory synapses in the nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B. {ECO:0000269|PubMed:19285470, ECO:0000269|PubMed:20064388, ECO:0000269|PubMed:30100184}. | Rattus norvegicus (Rat) |
D4A7T3 | BRDT_RAT | MSLPSRQMAIVNPPPPEYINAKKTGRLTNQLQFLQRVVLKALWKHSFSWPFQQPVDAAKLKLPDYYTIIETPMDLSTIKKRLENRYYEKASECVGDFNTMFSNCYLYNKPGDDIVVMAQALEKLFMQKLSQMPQEEQIVGGKERMKKDIQQKTAVSSAKEQTPSKSAENVFKRQEIPAGFPDVCLSPLNMAQEAPPTCDSQTVVQITKGVKRRADTTTPTTSSAKASSESPPPLREAKPANAPVKENTVKSVLPDSQQQHRVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDVDALGLHNYYDIVKNPMDLGTIKGKMDKQEYKDACEFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFEMHFAKIPDEPVESMRACHLTTNSAKALSRESSSEASSGDCSSEDSEDERVQRLAKLQEQLNAVHQQLQVLSQVPLRKLKKKNEKSKRAPKRKKVNRDENPKKKAKQMKQKEKAKSNQPKKKKPLLKLEEEDNAKPMNYDEKRQLSLDINKLPGDKLGRIVHIIQSREPSLRNSNPDEIEIDFETLKASTLRELEKYVLACLRKRSLKPHAKKVVRSKEELHSEKKLELERRLLDVNNQLNCRKRQTKRPAKVAVSPRPPLPPPPPPPPELASGSRLSDSSSSSSSSGSGSSSSSSSSSGSGSSSSDSSSSDSSDSEPEISPKFTGVKQNDLPSKENTKQIQCSVPDITSAETALVQQSTGPCGAPGKPPQQMPGCQVPHHLQATESTASVQTQPLAGDCKRVLHGPPVVHASAESHTVLELQCHAPVQKDIKIKNADSWKSLGKPVKASSVLKSSDELFNQFRKAAIEKEVKARTQEQIRKHLEHSAKDPKVSQESQREFGSGFTPESSSNKVQGRSHGEEQSEQQQLPSPSETQDISKLWLLKDRNLAREKEQERRRREAMAGTIDMTLQSDIMTMFENNFD | null | null | chromatin remodeling [GO:0006338]; male meiosis I [GO:0007141]; male meiotic nuclear division [GO:0007140]; mRNA processing [GO:0006397]; positive regulation of gene expression [GO:0010628]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]; sperm DNA condensation [GO:0035092]; spermatogenesis [GO:0007283] | chromatin [GO:0000785]; nucleus [GO:0005634] | histone binding [GO:0042393]; histone reader activity [GO:0140566]; lysine-acetylated histone binding [GO:0070577] | PF17035;PF17105;PF00439; | 1.20.1270.220;1.20.920.10; | BET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22215678}. Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q91Y44}. | null | null | null | null | null | FUNCTION: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin. {ECO:0000250|UniProtKB:Q91Y44}. | Rattus norvegicus (Rat) |
D4A7V9 | E2AK4_RAT | MAGGRGAAGRGPAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELRVKCPPTYPDVVPEIELKNTKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARQKEEQEQREILHEIQKRKEEIKEEKKRKEMAKQERLEITSLTNQDHASKRDPAGHRAAAFLHGGSPDFVGNGKARAHSSGRSRRERQYSVCSGEASPGSCDILYFCVGSADQLMVHKGKCVGSDEQLGKVVYNALETATGSFVLLYEWVLQWQKKMGPCLTSQEKEKIDKCKKQIQGAETEFSSLVKLSHPNIVRYFAMNSREEKDSIVVDILAEHISGISLAAHLSHSGPVPMHQLRKYTAQLLAGLDYLHRNSVVHKVLSTASVLVDAEGTVKITDYSISKRLADICKEDVFEQTRVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECEEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKMPLVEQSPEDSGGQDYIETIIPSNQLPSAAFFTETQRQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRQFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDYIPQAQNSSATGGKASGDTEELGSVEAAAPPPILSSSVEWSTSAERSNSARFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNEKDSRHEIEPSVTTEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFNAEGKQDDQAGDHVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIILFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFEDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANTDGKAYRTMMSQLFCQHSSPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTANSSLPTAETIYTIYEVIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGIAQLVKYSLKDLEEVVGLLKKLGVKLQVSINLGLVYKVQQHNGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQALGPVPTAVGVSIAIDKIFAAVLNMGEPVTVSSCDLLVVSAGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPTVSVISPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF | 2.7.11.1 | null | cell cycle [GO:0007049]; cellular response to amino acid starvation [GO:0034198]; cellular response to cold [GO:0070417]; cellular response to starvation [GO:0009267]; cellular response to UV [GO:0034644]; DNA damage checkpoint signaling [GO:0000077]; endoplasmic reticulum unfolded protein response [GO:0030968]; GCN2-mediated signaling [GO:0140469]; learning [GO:0007612]; long-term memory [GO:0007616]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation of CREB transcription factor activity [GO:0032792]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation [GO:0045947]; negative regulation of translational initiation in response to stress [GO:0032057]; neuron projection extension [GO:1990138]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of gene expression [GO:0010628]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of translational initiation in response to starvation [GO:0071264]; protein phosphorylation [GO:0006468]; regulation of cytoplasmic translational initiation in response to stress [GO:1990611]; regulation of feeding behavior [GO:0060259]; regulation of translational initiation [GO:0006446]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]; regulation of translational initiation in response to stress [GO:0043558]; response to endoplasmic reticulum stress [GO:0034976]; T cell activation involved in immune response [GO:0002286]; viral translation [GO:0019081] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tRNA binding [GO:0000049] | PF12745;PF00069;PF05773;PF13393; | 3.40.50.800;1.10.510.10;3.10.110.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Autophosphorylated; autophosphorylation on Thr-899 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT. {ECO:0000250|UniProtKB:Q9QZ05}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZ05}. | 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:Q9QZ05}; 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:Q9QZ05}; | null | null | null | null | FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By similarity). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (By similarity). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a role in feeding behavior to maintain amino acid homeostasis; contributes to the innate aversion toward diets of imbalanced amino acid composition (PubMed:15051816, PubMed:15774759). Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442, ECO:0000250|UniProtKB:Q9P2K8, ECO:0000250|UniProtKB:Q9QZ05, ECO:0000269|PubMed:15051816, ECO:0000269|PubMed:15774759}. | Rattus norvegicus (Rat) |
D4AA47 | AT8B1_RAT | MNTERDSETTFDEDSQPNDEVVPYSDDETEDELEDQGPAVEPEQNRVNREVEKKKETFRKDCTWQVKANDRKFHEQPHFMNTKFFCIKESKYASNAIKTYKYNALTFLPMNLFEQFKRAANFYFLILLILQAIPQISTLAWYTTLVPLLLVLGITAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKIIKWKDIQVGDVIRLKKNDFIPADILLLSSSEPNSLCYVETAELDGETNLKFKMALEITDQYLQIEDNLATFDGFIECEEPNNRLDKFTGTLFWRNQSFPLDADKILLRGCVIRNTDVCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIIIVLILVSAGLAIGHAYWEAQIGNYSWYLYDGENATPSYRGFLNFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKSRTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGTIYGDHRDASQHSHSKIELVDFSWNEFADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLSICHTVMVDRIDGQINYQAASPDEGALVNAARNFGFAFLARTQNTITVSELGTERTYSVLAILDFNSDRKRMSIIVRTPEGSIRLYCKGADTVIYERLHRMNPMKQETQDALDIFASETLRTLCLCYKEIEEKEFAEWNKKFMAASVASSNRDEALDKVYEEIERDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHTRMENQRNRGGVSAKFAPPAYEPFFPPGENRALIITGSWLNEILLEKKTKRSKILKLKFPRTEEERRMRSQSRRRLEEKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYSSLPVLLMGLLDQDVSDKLSLRFPGLYVVGQRDLLFNYKKFFVSLLHGVLTSMVLFFIPFGAYLQTVGQDGEAPSDYQSFAVTMASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWKRRQSVFRRGASSRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIIADGTAEYRRTVES | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | aminophospholipid transport [GO:0015917]; apical protein localization [GO:0045176]; bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; negative regulation of DNA-templated transcription [GO:0045892]; organic anion transport [GO:0015711]; phospholipid translocation [GO:0045332]; regulation of chloride transport [GO:2001225]; regulation of microvillus assembly [GO:0032534]; regulation of plasma membrane organization [GO:1903729]; sensory perception of sound [GO:0007605]; vestibulocochlear nerve formation [GO:0021650]; xenobiotic transmembrane transport [GO:0006855] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]; trans-Golgi network [GO:0005802] | aminophospholipid flippase activity [GO:0015247]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; cardiolipin binding [GO:1901612]; lipid transporter activity [GO:0005319]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidylserine flippase activity [GO:0140346]; phosphatidylserine floppase activity [GO:0090556] | PF13246;PF00122;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43520}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43520}. Apical cell membrane {ECO:0000250|UniProtKB:O43520}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q148W0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O43520}. Golgi apparatus {ECO:0000250|UniProtKB:O43520}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. Localizes to apical membranes in epithelial cells. {ECO:0000250|UniProtKB:O43520}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:19027009}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43520}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000250|UniProtKB:O43520}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:19027009}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000269|PubMed:19027009}; | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (By similarity) (PubMed:19027009). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane. Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (PubMed:19027009). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (By similarity). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (By similarity). Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury (By similarity). {ECO:0000250|UniProtKB:O43520, ECO:0000250|UniProtKB:Q148W0, ECO:0000269|PubMed:19027009}. | Rattus norvegicus (Rat) |
D4AB34 | ERFE_RAT | MASTRSPGGARTLLACASLLAAMGLGVPESAEPVGTQARPQPPGTELPAPPAHSPPEPTIAHAHSVDPRDAWMLFVKQSDKGINSKKRSRTKARRLKLGLPGPPGPPGPQGPPGPFIPSEVLLKEFQLLLKGAVRQRESTEHCTRDLTTPASGGPSRDPVTQELESQDQGAVLALLAATLAQSPRAPRVEAAFHCRLRRDVQVERRALHELGVYYLPEVEGAFRRGPGLNLTSGQYTAPVAGFYALAATLHVALTKQPRKGPPQPRDRLRLLICIQSLCQHNASLETVMGLENSSELFTISVNGVLYLQTGHYTSVFLDNASGSSLTVRGGSHFSAILLGL | null | null | establishment of localization in cell [GO:0051649]; fatty acid transport [GO:0015908]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of gluconeogenesis [GO:0045721]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoclast differentiation [GO:0045671]; positive regulation of fatty acid transport [GO:2000193]; positive regulation of glucose import [GO:0046326]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of fatty acid metabolic process [GO:0019217] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; identical protein binding [GO:0042802] | null | 2.60.120.40; | Adipolin/erythroferrone family | PTM: N-glycosylated; required for secretion of the mature protein. {ECO:0000250|UniProtKB:Q6PGN1}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6PGN1}. Note=Secreted when glycosylated at Asn-230 and Asn-282 (By similarity). Hydroxylation promotes secretion (By similarity). {ECO:0000250|UniProtKB:Q6PGN1}. | null | null | null | null | null | FUNCTION: Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores (By similarity). Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake (PubMed:22351773). Inhibits apoptosis and inflammatory response in cardiomyocytes via promotion of sphingosine-1-phosphate (S1P) and cAMP-dependent activation of AKT signaling (PubMed:30566056). Inhibits autophagy induced by nutrient deficiency in hepatocytes via promoting the phosphorylation of IRS1, AKT, and MTOR, and thereby subsequent activation of the AKT-MTOR signaling pathway (PubMed:24187137). Negatively regulates the differentiation of osteoblasts, potentially via sequestering BMP2, and thereby inhibits the activation of SMAD signaling (By similarity). The reduction in BMP2 signaling in osteoblasts also results in an increase in expression of the osteoclastogenesis-promoting factors TNFSF11/RANKL and SOST, thereby indirectly promotes bone resorption (By similarity). {ECO:0000250|UniProtKB:Q6PGN1, ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:24187137, ECO:0000269|PubMed:30566056}. | Rattus norvegicus (Rat) |
D4ABL6 | MCTP1_RAT | MEPRGAAAGEPEPAVSPSFQARLWKNLQLGVGKGKGGGGGRAGGPERRTAATPTPSLPPPKTTQDVGSTGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRLREHLLPVAKGSSTAAGTVGVTPPGGRSPDSAPSSSASSSLSSSPQPPPRGDRIRDEGTRRGSPEAHLCHQKSSSLPGTACLEQLLEPAPPPAEPARRPAEPQSLQKGEELDCSQKINPVETSNADVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGRKEVFRSKIIHKNLNPVWEEKACVLIDHLREPLYIKVFDYDFGLQDDFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGEPRDVTMLMRKSWKRSSKFQTQSLRLSDQHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTLNPQWREQFDFHLYEERGGVMDITAWDKDAGKRDDFIGRCQVDLSSLSREQTHKLELQLEEGEGHLVLLVTLTASATVSISDLSVNSMEDHKEREEILKRYSPLRIFNNIKDVGFLQVKVIRAEGLMAADVTGKSDPFCVVELNNDRLLTHTVYKNLNPEWNKVFTFNIKDIHSVLEVTVYDEDRDRSADFLGRVAIPLLSIQNGEQKAYVLKNKQLTGPTKGVIHLEIDVIFNAVKASLRTLIPKERKYIEEENRLSKQLLLRNFIRTKRCVMVLVNAAYYVNSCFDWDSPPRSLAAFVLFLLVVWNFELYMIPLLLLLLLTWNYFLIISGKDNRQRDTVVEDMLEDEEEEDDRDDKDGEKKGFINKIYAIQEVCVSVQNILDEAASLGERVKNTFNWTVPFLSWLAIIALCVFTAILYFIPLRYIVLVWGINKFTKKLRSPYAIDNNELLDFLSRVPSDVQVVQYQELKPDHSHSPYKRKKNNLG | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds Ca(2+) via the C2 domains in absence of phospholipids. {ECO:0000250|UniProtKB:Q6DN14}; | negative regulation of cell migration [GO:0030336]; negative regulation of endocytosis [GO:0045806]; negative regulation of response to oxidative stress [GO:1902883]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; recycling endosome [GO:0055037]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509] | PF00168; | 2.60.40.150; | MCTP family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:26195140}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:26195140}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A1ZBD6}. | null | null | null | null | null | FUNCTION: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (By similarity). Overexpression in cultured neurons significantly inhibits neuronal transferrin endocytosis, secretory vesicle retrieval, cell migration, and oxidative stress from glutamate toxicity (PubMed:26195140). {ECO:0000250|UniProtKB:A1ZBD6, ECO:0000269|PubMed:26195140}. | Rattus norvegicus (Rat) |
D4ACE5 | INTU_RAT | MADPARRDPRGRAPELPGDLSSQEEEEEESDSDAGASSLGSCSSASSDTDLEPEWLDSVQRNGELFYLELSEDEEESLLPETQTVNHVNHVRFSEKEVIIEEDDSRERKKYEPKLRRFTKILKSKSLLPKRHHKKKSSNTGPVSILKHQSTQRTGVTVQQRYKDVTVYINPKKLTAIKAREQAKLLEVLVGVIHQTKWSWKRSGKQADGERLVVHGLVPGGSAMKSGQVLVGDVLVAVNDVDVTSENIERVLSCIPGPMQVKLTFENAYAVKKETAQPKKKKAQSSTNDLVKLLCGSEADATQHSTLSIPHITMYLTLQLQSEVAREEQEMLYHYPVSEASQKLKSVRGIFLTLCDMLESVTGTQVTSSSLHVNGKQIHVAYLKESDKLLLIGLPAEEVPLPQLRNMTEDVAQTLKFMYGSLDSAFCQVENTPRLDHFFSLFFERALRPGKLHLSASPSAQQYDAASAVLLDNLPGVRWLLLPQELKVELDTALSDLEAADFQELSEDYYDMRRLYTILGSSLFYKGYMVCSHLPKDDVVEIAAYCRQYCLLPLAAQQRIGQLIIWREVFPQHHLQPATDSDPEAFQEPEGRYFLLIVGLRHYMLCVLLEAGGCASKATGNPGPDCIYVDQARATLHQLEGVESRIEEQLAATPGPCLSCADWFLAAPREKADSLTTSPILGRLQGPSKTAASPTCRRTFFSDYSFKARKPSPSRIGGGREPGEGEENVGLSPHTTPDTVRKQRESEGSDDNVALLKLARKKSTLPNPFHLGTSKKELSEKELEVYNMMKLTSGPENTLFHYVALETVQGIFITPTHEEVAQLGGSVHSQLIKNFHRCCLTIRAVFQQTLKVEKKKALSDGDHLESANSVSSLSPVKEHGVLFECSPENWTDQKKTPPVMSYWVVGRLFLNPKPQELYVCFHDSVSEIAIEMAFRLFFGLTL | null | null | cell division [GO:0051301]; cilium assembly [GO:0060271]; embryonic digit morphogenesis [GO:0042733]; establishment of planar polarity [GO:0001736]; hair follicle morphogenesis [GO:0031069]; keratinocyte differentiation [GO:0030216]; limb development [GO:0060173]; motile cilium assembly [GO:0044458]; negative regulation of cell division [GO:0051782]; negative regulation of keratinocyte proliferation [GO:0010839]; nervous system development [GO:0007399]; neural tube development [GO:0021915]; non-motile cilium assembly [GO:1905515]; positive regulation of smoothened signaling pathway [GO:0045880]; protein localization to organelle [GO:0033365]; regulation of ossification [GO:0030278]; regulation of smoothened signaling pathway [GO:0008589]; roof of mouth development [GO:0060021]; smoothened signaling pathway [GO:0007224]; spinal cord dorsal/ventral patterning [GO:0021513]; tongue morphogenesis [GO:0043587]; vesicle-mediated transport [GO:0016192] | cell surface [GO:0009986]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytoplasm [GO:0005737]; motile cilium [GO:0031514] | null | PF19031;PF19032;PF19033; | 2.30.42.10; | Inturned family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2I0E5}. Note=Enriched at the apical surface in ciliated cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling (By similarity). Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). {ECO:0000250|UniProtKB:Q059U7, ECO:0000250|UniProtKB:Q2I0E5}. | Rattus norvegicus (Rat) |
D4ACP5 | RECQ5_RAT | MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESAIMAVVKGDKDVFVCMPTGAGKSLCYQLPAVLAKGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLLSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKADNGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASERTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEKRGNKPSDKATLLAFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDCCQSPAAIRKKLDALEHSSSWGKTCIGPSQGDGFDPELYEGGRRGYGGFSRYDEGSGGSGDEGRDEAHKREWNLFYQRQMSLRKGKEAKPEEFTPPGEDCPLRDASSRKIPKLTVKAREHCLRLLEEALNSNHQAAGSTHGADLQAKAVELEHETFRSAKMVNLYKASVLKKVAEIHKASKDGQLYDMESSTKSCGAIAELLEPSDYDIPPTSHLYSLKPKRVGAGFSKGPCPFQTATELLGKSQTEKLAPEAALESEQEPSGWVCDPQDGDRSKPCLGYQEEAPGSRTNCGDPSPEKRTKGSSQGSAKARASKRQQLLATAARKDSQSITRFLRQRTECPPPAASVPSSEDASPCGDVPGKCTEEVGAQGHLVAVFQTECPRERLSTCSLEDQSLPKGQPSPLKETQAEKRPRPQQESQEKRAQKRLRPSTNSSALASDPSTENRVAREPCQLSAPGISLKEAADIVVRYLTPFYKEGRFISKDLFKGFARHLSHLLAQKLSPGRSVKEEAQSLIKQFFHNRARCESEADWHGLCGPQR | 5.6.2.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O94762}; Note=Binds a Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:O94762}; | cell division [GO:0051301]; cellular response to camptothecin [GO:0072757]; cellular response to xenobiotic stimulus [GO:0071466]; chromosome separation [GO:0051304]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; mitotic cell cycle [GO:0000278]; mitotic DNA-templated DNA replication [GO:1990506]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; four-way junction helicase activity [GO:0009378]; helicase activity [GO:0004386]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; RNA polymerase II complex binding [GO:0000993] | PF00270;PF00271;PF06959;PF16124; | 6.10.250.2460;6.10.250.3140;3.40.50.300; | Helicase family, RecQ subfamily | PTM: Phosphorylated by CDK1 at Ser-728; this phosphorylation is required for RECQL5-mediated disruption of RAD51 filaments on stalled replication forks. {ECO:0000250|UniProtKB:O94762}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O94762}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. {ECO:0000250|UniProtKB:O94762}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:O94762}; 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; Evidence={ECO:0000250|UniProtKB:O94762}; | null | null | null | null | FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination. {ECO:0000250|UniProtKB:O94762}. | Rattus norvegicus (Rat) |
D4ACX8 | PCD16_RAT | MQEELSVALSCPGMKSLGTLLPLLVLLGTTVPGIRGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLDIDEHSGVVCTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPAHDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLKLERPLDFEQRRVHELVVQARDGGAHPELGSAFVTVHVRDANDNQPSMTVIFLSADGSPRVSEAAPPGQLVARISVSDPDDGDFAHVNVSLEGGEGHFALSTQDSVIYLVCVARRLDREERDVYNLRVTATDSGSPPLRAEAAFVLHVTDVNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGTHTHWFSIDPTSGIITTAATLDYELEPQPQLIVVATDGGLPPLVSSATVSVALQDVNDNEPQFQRTFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGASGSPPFRIDAHSGEVCTTRILDRDQGPSSFDFTVTAIDGGGLKSMVYVKVFVADENDNPPQFYPREYAASLSAQSTPGTAVLRVHAHDPDQGPHGRLSYHILAGNSPPLFALDAHSGLLTVAWPLGRRANSVVQLEIGAQDGGGLQAEPIARVNISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGVVQAHNPPGRLGPVTLTLSGGDPRGLFSLDSASGLLKTLRPLDRELLGPVLELEVRAGSGTPPVFSAARIRVLLDDVNDNSPAFPAPEDTVLLPQNTAPGTPVYTLRALDPDSGANSRVTFSLLAGGDGLFTVDPTTGHVRLMGPLGPPGGPPHELEVEAQDGGSPPRTSHFRLRVVIQDLGIHGLAPRFDSPTYRVDLPSGTTTGTQILQVQAQAPDGSPVTYHLAADGASNPFGLESQSGWLWVRAALDRESQELYTLKVMAVSGSKAELGQQTGTATVRVVILNQNDHSPRLSEEPTFLAVAENQPPGTSVGRVFATDKDSGPNGRLTYSLQQLSEDSKAFRIHPQTGEVTTLQTLDREQQSSFQLLVQVQDAGSPPRSATGTVHVAVLDLNDNSPTFLQASGAAGGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGSGSELFSLHPHTGELHTAASLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSTRMVESPDLVEADSAATVPVVLTVTAAEGLRPGSLLGSVAPQEPASMGVLTYTLVGGADPEGTFALDSASGRLYLARVLDFESGPAWRALTVRAEGPGGAGARLMRVQVRVQDENEHAPAFARDPLALALPENPEPGATLYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPALLLIVEATDRPANASRRKATRVSARVFVTDENDNAPVFASPSRMRLPEDQPPGPAALHVVARDPDLGEAARVSYRLAAGGDGHFRLHATTGALSVVRPLDREQRAEHVLTVVASDHGSPPRSSTQLLTVSVVDVNDEAPAFPQQEYNVILRENSPPGTSLLTLKATDPDLGANGQVTYGGVSGESFSLDPNSGVLTTLRALDREEQEEINLTVYARDRGLPPLLTHITVRVTVEDENDHSPTFGNTHLSLEVPEGQDPQTLTTLRASDPDGGLNGQLQYRILGGDPSGAFALDLTSGEFGTTRPLDREVEPAFQLQIEARDGGQPALSATLLVTVTVLDANDHAPAFPVPSYSVEVPEDAPVGTLLLQLQAHDPDEGDNGRVMYYLGAGTAGAFLLEPTSGELSTATALDREHCASYAFSVTAVDGAAAGPLSTTVPITVTVRDVNDHAPAFPTSPLRLRLPRPGPSLNKPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPAALGPRDRVLFIVATDLGRPARSATGVVIVGIQGEPERGPRFPRANNEAVLRENAPPGTPVISPKAVHSGGSNGPITYSILSGNERGIFSIQPSTGTITVQSAEGLDFETNPRLRLVLQAESGGAFAFSVLTLTLQDANDNAPRFLQPHYVAFLPESRPLEGPLLQVEADDLDQGSGGQISYSLAASQPARGLFHVDPATGTITTTAILDREIWAETRLVLMATDRGSPALVGSATLTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQDPFSIGRYGGRVSLTGPLDFEQCDHYHLQLLAHDGPHEGHANLTVLVEDVNDNVPIFSQSLYQVMMLEHTPPGSAILSVSATDRDSGANGHISYHLASPAEGFSVDTNNGTLFTTVGAMALGHEGPGVVDVVLEARDHGAPGRSAQATVHVQLKDQNDHAPSFTLPHYRVAVSEDLPPGSTLLTLEAIDADGSRSHATVDYSIISGNRGRVFQLEPRLAEVGDGVGPGPQALGCLVLLEPLDFESLTQYNLTVTAADRGQPPRSSAVPVTVTVLDVNDNPPVFTRASYRVTVPEDMPVGAELLHVEASDADPGPHGLVHFTLSSGDPLGLFELDENSGALRLAHPLDCETQAQHQLVVQAADPAGTHFALVPVTVEVQDVNDHGPAFPLSLLSTSLAENQPPGTLVTTLHAMDGDAGTFGRLRYTLLEAVPGPEGREAFSLNSSTGELRARVPFDYEHTGSFRLLVGAADAGNLSASVTVSVLITGEDEYDPVFLAPSFHFQVPEGAQRGHSLGHVQATDEDGGADGLVLYSLATSSPYFGINQTTGALYLRVDSRAPGSGTATSGGGGRTRREAPRELRLEVVARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVLGLVRARSRKAEAAPGPMSQTAPIASSSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAGGPYPRGGSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDADGLSDTSCEPPAPDTWYKGRKAGLLLPGAGATLYREEGPPATATAFLGGCGLSPAPTGDYGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAHPGAKSVPPKPASTAATRAIFPPASHRSPISHEGSLSSAAMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSTESGLEPPDDTELRI | null | null | anatomical structure morphogenesis [GO:0009653]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration [GO:0016477]; cell migration involved in endocardial cushion formation [GO:0003273]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cochlea development [GO:0090102]; condensed mesenchymal cell proliferation [GO:0072137]; digestive tract development [GO:0048565]; heart morphogenesis [GO:0003007]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; hippo signaling [GO:0035329]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; kidney development [GO:0001822]; mitral valve formation [GO:0003192]; mitral valve morphogenesis [GO:0003183]; nephron development [GO:0072006]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; ossification involved in bone maturation [GO:0043931]; pattern specification process [GO:0007389]; post-anal tail morphogenesis [GO:0036342]; protein localization to plasma membrane [GO:0072659] | apical part of cell [GO:0045177]; catenin complex [GO:0016342] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF00028; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and DCHS1 accumulated at the cell-cell boundaries located apical to the adherens junction. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
D4AD37 | IMPA3_RAT | MAPMGIRLSPLGVAVFFLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAEVAVDGGTVDLREMLAVAVLAAERGGDEVRRVRESNVLHEKSKGKTREGAEDKMTSGDVLSNRKMFYLLKTAFPNVQINTEEHVDASDKEVIVWNRKIPEDILKEIAAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDSGSNVKARSSYNEKTPKIIVSRSHAGMVKQVALQTFGNQTLIIPAGGAGYKVLALLDVPDMTQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKSGH | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | chondrocyte development [GO:0002063]; chondroitin sulfate metabolic process [GO:0030204]; embryonic digit morphogenesis [GO:0042733]; endochondral ossification [GO:0001958]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; post-embryonic development [GO:0009791]; skeletal system development [GO:0001501] | endomembrane system [GO:0012505]; trans-Golgi network membrane [GO:0032588] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3',5'-nucleotide bisphosphate phosphatase activity [GO:0097657]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250|UniProtKB:Q9NX62}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}. Note=The catalytic core is predicted to reside within the Golgi lumen. {ECO:0000250|UniProtKB:Q9NX62}. | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q80V26}; | null | PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}. | null | null | FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4. {ECO:0000250|UniProtKB:Q80V26}. | Rattus norvegicus (Rat) |
D4AD53 | KCNG1_RAT | MTLLPGDNSDYDYSALSCASDTSFHPAFFPQRQAIKGVFYRRAQRLGPQDDLHQSISLGDRRRQIIINVGGIKYSLPWTTLDEFPLTRLGQLKACTNFDDILSVCDDYDVTCNEFFFDRNPGAFGTILTFLRAGKLRLLREMCALSFQEELLYWGIAEDHLDGCCKRRYLQKIEEFAEMMEREDEEEALDSEDQESEGPSTSEGRLSRCMRRLRDMVEKPHSGLPGKVFACLSVLFVTVTAVNLSVSTLPSLREEEEQGQCSQMCHNVFIVESVCVGWFSLEFLLRFIQAPSKFAFLRSPLTLIDLVAILPYYVTLLVDGAASSRRKPSTGNSYLDKVGLVLRVLRALRILYVMRLARHSLGLQTLGLTARRCTREFGLLLLFLCVAIALFAPLLYVIENEMADSPEFTSIPACYWWAVITMTTVGYGDMVPRSTPGQVVALSSILSGILLMAFPVTSIFHTFSRSYLELKQEQERVLIRRAQYLIKTKSQLSGMSQDSDILFGSASSDTRDNN | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259] | plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, G (TC 1.A.1.2) subfamily, Kv6.1/KCNG1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8980147}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 (PubMed:8980147). {ECO:0000269|PubMed:8980147}. | Rattus norvegicus (Rat) |
D4ADY9 | ELOV7_RAT | MAFSDLTSRTVRFYDNWIKDADPRVENWLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELFDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYFYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTVHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTMENGNCKSKHH | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL7 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03207}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:57384, ChEBI:CHEBI:71451; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384, ChEBI:CHEBI:71481; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57394, ChEBI:CHEBI:65115; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57384, ChEBI:CHEBI:71407; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316; Evidence={ECO:0000250|UniProtKB:A1L3X0}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:A1L3X0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000250|UniProtKB:A1L3X0}; | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03207}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207}. | Rattus norvegicus (Rat) |
D4AE59 | STK11_RAT | MDVADPQPLGLFPEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHRNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDIKPGNLLLTTNGTLKISDLGVAEALHPFAVDDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGRGDFTIPCDCAPPLSDLLRGMLEYEPAKRFSIRQIRQHSWFRKKHPLAEALVPIPPSPDTKDRWRSMTVVPYLEDLHGRAEEEEDEDLFDIEDGIIYTQDFTVPGQVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGAANPARKVCSSNKIRRLSACKQQ | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | activation of protein kinase activity [GO:0032147]; anoikis [GO:0043276]; autophagy [GO:0006914]; axonogenesis [GO:0007409]; cellular response to UV-B [GO:0071493]; dendrite extension [GO:0097484]; DNA damage response [GO:0006974]; epithelial cell proliferation involved in prostate gland development [GO:0060767]; establishment of cell polarity [GO:0030010]; G1 to G0 transition [GO:0070314]; glucose homeostasis [GO:0042593]; Golgi localization [GO:0051645]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of epithelial cell proliferation involved in prostate gland development [GO:0060770]; negative regulation of TORC1 signaling [GO:1904262]; positive regulation of autophagy [GO:0010508]; positive regulation of axonogenesis [GO:0050772]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of vesicle transport along microtubule [GO:1901610]; positive thymic T cell selection [GO:0045059]; protein autophosphorylation [GO:0046777]; protein dephosphorylation [GO:0006470]; protein localization to nucleus [GO:0034504]; regulation of cell growth [GO:0001558]; regulation of dendrite morphogenesis [GO:0048814]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; regulation of Wnt signaling pathway [GO:0030111]; response to activity [GO:0014823]; response to glucagon [GO:0033762]; response to ionizing radiation [GO:0010212]; response to lipid [GO:0033993]; response to peptide hormone [GO:0043434]; response to thyroid hormone [GO:0097066]; signal transduction [GO:0007165]; spermatid development [GO:0007286]; T cell receptor signaling pathway [GO:0050852]; tissue homeostasis [GO:0001894]; vasculature development [GO:0001944] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular protein-containing complex [GO:0140535]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; serine/threonine protein kinase complex [GO:1902554] | ATP binding [GO:0005524]; LRR domain binding [GO:0030275]; magnesium ion binding [GO:0000287]; p53 binding [GO:0002039]; protein kinase activator activity [GO:0030295]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, LKB1 subfamily | PTM: Phosphorylated by ATM at Thr-366 following ionizing radiation (IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is required to inhibit cell growth. Phosphorylation at Ser-431 is also required during neuronal polarization to mediate phosphorylation of BRSK1 and BRSK2. Phosphorylation by PKC/PRKCZ at Ser-397 in isoform 2 promotes metformin (or peroxynitrite)-induced nuclear export of STK11 and activation of AMPK. UV radiation -induced phosphorylation at Thr-366 mediates CDKN1A degradation. {ECO:0000250|UniProtKB:Q9WTK7}.; PTM: Acetylated. Deacetylation at Lys-48 enhances cytoplasmic localization and kinase activity in vitro. {ECO:0000269|PubMed:18687677}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18774945}. Cytoplasm {ECO:0000269|PubMed:18774945}. Membrane {ECO:0000269|PubMed:18774945}. Mitochondrion {ECO:0000250}. Note=A small fraction localizes at membranes. Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). Translocates to the mitochondrion during apoptosis (By similarity). PTEN promotes cytoplasmic localization (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Note=Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). | 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; 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; | null | null | null | null | FUNCTION: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (By similarity). {ECO:0000250|UniProtKB:Q9WTK7, ECO:0000269|PubMed:18774945}.; FUNCTION: [Isoform 2]: Has a role in spermiogenesis. {ECO:0000269|PubMed:18774945}. | Rattus norvegicus (Rat) |
D4AEC2 | CAMP2_RAT | MGDAADPREVRRTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTETVPEELREPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLILKSDAAKPLLGHDAVIQALAHKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMVSIEKVIACAQQYSAFFQATDLPYDIEDAVMYWINKVNEHLKDIMEQEQKSKEHHTAEAPGGQKSPSKWFWKLVPARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPAVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNHCCHFSLEDMLYAASSIKSNYLVFMAELFWWFEVVKPSFVQPRVVRPQGAEPAKDMPSVPVLNAAKRNVLDSSSSSDFTSRYTRPQTHSSVSGGIRRSSSMSYVDGFIGTWPKEKRTSVHGVSFDISFDKEDNAQSSTPNRGIIRSVSNEGLNNSRASKHIRKNLSFKPVNGGEEESIEEELHVDPHGDLKSYMPLSTNELNSNENTHHKLPNGALQNRVLLDEFGNQIETPSIEEALQIIHDTEKPPHTARPDQIANGFFLHGQDLSLLNSNIKLSQSSPDNITDPKGALSPITDTTEVDTGIHVPSEDIPETMDEDSSLRDYTVSLDSDMDDASKFLQDYDIRASNPREALSPCPSTISTKSQPGSSASSSSGVKMTSFAEQKFRKLNHTDGKSSGSSSQKTTPEGSELNIPHMVSWAQIPEESGVAQGRDTTQLLASEMVHLRMRLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKKKGDGISPLREEAAGAEDEKVYTDRAKEKESQKMDGQRSKSLADIKESMENPQGKWLKSPSTPVDPEKQWNLTSPSEETLNEGELLEYTKSIEKLNSSLHFLQQEMQRLSLQQEMLMQMREQQSWVISPPQPSPQKQIRDFKPRQAGLSSAAAPFSADSPRPTHPSPQSSTRKSASFSVKNQRTPRPNELKITPLNRTLTPPRSVDSLPRLRRFSPSQVPIQTRSFVCFGDDGEPQKEPKPKEEIKKEPSECKGTLESCDHNPGEKEVKPLESTVSEVLSQPITETVCVTPNEDQLNQPTDPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVSVEKFDGESDKEQFDDDQKVCCGFFFKDDQKAENDMAVKRAALLEKRLRREKETQLRKQQLEAEMEHRKEETRRKTEEERQKKEDERARREFIRQEYMRRKQLKLMEDMDTVIKPRPQVAKQKKQRPKSIHRDHIESPKTPIKGPPVSSLSLASLNTGDTESVHSGKRTPRSESVEGFLSPSRCGSRNGEKDWENASTTSSVASGTEYTGPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIGPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKRPVTPKKLLPTKA | null | null | axon development [GO:0061564]; cytoplasmic microtubule organization [GO:0031122]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; regulation of dendrite development [GO:0050773]; regulation of Golgi organization [GO:1903358]; regulation of microtubule polymerization [GO:0031113]; regulation of organelle organization [GO:0033043] | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q08AD1}. Golgi apparatus {ECO:0000250|UniProtKB:Q08AD1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8C1B1}. Cytoplasm {ECO:0000250|UniProtKB:Q8C1B1}. Note=Associated with the minus-end of microtubules and also detected at the centrosomes. Decorates the minus-end of microtubules by decreasing the rate of tubulin incorporation and remaining bound. The length of CAMSAP2-decorated stretches on the minus-end of microtubules is dependent on MAPRE1/EB1 and MAPRE3/EB3, which promote elongation of CAMSAP2-decorated microtubule stretches. Recruited to the Golgi apparatus by AKAP9 and PDE4DIP. In neurons, localizes to the minus-end of microtubules in axon and dendrites. {ECO:0000250|UniProtKB:Q08AD1}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:24908486). Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In addition, it also reduces the velocity of microtubule polymerization (By similarity). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (By similarity). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation (PubMed:24908486). Through the microtubule cytoskeleton, regulates the autophagosome transport (By similarity). {ECO:0000250|UniProtKB:Q08AD1, ECO:0000269|PubMed:24908486}. | Rattus norvegicus (Rat) |
D4B387 | GGT1_ARTBC | MAPAAMNLLCTVLYLLSSFAQVSDAAPWLFSRSIPASYHDGRLGAVASENSMCSEYGADMLKIGGNAADAVCIYRLSLFFAFLPYPALQEDRAMYHSGIGGGGFMLIRAPNGTYEFIDFRETAPAAAFQDMFKNNTSGSTSGGLASGVPGEVRGLEYLHKNYGKLPWKTVMEPAIRTARDGFRVTEDLSRIMLHSTKNGNFLAENAAWALDFAPQGTLLKVGDIITRRRYGDTLDKIAKYGADAFYTGPMAQAMVNALRAANGTMTLEDLKNYTVVSRPTAQIEYRGMTVTSTTAPSSGVVLLSILKLLNGYKNFFRMDPGPLSTHRMDEAIRFGYGQRTELGDPLFFSNLTDYQKKMISDEAANKNRMNISDEYTQDIAVYDPKGLESLNTPGTSHISTADRSGMAVSLTTTINLYFGSRVIVPETGIIMNNEMDDFSVPGRSNSFGYKPSPSNFIRPGKRPLSSICPTIITRPDGSLYFVSGAAGGSQIITGTLQSVINVMDRKMNVRQALKAPRLHDQLVPNVALMEDEFDKKTVDFMISRKHNVTREKSGSTVESIMRLKNGVFEASGEPRLANSGGVVV | 2.3.2.2; 3.4.19.13; 3.4.19.14 | null | glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068]; leukotriene-C(4) hydrolase [GO:0002951] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000250|UniProtKB:P19440}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; Evidence={ECO:0000250|UniProtKB:P19440}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4; Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14; Evidence={ECO:0000250|UniProtKB:P19440}; | null | PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000250|UniProtKB:P19440}. | null | null | FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. {ECO:0000250|UniProtKB:P19440}. | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
D4GP31 | XACC_HALVD | MTVTRVVDTSCRLGEGPVWHPDEKRLYWVDIESGRLHRYDPETGAHDCPVETSVIAGVTIQRDGSLLAFMDRGRVGRVVDGDRRESARIVDSPTRFNDVIADPAGRVFCGTMPSDTAGGRLFRLDTDGTVTTVETGVGIPNGMGFTRDRERFYFTETEARTVYRYAYDEETGAVSARERFVESPETPGLPDGMTVDSAGHIWSARWEGGCVVEYDADGTELGRFDVPTEKVTSVAFGGPDLDSLYVTTAGGDGDGSAGEGDESTGDAAGALFRLDVAATGRPEFRSDVRLG | 3.1.1.15; 3.1.1.68 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:28854683}; Note=Binds 1 divalent metal cation per subunit (By similarity). Most active with Co(2+), Mg(2+) or Mn(2+). Has weaker activity with Fe(2+), Ni(2+) or Zn(2+) (PubMed:28854683). {ECO:0000250|UniProtKB:Q15493, ECO:0000269|PubMed:28854683}; | arabinose catabolic process [GO:0019568]; D-xylose metabolic process [GO:0042732]; L-ascorbic acid biosynthetic process [GO:0019853] | null | calcium ion binding [GO:0005509]; gluconolactonase activity [GO:0004341]; L-arabinonolactonase activity [GO:0050021]; xylono-1,4-lactonase activity [GO:0050402] | PF08450; | 2.120.10.30; | SMP-30/CGR1 family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate; Xref=Rhea:RHEA:16217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16501, ChEBI:CHEBI:17100; EC=3.1.1.15; Evidence={ECO:0000269|PubMed:28854683}; CATALYTIC ACTIVITY: Reaction=D-xylono-1,4-lactone + H2O = D-xylonate + H(+); Xref=Rhea:RHEA:18341, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16392, ChEBI:CHEBI:17746; EC=3.1.1.68; Evidence={ECO:0000269|PubMed:28854683}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37.1 mM for L-arabino-gamma-lactone {ECO:0000269|PubMed:28854683}; KM=10.9 mM for D-xylono-gamma-lactone {ECO:0000269|PubMed:28854683}; Vmax=761 umol/min/mg enzyme with L-arabino-gamma-lactone as substrate {ECO:0000269|PubMed:28854683}; Vmax=437 umol/min/mg enzyme with D-xylono-gamma-lactone as substrate {ECO:0000269|PubMed:28854683}; | PATHWAY: Carbohydrate degradation. {ECO:0000269|PubMed:28854683}. | null | null | FUNCTION: Pentonolactonase involved in D-arabinose and D-xylose catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone and D-xylono-gamma-lactone to the corresponding acids. Can also hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone. {ECO:0000269|PubMed:28854683}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GP33 | ARADH_HALVD | MARIAVTGAAGNVGRVTVEALASDHDVTPITHREREGLDSVILDVRDEDALTEAFEGHDIVVHLAANPNPDAAWDSVYEVNIGGTYNVYEAALAADIDRLVFASTNHVHQMYNIADATRPETLAADAEAVGVSDPPRPDSYYGVSKVFGEALGNYYADRHGLEVLNLRIGWLLTADEVREKMDEEESVARYVRAMWLSPGDCEQGMRRAVEASLPDSPLAVNLISANDDRYLSLTETMRAIGYRPRDNSATVVE | 1.1.1.376 | null | L-arabinose catabolic process [GO:0019572]; L-arabinose catabolic process to 2-oxoglutarate [GO:0019570] | null | L-arabinose 1-dehydrogenase (NAD+) activity [GO:0050022]; L-arabinose 1-dehydrogenase (NADP+) activity [GO:0044103]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH; Xref=Rhea:RHEA:17925, ChEBI:CHEBI:15378, ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.376; Evidence={ECO:0000269|PubMed:23949136}; CATALYTIC ACTIVITY: Reaction=alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-lactone + NADPH; Xref=Rhea:RHEA:42664, ChEBI:CHEBI:15378, ChEBI:CHEBI:17100, ChEBI:CHEBI:46987, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.376; Evidence={ECO:0000269|PubMed:23949136}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for NADP(+) {ECO:0000269|PubMed:23949136}; KM=2 mM for NAD(+) {ECO:0000269|PubMed:23949136}; KM=2.1 mM for L-arabinose {ECO:0000269|PubMed:23949136}; | PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinono-1,4-lactone pathway. {ECO:0000305|PubMed:23949136}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. It shows 50% activity at pH values of 6 and 10. {ECO:0000269|PubMed:23949136}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:23949136}; | FUNCTION: L-AraDH initiates the degradation of L-arabinose. Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. It is highly specific for L-arabinose as substrate and can use both NADP(+) and NAD(+) as electron acceptor, with a slight preference for NADP(+). {ECO:0000269|PubMed:23949136}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GPK6 | LACC_HALVD | MTDWSRRRFLQTGAALGIAGTLPQTTTEVSAASPTLEKFVQPLPIPSVREPDGQRDGADAYEIAVTEFTQQLHPDLPETTVWGFDGSYPGPTIEADAGSPVHVRFDNSGLPSEHLFPVDDRLGGTTAENHPGYDGPVPEVRTVTHFHGLELDPANDGQSDMWTSPGGVEGPRFDSAWQELPMEQGRTTSTYHDHTLGITRLNAYAGLLGLYSITTDAERELGLPSGDYDIPLLLQDKEFNDDGSLHYPEEFVSAFLGDTAVVNGAVWPYVEVEPRRYRFRILNGANHRSFDLQLESESGSGVPTMYQFAPGHGFLESVVPIGPNGDLDSLLLTPFERGELVVDFSDHAGETLTLANGADMGPELTDLVEFRVSDPSTPPEDASADPTSLSLPTPASYDESDARVTREMTLGTEVRNGLITHTLNGHVFGDEDAPVYPQLGATEIWELQNESGGRHPIHLHLVTFRVIGRGPDGTQPPDPNELGPKDTVRVDPGERVRILVTFEGYTGQFPWHCHMLEHEDNKMMIPFVVENPVADYANEENVVDATGLTDAVGDWRNETLETEVLLEVIDQWRSGDEVA | 1.10.3.2 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000305}; Note=Binds 4 copper ions per subunit. {ECO:0000305}; | null | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716] | PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | PTM: Exported by the Tat system.; PTM: Glycosylated. {ECO:0000269|PubMed:19966030}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966030}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:19966030}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=671 uM for 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid {ECO:0000269|PubMed:19966030}; KM=35 uM for syringaldazine {ECO:0000269|PubMed:19966030}; Note=kcat is 9.9 sec(-1) with 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid as substrate. kcat is 21.7 sec(-1) with syringaldazine as substrate. Optimal activity at 200 mM salt, with 65% activity at 1 M NaCl.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for the oxidation of 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid and 8.4 for the oxidation of syringaldazine. {ECO:0000269|PubMed:19966030}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:19966030}; | FUNCTION: Catalyzes the oxidation of a wide variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and dimethoxyphenol (DMP). No oxidation of Fe(2+) or guaiacol. {ECO:0000269|PubMed:19966030}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSE6 | KDGK1_HALVD | MTALVTFGETMLRLSPPRGERLETARELEVQAGGAESNVAVAAARLGRDAAWFSKLPDSPLGRRIVSELRSHSVDTDGVVWTDDADARQGVYYLEHGASPRPTNVVYDRADAAVTTLETGEFDLDAVRDAEVCFTSGITPALSETLSETTADVLDEAQNAGTTTAFDLNYRTKLWSPDEAAEVYRDLLDSVDLLFAAERDAATVLGRDGDAESVARGLADDYDIETVVVTRGEEGSLAVSDGAVSEQGVYETETYDAIGTGDAFVGGFLAKHLDGGSVTESLEWASATASFKRTVEGDIAVVTPEDVERVVAEEGDGISR | 2.7.1.178 | null | D-galacturonate catabolic process [GO:0019698]; D-glucuronate catabolic process [GO:0042840]; DNA damage response [GO:0006974] | cytosol [GO:0005829] | 2-dehydro-3-deoxygalactonokinase activity [GO:0008671]; 2-dehydro-3-deoxygluconokinase activity [GO:0008673]; ATP binding [GO:0005524] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-phospho-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:14797, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57569, ChEBI:CHEBI:57990, ChEBI:CHEBI:456216; EC=2.7.1.178; Evidence={ECO:0000269|PubMed:25287957}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14798; Evidence={ECO:0000269|PubMed:25287957}; CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-D-galactonate + ATP = 2-dehydro-3-deoxy-6-phospho-D-galactonate + ADP + H(+); Xref=Rhea:RHEA:16525, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57989, ChEBI:CHEBI:58298, ChEBI:CHEBI:456216; EC=2.7.1.178; Evidence={ECO:0000269|PubMed:25287957}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16526; Evidence={ECO:0000269|PubMed:25287957}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 mM for KDG {ECO:0000269|PubMed:25287957}; KM=0.73 mM for KDGal {ECO:0000269|PubMed:25287957}; KM=0.36 mM for ATP {ECO:0000269|PubMed:25287957}; Vmax=78 umol/min/mg enzyme with KDG as substrate {ECO:0000269|PubMed:25287957}; Vmax=33 umol/min/mg enzyme with KDGal as substrate {ECO:0000269|PubMed:25287957}; | PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 1/2. {ECO:0000305}. | null | null | FUNCTION: Involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deoxy-6-phosphogalactonate (KDPGal). {ECO:0000269|PubMed:25287957}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSF3 | UBAA_HALVD | MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD | 2.7.7.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | protein urmylation [GO:0032447]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; ubiquitin-like modifier activating enzyme activity [GO:0008641]; URM1 activating enzyme activity [GO:0042292] | PF00899; | 3.40.50.720; | HesA/MoeB/ThiF family | PTM: Sampylated at Lys-113 with the archaeal ubiquitin-like protein SAMP2. Also sampylated with SAMP1. {ECO:0000269|PubMed:20054389}. | null | CATALYTIC ACTIVITY: Reaction=[small archaeal modifier protein]-C-terminal Gly-Gly + ATP + H(+) = [small archaeal modifier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:56100, Rhea:RHEA-COMP:14381, Rhea:RHEA-COMP:14383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; | null | null | null | null | FUNCTION: Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus (PubMed:21368171, PubMed:24097257, PubMed:24906001). In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171, PubMed:24097257). {ECO:0000269|PubMed:21368171, ECO:0000269|PubMed:24097257, ECO:0000269|PubMed:24906001}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSH6 | NCSA_HALVD | MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEAV | 2.7.7.- | null | response to heat [GO:0009408]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble position uridine thiolation [GO:0002143] | cytosolic tRNA wobble base thiouridylase complex [GO:0002144] | CCA tRNA nucleotidyltransferase activity [GO:0004810]; enzyme binding [GO:0019899]; sulfurtransferase activity [GO:0016783]; tRNA binding [GO:0000049] | PF01171; | 3.40.50.620; | TtcA family, CTU1/NCS6/ATPBD3 subfamily | PTM: Sampylated at Lys-204 with the archaeal ubiquitin-like protein SAMP2. Polymeric chains of SAMP2 are also linked. {ECO:0000269|PubMed:24906001}. | null | null | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000269|PubMed:24906001}. | null | null | FUNCTION: Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble position. Required for cell growth at elevated temperatures. {ECO:0000269|PubMed:24906001}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GSH7 | FTSZ2_HALVD | MQDIVREAMERDEAERQTQSSLEDSDDQFGDPRIVIVGAGGAGNNTINRLYNIGVEGADTVAINTDKQHLKMIEADTKILVGKSLTQGLGAGGDPSMGERATEMAQGTIKDVLGDADLVFVTAGMGGGTGTGAAPVVAKIAKEQGAIVVGMVSTPFNVERARTVKAEEGLENLRNEADSIIVLDNNRLLDYVPNLPIGKAFSVMDQIIAETVKGISETITQPSLINLDYADMSTIMNQGGVAVMLVGETQDKNKTQEVVNDAMNHPLLDVDYRGASGGLVHITGGPDLTLKEAEGIASNITERLEAAANVIWGARIQDEYKGKVRVMAIMTGVQSAQVLGPSTQKQADKSRQSIQSRESQQQHSGSEFDSSERAQTAQSGTWSDGGRDEVEKNNGLDVIR | null | null | cell division [GO:0051301]; contractile ring contraction [GO:0036213]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; protein polymerization [GO:0051258] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytoplasmic side of membrane [GO:0098562] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF12327;PF00091; | 3.30.1330.20;3.40.50.1440; | FtsZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}. | null | null | null | null | null | FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (By similarity). Required for division ring constriction (PubMed:33903747). {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GT97 | IPYR_HALVD | MVNLWEDMETGPNAPDEIYAVVECLKGERNKYEYDKDIPGVVLDRVLHSNVHYPSDYGFIPQTYYDDEDPFDVLVLVEDQTFPGCVIEARPVALMKMDDDGEQDDKVIAVPVEDPRYDHIEDLDDIPQQTLDEIDEFFATYKNLEAGKEVETLGWEDKQAAKDAIEHAMDLYEENFA | 3.6.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423}; | phosphate-containing compound metabolic process [GO:0006796] | cytosol [GO:0005829] | inorganic diphosphate phosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287] | PF00719; | 3.90.80.10; | PPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}. | CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.55 mM for diphosphate (at 42 degrees Celsius) {ECO:0000269|PubMed:26546423}; KM=0.26 mM for diphosphate (at 25 degrees Celsius) {ECO:0000269|PubMed:26546423}; Vmax=465 umol/min/mg enzyme (at 42 degrees Celsius) {ECO:0000269|PubMed:26546423}; Vmax=53 umol/min/mg enzyme (at 25 degrees Celsius) {ECO:0000269|PubMed:26546423}; Note=Displays non-Michaelis-Menten kinetics for PPi hydrolysis. Hill coefficients indicate cooperative binding to PPi and Mg(2+). {ECO:0000269|PubMed:26546423}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:26546423}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. Is moderately thermostable, with a half-life of thermal inactivation of 2 hours at 65 degrees Celsius, and retains 82% activity after incubation for 2 hours at 42 degrees Celsius. {ECO:0000269|PubMed:26546423}; | FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions (By similarity) (PubMed:26546423). The hydrolysis of PPi by inorganic pyrophosphatase releases a considerable amount of energy that can drive unfavorable biochemical transformations to completion (Probable). Is not active on nucleoside triphosphates (ATP, TTP, GTP, or CTP) or nucleoside diphosphate (ADP) (PubMed:26546423). {ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423, ECO:0000305|PubMed:26546423}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTL2 | ACEB_HALVD | MTERRHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGIWSLTPGQVVEANTSPLPPKTGSWLLDADGEEVELASEDGVEAYDGDRLSLEATDGGYELRVGGDARELTADELREELLGLTSYVPSMDDIVDSMEEFEAAKEAGRGAIAMTQSATLRIGGTEIDIEKDRMWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVERAMEVGL | 2.3.3.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21569248}; | glyoxylate cycle [GO:0006097]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | magnesium ion binding [GO:0000287]; malate synthase activity [GO:0004474]; metal ion binding [GO:0046872] | null | 1.20.58.1560;3.20.20.60; | HpcH/HpaI aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 uM for glyoxylate (with 0.2 mM acetyl-CoA at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; KM=0.119 uM for acetyl-CoA (with 0.5 mM glyoxylate at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; Note=AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold).; | PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 45 and 65 degrees Celsius. The activity of the enzyme at 80 degrees Celsius is half of the maximum. {ECO:0000269|PubMed:9738442}; | FUNCTION: Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA. {ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:21569248, ECO:0000269|PubMed:9738442}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTL3 | ACEA_HALVD | MNPTELDSDVFAQDVDNQKARELREMLNTQDFVFAPGMYHALDARLAEMTGHDAAYMSGYSTVLGQFGFPDLEMVTMTEMVENAKRMVEATNLPVIADCDTGYGGIHNVRRAVREYEKAGVAAVHIEDQTTPKRCGHIAGKQIVSREKAKARFEAAVDAKQSEDTVVIARTDAYGSSNGDWDEHVERGRIYADAGVDIVWPEMPNPSREDAVAYAEEIHETHPDLKLAFNYSSSFAWSEEEDPLTFQELGDLGYKYIFITLFGLHSGAHAVYEDFKKLAEQDEEGQFDLEQRYLDHPTESHHELSFVSRYQDIETEFDPEARRRIEESEGFSEEQADPITSNDDD | 4.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0A9G6}; | glyoxylate cycle [GO:0006097]; propionate catabolic process, 2-methylcitrate cycle [GO:0019629] | null | isocitrate lyase activity [GO:0004451]; metal ion binding [GO:0046872]; methylisocitrate lyase activity [GO:0046421] | PF13714; | 3.20.20.60; | Isocitrate lyase/PEP mutase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate = glyoxylate + succinate; Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.16 uM for isocitrate (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:9738442}; | PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. {ECO:0000305|PubMed:9738442}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Very little activity is detected at pH 6.1 or 8.0. {ECO:0000269|PubMed:9738442}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Very little activity is found above 65 degrees Celsius, and the activity at 40 degrees Celsius is 50% of the maximum. {ECO:0000269|PubMed:9738442}; | FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. {ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:9738442}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GTS4 | JAMM1_HALVD | MTSSRLSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE | 3.4.19.15 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22970855}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22970855}; | proteolysis [GO:0006508] | null | metalloexopeptidase activity [GO:0008235]; zinc ion binding [GO:0008270] | PF14464; | 3.40.140.10; | Peptidase M67B family | null | null | CATALYTIC ACTIVITY: Reaction=an N(6)-[small archaeal modifier protein]-[protein]-L-lysine + H2O = a [protein]-L-lysine + a [small archaeal modifier protein].; EC=3.4.19.15; Evidence={ECO:0000269|PubMed:22970855}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-10. Displays little to no activity at low pH (pH 6.5 and below). {ECO:0000269|PubMed:22970855}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. Is active over a wide range of temperature (20-60 degrees Celsius). However, the enzyme is not active at 70 degrees Celsius. {ECO:0000269|PubMed:22970855}; | FUNCTION: Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. {ECO:0000269|PubMed:22970855, ECO:0000269|PubMed:24097257}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GUA0 | AGLD_HALVD | MGRPTERRPAAATAAGVEVSVVLPAYNEARTIENTVRVTVETLESFLPADAFEVIVAEDGCDDETPEIADRLAAEDDRIRHYHSDDRLGRGGALERAFEAARGDTLVYFDTDLATDMRHLEELVERVRSGEYDAATGSRWMPDRVADRPRKRGVPSRAYNGLVRLFLRSDLRDHQCGFKAFSREAFEALRDDVEDNHWFWDTEMLVRAQRAGFRVAEFPVDWEPKGDTKVDLVRDILGMGSQILRTWWQLTVRPRITRRVTIVAGLLLTVLALALMTLYIDPSEVISVLGDADPALVAAAAVIYVVSWPLRGIRYREILRELGYREKAGFLTGAIFISQTGNLVFPARAGDAVRAYVVKARRNIPYPSGFASLAVERVFDLLTIAGLAGVVLVGLAATGGLDDIATVLATGVSGGSVDVSADDVRTAAYVATGVGVVAILGVLGIALSARADRNVVRAFVGRFSSDSYVELVAGVIEQFVSDLQAVAGNRAAFGRVGLTSLAIWTVDVVTAVVVLLALGVDIDPVVLVGVSFFAVSVGNLAKVLPLSPGGVGLYEIAFTVFMAALAPVTPAAALAAAVLDHAVKNAVTIVGGVGSMLSLNVSLTTAVEESAEVRDREHELADSK | 2.4.1.- | null | S-layer organization [GO:0045232] | plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757] | PF00535;PF03706; | null | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:17996897}. | null | null | FUNCTION: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier. {ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GUJ7 | PAN1_HALVD | MMTDTVDDVDLPYDKDSASQQEKITALQERLEVLETQNEEMRDKLLDTNAENNKYQQKLERLTHENKKLKQSPLFVATVQEITDEGVIIKQHGNNQEALTEVTDEMREELEPDARVAVNNSLSIVKRLDKETDVRARVMQVEHSPDVTYEDIGGLEEQMQEVRETVEMPLDRPEMFAEVGIDPPSGVLLYGPPGTGKTMLAKAVANQTNASFIKMAGSELVHKFIGEGAKLVRDLFEVARENEPAVIFIDEIDAIASKRTDSKTSGDAEVQRTMMQLLAEMDGFDERGNIRIIAATNRFDMLDPAILRPGRFDRLIEVPKPNEDGREIIFQIHTRKMNVSDDVDFVELAEMADNASGADIKAVCTEAGMFAIRDDRTEIFMQDFVDAWEKIQQEASDETEVSRAFA | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein unfolding [GO:0043335] | cytoplasm [GO:0005737]; proteasome regulatory particle, base subcomplex [GO:0008540]; proteasome-activating nucleotidase complex [GO:0022623] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proteasome-activating activity [GO:0036402] | PF00004;PF17862; | 1.10.8.60;2.40.50.140;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=438 uM for ATP (at 42 degrees Celsius, pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376}; Vmax=471 nmol/h/mg enzyme for ATPase activity (at 42 degrees Celsius, pH 8 and 2 M NaCl) {ECO:0000269|PubMed:24343376}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. ATPase activity is 1.5-fold decreased at 25 degrees Celsius and 37 degrees Celsius, 4.7-fold at 20 degrees Celsius. The protein is not active at 50 degrees Celsius. {ECO:0000269|PubMed:24343376}; | FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable). Is also able to cleave other nucleoside triphosphates including GTP and TTP, but the rate of hydrolysis is 4- to 5-fold slower than for ATP. {ECO:0000269|PubMed:24343376, ECO:0000305}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GWB3 | Z2753_HALVD | MSESEQRHAHQCVSCGINIAGMSAATFKCPDCGQEISRCSKCRKQSNLYECPDCGFMGP | null | null | archaeal-type flagellum-dependent cell motility [GO:0097590]; single-species surface biofilm formation [GO:0090606] | null | zinc ion binding [GO:0008270] | PF07754; | null | null | null | null | null | null | null | null | null | FUNCTION: Zinc-binding protein that binds only one zinc ion. Is required for swarming and biofilm formation. {ECO:0000269|PubMed:32905660}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GY98 | DNLJ_HALVD | MSDADVDAESNPYLRDPPTEFEPAESLSREAAEGQAALLREAVREHDHRYYVAADPLVSDAAYDALFSRLVALEDAFDLDTTNSPTNRVGGEPIDALETVEHVAPMLSIDQSTDADDLREFDERVRREVGAVDYVCEPKFDGLSVEVVYEDGEFVRAATRGDGRRGDDVSAQVKTIPTVPLSLRGDHPDRLAVRGEIYMPKSDFSDLNARRVEAGEDAFANPRNAAAGTLRNLDPSVVADRPLAVFFYDILDASARPDSQWAALDRLREWGLRVTDRIERAEDVAEAIDYRDRMQAARDDLDYEIDGTVIKVDSRDARERLGEKSRSVRWAFAYKFPARHEVTTVRDIVVQVGRTGRLTPVAILDPVDVGGVTVSRATLHNPDERAALGVAVGDRVRVKRAGDVIPQVVEVTEDGGGCYEFPDECPVCGSAVDRDGPLAFCSGGLSCPAQREASIGHFAVKGAMDIDGLGEERVAQLVDAGLVETVADLYDLTADDLAELEGWGETSAENLVAAVENAKHPSLDSFLVGLSIPEVGEATARGLAREFGSIEAFPIEADAEEDEFDAFEERLTTVPDVGETVARRVRDFFENADNRAVIRALLDRGVDPEPVESGGDELDGLTFVVTGTLAASRSDVTELVESHGGNVTGSVSGNTDYLVVGENPGRSKRDDAEANDVPTLAETEFEALLAERGVAYPPE | 6.5.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; | base-excision repair, DNA ligation [GO:0006288]; DNA replication [GO:0006260] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872] | PF00533;PF01653;PF03120;PF12826;PF14520; | 1.10.150.20;3.40.50.10190;3.30.470.30;1.10.287.610;2.40.50.140; | NAD-dependent DNA ligase family, LigA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}; | null | null | null | null | FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. {ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYE0 | ALF_HALVD | MPFYGGEELATVYDEALDEGFGLIASNIAEPNIMMGLMEGADRMDSDLLLQMSGGACRFAGDGDAVAGLKAMGNYIETIAERYDIGVFLNMDHQTDLEFIEQQIELDIPSSIMIDASHEPFDENVATSREVVEMVEAAGSDVLIEAELGQIKGVEDEIEAEEAFYTDPEQAVEFVDKTGADLLAISVGTQHGVAKGKDLELRPDLANDIRQALRDHGLDTPLVLHGSSGVQPDQLQEMLKHGICKVNKDTRYQYEYTRTAYDRYNEEPNAIVPPEGVADARDTFFNETDWSPNKDVFDPRVAGRDIRERIADVHADLTEVSGSAGQSLFK | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. {ECO:0000250}; | glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; tagatose-bisphosphate aldolase activity [GO:0009025]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:22493022}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for D-fructose 1,6-bisphosphate {ECO:0000269|PubMed:22493022}; Vmax=55 umol/min/mg enzyme {ECO:0000269|PubMed:22493022}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22493022}; | null | FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. Plays a role in gluconeogenesis during growth on acetate, D-xylose, and casamino acids. {ECO:0000269|PubMed:22493022}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYG6 | AGLQ_HALVD | MTSLSDILASSAEAGLSLQRSDGSMPAGHNGPYHDPETPVRNTSHWLVTFLKAHELTDENRFRQAASDAVSYLLSEEARPHGHTFEHRQNDTKDRCNGLMGQAWSLEALALAARALDNERAAAVAADVFLSHPFCDKLKLWQRVDTDGTILGFDRTFNHQLWFAASGGLVAHTAPQEVSQRVRDFLDSLPSTIDLYENGLIRHPLRPSMDLSELAESVTHDVHRSMVRNHLLHYLRPPRSKRRLRNKAEGYHSFNLYALAILAREFPSHSVWSTDLLSDILEYTLSEEFREATTDNKFSHPYNPPGFEVPAAMETFSVGSYKEREMWVNEQIQHSFDPNTSLLTRGTDDKQTHAARLYEATRLDDYEIYLD | null | null | carbohydrate metabolic process [GO:0005975]; S-layer organization [GO:0045232] | cytoplasm [GO:0005737] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24236216}. | null | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:24236216}. | null | null | FUNCTION: Putative isomerase involved in the N-glycosylation pathway. Required for the appearance of the methyl ester of hexuronic acid found at position four of the pentasaccharide N-linked to the S-layer glycoprotein. Either involved in preparing the third sugar for attachment of the fourth pentasaccharide subunit or processing the fourth sugar prior to its addition to the lipid-linked trisaccharide. {ECO:0000269|PubMed:24236216}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYH4 | AGLB_HALVD | MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHLRQVEYTVRNWPATMPFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSLLVAPAVFGALTVIPTYLIGKRLGGRLGGLFGAVILMLLPGTFLQRGLVGFADHNIVEPFFMGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAGVATAIYMWSWPPGILLVGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQPLFSLGVALGAVFLAALARWWESNDVDERYYPAVVGGTMLVGIVLFSLVLPSVFDSIARNFLRTVGFSAGAATRTISEAQPFLAANVLQSNGQTAVGRIMSEYGFTFFTGALAAVWLVAKPLVKGGNSRKIGYAVGSLALIGVLFLIPALPAGIGSALGVEPSLVSLTIVTALIVGAVMQADYESERLFVLVWAAIITSAAFTQVRFNYYLAVVVAVMNAYLLREALGIDFVGLANVERFDDISYGQVAAVVIAVLLILTPVLIIPIQLGNGGVSQTAMQASQTGPGTVTQWDGSLTWMQNNTPAEGEFGGESNRMEYYGTYEYTDDFDYPDGAYGVMSWWDYGHWITVLGERIPNANPFQGGATEAANYLLAEDEQQAESVLTSMGDDGEGDQTRYVMVDWQMASTDAKFSAPTVFYDESNISRSDFYNPMFRLQEQGEQTTVAAASSLKDQRYYESLMVRLYAYHGSAREASPIVVDWEERTSADGSTTFRVTPSDGQAVRTFDNMSAAEEYVANDPTSQIGGIGTFPEERVSALEHYRLVKSSNSSALRSGSYQRSLISEGNTYGLQPQALVPNNPAWVKTFERVPGATVDGSGAPANTTVTARVQMRDLTTGTNFTYTQQAQTDADGEFTMTLPYSTTGYDEYGPDNGYTNVSVRAAGGYAFTGPTSVTGNSTIVSYQAENVAVDEGLVNGAEDGTVQVTLERNEQELDLPGDSSSEDSSSEDGTSDGSQTNESASTSTSASVDASAVSAAA | 2.4.99.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O29867}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O29867}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; S-layer organization [GO:0045232] | plasma membrane [GO:0005886] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF18079;PF02516; | 2.60.40.3390;3.40.50.12610; | STT3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.; EC=2.4.99.21; Evidence={ECO:0000269|PubMed:21091511}; | null | PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. {ECO:0000269|PubMed:17996897}.; PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:17996897}. | null | null | FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a hexose-linked tetrasaccharide composed of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in H.volcanii) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (Probable) (PubMed:17996897, PubMed:21091511). {ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511, ECO:0000305|PubMed:22730124, ECO:0000305|PubMed:27015803}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYI2 | GLPA1_HALVD | MKKSPSVLVIGGGSTGTGIARDLAMRGLDVTLVEKGNLTHGTTGRMHGLLHSGGRYAVSDQPSAKECIEENRVLRRIAGHCVEMTGGLFVQRPEDSDEYFEKKLEGCRECGIPAEVLSAEEAREIEPYLAKDIKRAIKVPDGAVDPFRLCVANAASAVEHGARIETHSEVTDVLVEGGEVVGVEVTHQTGTGPYVHGEPGEVEEIRADYVVNATGAWAGQIGDFAGVNVEVRPSKGVMTIMNTRQVDTVVNRCRPKGDADIIVPHETTCILGTTDEEVEDPEDYPEEGWEVDLMIETLSELVPMLADARTIRSFWGVRPLYEPPGTGTEDPTDITREFFLLDHADRDDLPGMTSIVGGKLTTYRMMAEQISDHVCEKLGVDAECRTADEPLPGSEDFTVLRDYMDDFGLRSPIGRRSAQRLGSRADEVLNSVDPNPVVCECEAVTRAEIQDALDTAGTDLNSVRIQTRASMGNCQGAICCHRMANELAPEYDEKTVRASLDDLYQERWKGERHAMWGTQLSQTALKHMLHAATMNRDEDPAAADADIDFAAFDDGVASGGAVADGGRERAADRADDDALGGADGDN | 1.1.5.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; | glycerol catabolic process [GO:0019563]; glycerol-3-phosphate metabolic process [GO:0006072] | glycerol-3-phosphate dehydrogenase complex [GO:0009331]; plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368] | PF01266;PF04324; | 1.10.10.1100;3.30.9.10;3.50.50.60; | FAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; Evidence={ECO:0000269|PubMed:21725010}; | null | PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. | null | null | FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Required for growth on glycerol and for glycerol metabolism. {ECO:0000269|PubMed:21725010}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYV5 | SUFS_HALVD | MRVQESYPVDVDAIRADFPILERKVGGDISTPGEHDDDTTPLVYLDNAATSHTPEQVVDAIVDYYHGYNSNVHRGIHHLSQEASVAYEDAHDRVAEFIGASGGREEVVFTKNTTESMNLVAYAWGLDELGPGDSVVMTEMEHHASLVTWQQIAKKTGAEVRYIRVDDDGRLDMEHAKELIDDSTKMVSVVHVSNTLGTVNPVSELADMAHEVGSYIFVDGAQSVPTRPVDVEDIDADFFAFSGHKMCGPTGIGALYGKRDILDEMGPYLYGGEMIRSVTYEDSTWEDLPWKFEAGTPPIAQGVGFAAAVDYLDDIGMENVQAHEELLAEYAYDRLTEFDDIEIYGPPGDDRGGLVSFNLDSVHAHDLSSILNEQGVAIRAGDHCTQPLHDKLGVAASTRASFYIYNAREEVDKLVDAIDAARELFA | 2.8.1.7; 4.4.1.16 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20226884}; | cysteine metabolic process [GO:0006534] | null | cysteine desulfurase activity [GO:0031071]; pyridoxal phosphate binding [GO:0030170]; selenocysteine lyase activity [GO:0009000] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family, Csd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:20226884}; CATALYTIC ACTIVITY: Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843, ChEBI:CHEBI:57972; EC=4.4.1.16; Evidence={ECO:0000269|PubMed:20226884}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.032 mM for L-cysteine {ECO:0000269|PubMed:20226884}; KM=0.97 mM for L-selenocysteine {ECO:0000269|PubMed:20226884}; Vmax=0.051 umol/min/mg enzyme with L-cysteine as substrate {ECO:0000269|PubMed:20226884}; Vmax=11.8 umol/min/mg enzyme with L-selenocysteine as substrate {ECO:0000269|PubMed:20226884}; | PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Remains partially active at pH 11. {ECO:0000269|PubMed:20226884}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius in the presence of 0-0.5 M KCl and 70-75 degrees Celsius in the presence of 2.5-3.0 M KCl. {ECO:0000269|PubMed:20226884}; | FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Able to reassemble a removed [2Fe-2S] cluster of an apo-ferredoxin. Shows a selenocysteine lyase activity approximately 280-fold higher than its cysteine desulfurase activity. {ECO:0000269|PubMed:20226884}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GYZ1 | PSB_HALVD | MRTPTHDEFSGRLDSLNGDRSNVFGPELGEFSNADRRADELGDKETKTGTTTVGIKTEEGVVLATDMRASMGYMVSSKDVQKVEEIHPTGALTIAGSVSAAQSLISSLRAEVRLYEARRGEDMSMQALSTLVGNFLRSGGFYVVQPILGGVDETGPHIYSIDPAGSILEEEYTVTGSGSQYALGVLEQEFEDGLSIEEAKGVATKAIRSAVERDLASGNGINIAVVTEDGVDIQRHQNFEGLE | 3.4.25.1 | null | proteasomal protein catabolic process [GO:0010498] | cytoplasm [GO:0005737]; proteasome core complex, beta-subunit complex [GO:0019774] | endopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298] | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525}; | FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4GZE7 | SAMP2_HALVD | MNVTVEVVGEETSEVAVDDDGTYADLVRAVDLSPHEVTVLVDGRPVPEDQSVEVDRVKVLRLIKGG | null | null | protein modification by small protein conjugation [GO:0032446] | null | nucleotide binding [GO:0000166]; protein tag activity [GO:0031386] | null | 4.10.410.50; | null | PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer. {ECO:0000269|PubMed:21368171}. | null | null | null | null | null | null | FUNCTION: Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes. {ECO:0000269|PubMed:20054389, ECO:0000269|PubMed:21368171, ECO:0000269|PubMed:24097257}. | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
D4HRL0 | GH7B_LIMQU | MSLAVVFLLGFLAVSHGQQAGTETEEYHLPLTWERDGSSVSASVVIDSNWRWTHSTEDTTNCYDGNEWDSTLCPDADTCTENCAIDGVDQGTWGDTYGITASGSKLTLSFVTEGEYSTDIGSRVFLMADDDNYEIFNLLDKEFSFDVDASNLPCGLNGALYFVSMDEDGGTSKYSTNTAGAKYGTGYCDAQCPHDMKFIAGKANSDGWTPSDNDQNAGTGEMGACCHEMDIWEANSQAQSYTAHVCSVDGYTPCTGTDCGDNGDDRYKGVCDKDGCDYAAYRLGQHDFYGEGGTVDSGSTLTVITQFITGGGGLNEIRRIYQQGGQTIQNAAVNFPGDVDPYDSITEDFCVDIKRYFGDTNDFDAKGGMSGMSNALKKGMVLVMSLWDDHYANMLWLDATYPVDSTEPGALRGPCSTDSGDPADVEANFPGSTVTFSNIKIGPIQSYD | 3.2.1.91 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162] | PF00840; | 2.70.100.10; | Glycosyl hydrolase 7 (cellulase C) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:23733951}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2676.4 uM for p-nitrophenyl-beta-d-cellotrioside (pNP-G3) {ECO:0000269|PubMed:23733951}; KM=2121.7 uM for p-nitrophenyl-beta-d-cellopentaoside (pNP-G5) {ECO:0000269|PubMed:23733951}; Note=kcat is 10.57 min(-1) for p-nitrophenyl-beta-d-cellotrioside (pNP-G3). kcat is 24.42 min(-1) for p-nitrophenyl-beta-d-cellopentaoside (pNP-G5). {ECO:0000269|PubMed:23733951}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6.5 for p-nitrophenyl-beta-d-cellotrioside (pNP-G3), and 4-8 for p-nitrophenyl-beta-d-cellopentaoside (pNP-G5). {ECO:0000269|PubMed:23733951}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 25-45 degrees Celsius. High activity is maintained over a wide temperature range. {ECO:0000269|PubMed:23733951}; | FUNCTION: Exocellobiohydrolase (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:23733951). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable). {ECO:0000269|PubMed:23733951, ECO:0000305}. | Limnoria quadripunctata (Gribble) |
D4N500 | DIOX1_PAPSO | MEKAKLMKLGNGMEIPSVQELAKLTLAEIPSRYVCANENLLLPMGASVINDHETIPVIDIENLLSPEPIIGKLELDRLHFACKEWGFFQVVNHGVDASLVDSVKSEIQGFFNLSMDEKTKYEQEDGDVEGFGQGFIESEDQTLDWADIFMMFTLPLHLRKPHLFSKLPVPLRETIESYSSEMKKLSMVLFNKMEKALQVQAAEIKGMSEVFIDGTQAMRMNYYPPCPQPNLAIGLTSHSDFGGLTILLQINEVEGLQIKREGTWIAVKPLPNAFVVNVGDILEIMTNGIYHSVDHRAVVNSTNERLSIATFHDPSLESVIGPISSLITPETPALFKSGSTYGDLVEECKTRKLDGKSFLDSMRI | 1.14.11.31; 2.1.1.- | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:20228795}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:20228795}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | methylation [GO:0032259]; morphine biosynthetic process [GO:0097295] | null | (S)-tetrahydroprotoberberine N-methyltransferase activity [GO:0030782]; metal ion binding [GO:0046872]; oripavine 6-O-demethylase activity [GO:0102804]; thebaine 6-O-demethylase activity [GO:0102802] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thebaine = CO2 + formaldehyde + neopinone + succinate; Xref=Rhea:RHEA:27477, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:59950, ChEBI:CHEBI:59953; EC=1.14.11.31; Evidence={ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:23928311}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + oripavine = CO2 + formaldehyde + neomorphinone + succinate; Xref=Rhea:RHEA:75951, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:194188, ChEBI:CHEBI:194499; Evidence={ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:23928311}; CATALYTIC ACTIVITY: Reaction=(S)-canadine + S-adenosyl-L-methionine = (S)-cis-N-methylcanadine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12805, ChEBI:CHEBI:16592, ChEBI:CHEBI:50540, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:23928311}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thebaine = 6-O-demethylthebaine + CO2 + formaldehyde + H(+) + succinate; Xref=Rhea:RHEA:76115, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:59953, ChEBI:CHEBI:194545; Evidence={ECO:0000269|PubMed:23928311}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.4 uM for oripavine {ECO:0000269|PubMed:20228795}; KM=20.3 uM for thebaine {ECO:0000269|PubMed:20228795}; KM=16.4 uM for 2-oxoglutarate {ECO:0000269|PubMed:20228795}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:20228795, PubMed:29779229). Mediates the conversion of thebaine to neopinone (PubMed:20228795, PubMed:22098111). Catalyzes also, with lower efficiency, the 6-O-demethylation of oripavine to neomorphinone, which is converted spontaneously to morphinone (PubMed:20228795, PubMed:29779229). Supports dealkylation reactions such as O,O-demethylenation in the metabolism of protopine, benzo[c]phenanthridine, and rhoeadine alkaloids; cleaves a methylenedioxy bridge leaving two hydroxyl groups (PubMed:23928311). Catalyzes the O-demethylation of methylenedioxy bridges on protopine alkaloids such as allocryptopine (PubMed:23928311). No activity with (S)-reticuline, salutaridine, papaverine, (S)-corytuberine, (S)-scoulerine, pavine, noscapine or codeine (PubMed:20228795). {ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:23928311, ECO:0000269|PubMed:29779229, ECO:0000303|PubMed:29779229}. | Papaver somniferum (Opium poppy) |
D4N502 | DIOX3_PAPSO | METPILIKLGNGLSIPSVQELAKLTLAEIPSRYTCTGESPLNNIGASVTDDETVPVIDLQNLLSPEPVVGKLELDKLHSACKEWGFFQLVNHGVDALLMDNIKSEIKGFFNLPMNEKTKYGQQDGDFEGFGQPYIESEDQRLDWTEVFSMLSLPLHLRKPHLFPELPLPFRETLESYLSKMKKLSTVVFEMLEKSLQLVEIKGMTDLFEDGLQTMRMNYYPPCPRPELVLGLTSHSDFSGLTILLQLNEVEGLQIRKEERWISIKPLPDAFIVNVGDILEIMTNGIYRSVEHRAVVNSTKERLSIATFHDSKLESEIGPISSLVTPETPALFKRGRYEDILKENLSRKLDGKSFLDYMRM | 1.14.11.31; 1.14.11.32 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:20228795}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:20228795}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | methylation [GO:0032259]; morphine biosynthetic process [GO:0097295] | null | codeine O-demethylase activity [GO:0102805]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; thebaine 6-O-demethylase activity [GO:0102802]; thebane O-demethylase activity [GO:0102803] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + codeine + O2 = CO2 + formaldehyde + morphine + succinate; Xref=Rhea:RHEA:27413, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:57871, ChEBI:CHEBI:58097; EC=1.14.11.32; Evidence={ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:23928311, ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thebaine = CO2 + formaldehyde + oripavine + succinate; Xref=Rhea:RHEA:75955, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:59953, ChEBI:CHEBI:194499; EC=1.14.11.32; Evidence={ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:23928311, ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=(S)-scoulerine + 2-oxoglutarate + O2 = (S)-3-O-demethylscoulerine + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:75959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:17129, ChEBI:CHEBI:30031, ChEBI:CHEBI:194500; Evidence={ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:23928311, ECO:0000269|PubMed:29779229}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thebaine = CO2 + formaldehyde + neopinone + succinate; Xref=Rhea:RHEA:27477, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:59950, ChEBI:CHEBI:59953; EC=1.14.11.31; Evidence={ECO:0000269|PubMed:20228795}; CATALYTIC ACTIVITY: Reaction=(S)-reticuline + 2-oxoglutarate + O2 = (S)-6-O-demethylreticuline + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:76027, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:57873, ChEBI:CHEBI:194502; Evidence={ECO:0000269|PubMed:23928311}; CATALYTIC ACTIVITY: Reaction=(S)-tetrahydropalmatine + S-adenosyl-L-methionine = (S)-cis-N-methyltetrahydropalmatine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76047, ChEBI:CHEBI:16563, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194514; Evidence={ECO:0000269|PubMed:23928311}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=198 uM for (S)-scoulerine {ECO:0000269|PubMed:23928311}; KM=20.5 uM for codeine {ECO:0000269|PubMed:20228795}; KM=41.9 uM for thebaine {ECO:0000269|PubMed:20228795}; KM=19 uM for 2-oxoglutarate {ECO:0000269|PubMed:20228795}; Vmax=11.6 pmol/sec/mg enzyme with (S)-scoulerine as substrate {ECO:0000269|PubMed:23928311}; Note=kcat is 0.095 sec(-1) with (S)-scoulerine as substrate. {ECO:0000269|PubMed:23928311}; | PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:29779229). Mediates the conversion of codeine to morphine (PubMed:20228795, PubMed:22098111, PubMed:29779229). Catalyzes also, with lower efficiency, the 3-O-demethylation of thebaine to oripavine and of (S)-scoulerine to 3-O-demethylscoulerine (PubMed:20228795, PubMed:29779229). Supports, with a lower turnover, the conversion of codeinone to morphinone, of thebaine to neopinone, and of neopine to neomorphine (PubMed:29779229). Supports dealkylation reactions such as O,O-demethylenation in the metabolism of protopine, benzo[c]phenanthridine, and rhoeadine alkaloids; cleaves a methylenedioxy bridge leaving two hydroxyl groups (PubMed:23928311). Catalyzes the O,O-demethylenation of methylenedioxy bridges on protopine alkaloids such as allocryptopine, cryptopine and protopine (PubMed:23928311). No activity with (S)-reticuline, salutaridine, papaverine, (S)-corytuberine, oripavine, pavine or noscapine (PubMed:20228795). {ECO:0000269|PubMed:20228795, ECO:0000269|PubMed:22098111, ECO:0000269|PubMed:23928311, ECO:0000269|PubMed:29779229}. | Papaver somniferum (Opium poppy) |
D4NUX0 | HCT1_ACTRA | MVCIKSSCVVKPSEPTPNVKLFLPESDQVKPWTHAPVFFVYQPEVDNSVSTSLENLKFSLSRALVPYYPLAGRLNGIGGGRFELHCNTMGAVIIEAESDARLEDFGDFRPTSETTKLAPYVDYAKDVSELPLLLVQLTRFKCGGIGIGIAMSHIVSDGKGAFGFITTWAKINRGEKGIIEPFHDRTAFYKGDPTAKPRCDHVELKGYPVLLGNKSAKEERAKETTTRMLNLSKNQVDKLKEKSNLGKPKDYVGREYSRFEAMSGHIWRCASKARRHENEQLTSLRITIDCRNRLRPPLPPRYSGNATMVTTSIAESGELLSNPLGLGFVCSVIRKCIDKVDDDYIKSATDFLISQDDLTPYRSGFHNVGSTEGVFLGNPNLAITSWVGLPINDVDFGWGKPIYMGPTALGYDGKLLIIPGKDDGSVIVPIRLQVAHIDDFEKFFYEDI | 2.3.1.- | null | alkaloid metabolic process [GO:0009820]; phenylpropanoid metabolic process [GO:0009698]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV [GO:0009411] | null | hydroxycinnamoyltransferase activity [GO:0050734] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-4-coumaroyl-CoA = cimicifugate K + CoA; Xref=Rhea:RHEA:73319, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:192789, ChEBI:CHEBI:192790; Evidence={ECO:0000269|PubMed:31069522}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-caffeoyl-CoA = cimicifugate D + CoA; Xref=Rhea:RHEA:73323, ChEBI:CHEBI:57287, ChEBI:CHEBI:87136, ChEBI:CHEBI:192789, ChEBI:CHEBI:192791; Evidence={ECO:0000269|PubMed:31069522}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-sinapoyl-CoA = cimicifugate J + CoA; Xref=Rhea:RHEA:73327, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:192789, ChEBI:CHEBI:192792; Evidence={ECO:0000269|PubMed:31069522}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-piscidate + (E)-feruloyl-CoA = cimicifugate E + CoA; Xref=Rhea:RHEA:73331, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305, ChEBI:CHEBI:192789, ChEBI:CHEBI:192793; Evidence={ECO:0000269|PubMed:31069522}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.8 uM for 4-coumaroyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=10.5 uM for sinapoyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=16.3 uM for caffeoyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=51.4 uM for feruloyl-CoA (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; KM=32.3 uM for piscidic acid with 4-coumaroyl-CoA as cosubstrate (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31069522}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:31069522}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:31069522}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:31069522}; | FUNCTION: Catalyzes the formation of cimicifugic acids. Uses hydroxycinnamoyl-CoA thioesters as hydroxycinnamoyl donor substrates. Has a strict specificity for piscidic acid as an acceptor substrate as none of the various other acceptors tested including 4-hydroxyphenyllactic acid, malate, spermidine or tetrahydroxyhexanedioic acid are substrates. Donor substrates include 4-coumaroyl-CoA, caffeoyl-CoA, sinapoyl-CoA and feruloyl-CoA. No activity with cinnamoyl-CoA, isoferuloyl-CoA, 3,4-dimethoxycinnamoyl-CoA or 3,4-dihydroxybenzoyl-CoA as donors. In the reverse reaction with fukinolic acid and CoA as substrates, a formation of fukiic acid is evident. Hence, fukiic acid may also serve as an acceptor substrate. Involved in the biosynthesis of cimicifugic and possibly fukinolic acids. {ECO:0000269|PubMed:31069522}. | Actaea racemosa (Black cohosh) (Cimicifuga racemosa) |
D4P095 | CNPD3_PSEAI | MSRHSNTPATDASVLLVQLSDSHLFAEDGARLLGMDTAHSLEKVVERVAREQPRIDLILATGDVSQDGSLDSYTRFRRLSAPLAAPLRWFAGNHDEREPMQRATEGSDLLEQIVDVGNWRVVLLDSSIPGAVPGYLEDDQLDLLRRAIDSAGERFLLVSFHHHPVPIGSDWMDPIGLRNPQALFDLLAPYPQLRCLLWGHIHQEFDRQRGPLRLLASPSTCVQFAPGSSDFTLDRLAPGYRWLRLHDDGRLETGISRVDDVVFEVDYDTAGY | 3.1.4.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:20348254}; Note=Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe(3+) ions, while site 2 may have a preference for Fe(2+) ions. {ECO:0000269|PubMed:20348254}; | null | null | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00149; | 3.60.21.10; | Cyclic nucleotide phosphodiesterase class-III family | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:20348254}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.2 uM for cAMP {ECO:0000269|PubMed:20348254}; Vmax=3.4 nmol/min/ng enzyme {ECO:0000269|PubMed:20348254}; | null | null | null | FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specifically required for regulation of virulence factors. Can also hydrolyze cGMP, but cGMP is unlikely to be synthesized by P.aeruginosa and cAMP is probably the biologically relevant substrate for CpdA in vivo. {ECO:0000269|PubMed:20348254}. | Pseudomonas aeruginosa |
D4YWD1 | TPF_PELSA | FLGTINLSLCEEERDADEEERRDEPDESNVEVKKRFFFLSRIFGK | null | null | defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | PF03032; | null | Frog skin active peptide (FSAP) family, Temporin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20308076}. Target cell membrane {ECO:0000269|PubMed:20308076}. Note=Inserts into the lipid bilayer with an in-plane (parallel) orientation. {ECO:0000269|PubMed:20308076}. | null | null | null | null | null | FUNCTION: Non-amphipathic alpha-helical antimicrobial peptide with potent activity against some Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus (MRSA)), weak activity against Gram-negative bacteria and no activity against fungi (PubMed:20308076, PubMed:26181487, PubMed:27915018). Permeabilizates membranes through a detergent-like effect probably via the carpet mechanism (PubMed:20308076). More precisely, it strongly and selectively perturbs anionic bilayers membranes by interacting with the polar headgroups and the glycerol backbone region of the phospholipids, hence disrupting the acyl chain packing of the bilayer (PubMed:20308076). Is not active against Leishmania (promastigote and axenic amastigote forms) (PubMed:20308076). Does not show hemolytic activity (PubMed:20308076, PubMed:26181487). Does not show toxicity for human THP-1-derived macrophages (PubMed:26181487). {ECO:0000269|PubMed:20308076, ECO:0000269|PubMed:26181487, ECO:0000269|PubMed:27915018}. | Pelophylax saharicus (Sahara frog) (Rana saharica) |
D4Z2G1 | LINB_SPHIU | MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIACDLIGMGDSDKLDPSGPERYAYAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARRHRERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFINAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA | 3.8.1.5 | null | response to toxic substance [GO:0009636] | periplasmic space [GO:0042597] | haloalkane dehalogenase activity [GO:0018786] | PF00561; | 3.40.50.1820; | Haloalkane dehalogenase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10464214}. | CATALYTIC ACTIVITY: Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol + H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01231, ECO:0000269|PubMed:10100638, ECO:0000269|PubMed:9293022}; CATALYTIC ACTIVITY: Reaction=(3R,6R)-1,3,4,6-tetrachlorocyclohexa-1,4-diene + 2 H2O = 2,5-dichlorocyclohexa-2,5-dien-1,4-diol + 2 chloride + 2 H(+); Xref=Rhea:RHEA:11944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:18904, ChEBI:CHEBI:28975; Evidence={ECO:0000269|PubMed:7691794}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for 1,2-dibromoethane {ECO:0000269|PubMed:9293022}; KM=3.9 mM for 1-chloro-2-bromoethane {ECO:0000269|PubMed:9293022}; KM=0.9 mM for 1,2-dibromopropane {ECO:0000269|PubMed:9293022}; KM=0.05 mM for 1-bromo-2-methylpropane {ECO:0000269|PubMed:9293022}; KM=0.7 mM for 2,3-dichloropropene {ECO:0000269|PubMed:9293022}; KM=0.14 mM for 1-chlorobutane {ECO:0000269|PubMed:10100638}; Note=kcat is 0.98 sec(-1) with 1-chlorobutane as substrate. {ECO:0000269|PubMed:10100638}; | PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane degradation. {ECO:0000305|PubMed:7691794}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:9293022}; | null | FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols are good substrates (PubMed:10100638, PubMed:9293022). Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog (PubMed:9293022). Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL) (PubMed:7691794). This degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and energy. {ECO:0000269|PubMed:10100638, ECO:0000269|PubMed:7691794, ECO:0000269|PubMed:9293022}. | Sphingobium indicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S) (Sphingobium japonicum) |
D5ARP7 | CCOP_RHOCB | MSKKPTTKKEVQTTGHSWDGIEELNTPLPRWWLWTFYATIVWGVAYSIAMPAWPIFASGATPGILGSSTRADVEKDIAKFAEMNKAVEDKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGSIETIYTNIKHGIRDPLDPDTLPVANMPAHLTDELLEPAQIDDVVQYVLKISGQPADEARATAGQQVFADNCVSCHGEDAKGMVEMGAPNLTDGIWLYGGDANTITTTIQLGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8130227}; Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8130227}; | oxidative phosphorylation [GO:0006119]; proton transmembrane transport [GO:1902600] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF00034;PF13442;PF14715; | 6.10.280.130;1.10.760.10; | CcoP / FixP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305|PubMed:17143652, ECO:0000305|PubMed:18556791, ECO:0000305|PubMed:20952576, ECO:0000305|PubMed:8130227, ECO:0000305|PubMed:9473054}. | null | null | FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The complex also functions as a proton pump. {ECO:0000250|UniProtKB:Q3J015, ECO:0000269|PubMed:17143652, ECO:0000269|PubMed:18556791, ECO:0000269|PubMed:20952576, ECO:0000269|PubMed:8130227, ECO:0000269|PubMed:9473054, ECO:0000303|PubMed:20952576}. | Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) |
D5AUZ9 | CBIM_RHOCB | MHIMEGYLPVTHAIGWSLAAGPFVVAGAVKIRKIVAERPEARMTLAASGAFAFVLSALKIPSVTGSCSHPTGTGLGAVVFGPSVMAVLGVIVLLFQALLLAHGGLTTLGANAFSMAIVGPWVAWGVYKLAGKAGASMAVAVFLAAFLGDLATYVTTSLQLALAYPDPVSGFLGAALKFGSVFALTQIPLAIAEGFLTVIVVDALAGKVDDKDKLRILAGEAR | null | null | cobalamin biosynthetic process [GO:0009236]; cobalt ion transport [GO:0006824] | ATP-binding cassette (ABC) transporter complex [GO:0043190] | cobalt ion transmembrane transporter activity [GO:0015087] | PF01891; | 1.10.1760.20; | CbiM family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:20868747}; Multi-pass membrane protein {ECO:0000305|PubMed:20868747}. | null | null | PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. | null | null | FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. A Cbi(MN) fusion protein has about 70% import capacity, but the holo-Cbi(MN)QO complex cannot be isolated, suggesting CbiN may destabilize it. {ECO:0000269|PubMed:16352848, ECO:0000269|PubMed:20868747}. | Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) |
D5CBA0 | CDIA_ENTCC | MMKQDQVRFSQRALSALLSVLLATQPLLPAVAASITPSGNTQMDKAANGVPVVNIATPNQSGISHNKYNDYNVGKEGLILNNATGQLNQTQLGGLIQNNPNLKAGQEAKGIINEVTGANRSNLQGYTEVAGKAANVIVANPYGITCNGCGFINTPNVTLTTGKPVLDASGKLQSLDVTQGAVTIEGAGLNGSQSDAVSIISRATEINVQLHAKDLRVVAGANRVAADGSVSALKGEGTAPKVAVDTGALGGMYANRIRLVSSETGVGVNLGNLNARQGDIALSSAGKVVLKNTLASGSTTVSAADVTLRGDHKAGGNVTVSGQTALTLDQAHVAADNNLQLTTRGTLTQNGGAFTAANDATLAATTLIQSVDAQASAGRHLAVNAEKNAALNGSVVAGQQLSVKGGELVQQGNLSASEIALNAQTLTQESRSTTNASGNITLTTSGHSQLKGSTTAGQSLAVSAGSLANHGALAAVADTRINTGIFSNTGTVQGNSLTVSGTDITSSGALKSASTLDIRADNATLSGETGAKGKTTVTASGNLNNSGTLISDDTLTLNAAQIVNSGTLSGVRGLTTSGKTFTASATSVTQSDGDVALNNTDTTLAGETSAGGAVTVQGRSLNTTATAQTQGNSVGVAVQNAKLEGTQAAKGNMTLKADSSLNHTGKSSASGLKVETGHLSNSGTLTASALVIDSPEVINGGLIHAGQTLSLVTRLLDNRSSGVLYSPSALSLSLSELNNAGIITSDAALSLSGSNLTNSGELSGTSLAIDYETLKNSAEGMLLAQGANRITAQSVSSAGSMVGNTLTLNADRLESAGLLQGDSALSLTAGILNLLTGSRTLTGGALGLSGTTLTTAGQLQGQDVSIRSHDWTNRGSSLATGSLDVTTAGTLSNTGELMSQGNGTLNAVTTVNSGNMLSAGDLSLNGKTLRNSGTLQGNRVTAHQDTITNSGTLTGIAALMLAARLEMAAPLLTLVNDASGSLLTAGELSVTGGDLRNAGQWQGKRVLIHAQALTNGGAIQAENLLDAQIDSTLTGTAGSKITSNGELALSALTLANSGQWIAKHLTLGASTLNNSGEITGVVALSVALTQLNNQAGGKLLSAGALTLDVENATNAGQIQGKATTVTAGQLINSGRLQGEALTLNASGALNNTASGVLLSENALTVSTATLNNQGTLQGGGESSVKATTRVQNDGKMLSGGKLTLTAPELANSSSGLVQAVRLLLDVVKAVNGGNVLATTRAELRGSSLDNSGTLQGADLQANYQSVTNSGTVLGTTSLTINGDALDNTESGKLYSGDKLLLDVRNYSGRGDVVSLGDTTLKLVNALVNTGTLAASKTLSVSSQNAMTNSGVMQGNAIALSAGGAFTNNGTLTTGNGSSTFNAQSLLLNASGSLQAGGDVQLTSRENITVNGFTGTAGSLTMTAAGTLLNTALIYAGNNISLFAARIHNIYGDILADNSLWMQKNAVGEANAEVVNRSGTIETTRGDITVNTGHLLNEADGLTVSQSEREYPDAIPAADEHYFSYDLNGRRSDFVLLLEDWKNDGSKVVYDWYEQCLGSGANGSGQCRDRVDYRLTGEDIRQFLLSESVVSVSATGSSARIAAGRDITINAGTLDNRASHILAGRNAVLAGGTLNNLSAEGGRRVTYVQAEYRCEWFYRDCSDSKWEPLTQYPDGSWGWFDEDYGWYGWVPYILGERTTEFVADGGVYRSVISAGGNVSANFTSDISNTNVTANSGEFSNTIDAPTLNTLSPEAIGKGLNSESLAQGGSADIRFPEQLGNITDALKDISGGSSLSDQNGSSGNYPLPSGNNGYFVPSTDPDSPYLITVNPKLDELGNMDDSLFNGLYDLLGITPGATPRETNSAYTDRNQFLGSSYFLDRLGLNPDRDYRFLGDAAFDTRYVSNAILNQTGSRYINGIGSDLDQMRYLMDSAAEQQKTLGLKFGVALTAEQVAALDKSMLWWESATINGQTVMIPKVYLSPKDVTVHSGSVISGNNVQLAGGNVINSGSTIAAQNGLSIDSSNSLSNLNAGLLSAGGGLNLSALGDINNIGSTISGKTVGLESVAGSINNITRAQQWNVDAGNVHFSGTDVGKTASITATDGLTMRAGQDINVTGANVSAGGSLGMAAGNDINITANEIVTSEGRAGRNRATTETASVTHQGSTLSAGDDLTLQAGNDVNARAAAIAAEGDVGIQAGRDVDLLAEASMERSSSQAKKKTAIDESVRQQGTEIASGGNTVILAGRDVTAQAADVTAQGDIGVAAGRDVNLTTATESDYRYREQTKTSSGFLSKKTTHTIEEESATREKGSLLSGDNVTVSAGNNLRVLGSAVAGDGDVALSAGNNVDIVAATNTDTAWRFKETKKSGLMGTGGIGFTIGSSKSTHDLREQGTTQSESFSTVGSTGGNVSIAAGKQAHIGGADIIAQKDISLTGDSVVIEPGHDKRTRDEKFEQKSSGLTVALSGAAGSAVNNAVTTAQSAKQSSDSRLAALQGTQAALSGVQAGQAVALDQVKGDSDKRNNNTIGVSASIGSQSSKSSSHMESETTTGSTLSAGNNVTIKATGSDITVAGSQIKAGKDVTLDAARDVNLIASQDTQQTTGKNSSSGGSLGVGVGVGSGGAGISISANANSSKGHEKGNGVWQNETTVDAGNRVTINTGRDATIAGAQVSGETVVADIGRDLTIASTQDSDHYNSKQNSVSGGAGYTFGAGGFSGSINVSRDKMTSDYDSVQEQSGLFAGNGGFDVTVGNHTQLDSGVIASTATADKNRLDTGTLGFSDIHNQADFKTEHQGAGISSGGSIGKQFAGNMANALLAGGGNSGHAEGTTQAAVSEGTLIIRDKENQKQDVADLSRDAEHANGSISPIFDKEKEQQRLQEVQLIGEIGSQVVDIANTQGEINGLNAGRKELADKGITEPGADASDEVKAAYQNALRETDAYKTTTAKYGTGSDLQRGIQAATAALQGLAGSDLTAALAGASAPELAYRIGHGMGIDNNTAAKTIAHAILGGAVAALQGNSAAAGAAGAATGELAAKAIAGMLYPDVKDLSTLSEEQKQTVSALATISAGMAGGLAGDSTGSAVAGGQAGKNAAENNSLALVARGCAVAAPCRTKVAEQLLEIGAKAGIAGLAGAAVKDMADKMTSDELEHLVTLEMMGNDEIIAKYVSLLHDKYAPSHTGGNLLPETLPGHTGNNTGSVDTGPNHTGNTNRQNDSGSNNTGNTEGAPNTGGNTTITPIPNGPSKDDIAYLALKGKEAQEAASNLGFDRRIPPQKAPFNSHGQPVFYDGKNYITPDIDSHNVTNGWKMFNSKGKRIGTYDSGLNRIKD | 3.1.-.- | null | null | host cell cytoplasm [GO:0030430] | RNA endonuclease activity [GO:0004521]; toxin activity [GO:0090729] | PF13332;PF15526;PF04829;PF05860; | 3.10.380.20;2.160.20.10; | CdiA toxin family | null | SUBCELLULAR LOCATION: Target cell, target cell cytoplasm {ECO:0000269|PubMed:24657090, ECO:0000269|PubMed:24889811, ECO:0000269|PubMed:25174572}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable). Toxin translocation into the target cell depends on the proton motive force of the target cell, but not on tolA or tonB. {ECO:0000269|PubMed:25174572, ECO:0000305}. | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion; upon forced induction decreases E.cloacae target cell counts about 20-fold, about 100-fold in E.coli. Intracellular expression of CdiA-CT (residues 3087-3321) inhibits E.coli cell growth when induced, but coexpression with its cognate immunity protein CdiI allows cell growth. Cleaves 16S rRNA in vivo and in vitro between adenine 1493 and guanosine 1494 of E.coli 16S rRNA. Inhibition of 16S rRNA cleavage is specific to the cognate immunity protein, non-cognate CdiI from E.chrysanthemi strain EC16 does not inhibit this protein (PubMed:24657090). Purified CdiA-CT inhibits E.coli cell growth when added to cultures but not when added as a complex with cognate CdiI, suggesting cognate CdiI prevents import into the target cell. CdiA-CT (without CdiI) is probably imported in an F-pilus-mediated fashion, although it is not clear if this is physiologically significant (PubMed:24889811). Gains access to the cytoplasm of target cells by using integral inner membrane protein FtsH (PubMed:26305955). {ECO:0000269|PubMed:24657090, ECO:0000269|PubMed:24889811, ECO:0000269|PubMed:26305955}.; FUNCTION: The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein (FtsH for this CDI). {ECO:0000305}. | Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56) |
D5EY13 | XYFA_XYLR2 | MKKLLVALSLIAGSLTASAQWGRPVDYAAGPGLKDAYKDYFTVGVAVNKFNISDPAQTAIVKKQFNSVTAENAWKPGEIHPKEGVWNFGLADSIANFCRENGIKMRGHCLCWHSQFADWMFTDKKGKPVKKEVFYQRLREHIHTVVNRYKDVVYAWDVVNEAMADDGRPFEFVDGKMVPASPYRQSRHFKLCGDEFIAKAFEFAREADPTGVLMYNDYSCVDEGKRERIYNMVKKMKEAGVPIDGIGMQGHYNIYFPDEEKLEKAINRFSEIVNTIHITELDLRTNTESGGQLMFSRGEAKPQPGYMQTLQEDQYARLFKIFRKHKDVIKNVTFWNLSDKDSWLGVNNHPLPFDENFKAKRSLQIIRDFDAAMDNRKPKEDFVPNPMNQPGQEYPMVNSEGYARFRVEAPDAKSVIVSLGLGGRGGTVLRKDKNGVWTGTTEGPMDPGFHYYHLTIDGGVFNDPGTHNYFGSCRWESGIEIPAKDQDFYAYRKDINHGNIQQVTFWSESTGKMQTANVYLPYGYGKVVKGKQERYPVLYLQHGWGENETSWPVQGKAGLIMDNLIADGKIKPFIVVMAYGLTNDFKFGSIGKFTAEEFEKVLIDELIPTIDKNFLTKADKWNRAMAGLSMGGMETKLITLRRPEMFGYWGLLSGGTYMPEEIKDPKAVKYIFVGCGDKENPEGINKSVEALKAAGFKAEGLVSEGTAHEFLTWRRCLEKMAQSLFK | 3.1.1.73; 3.2.1.8 | null | xylan catabolic process [GO:0045493] | null | endo-1,4-beta-xylanase activity [GO:0031176]; feruloyl esterase activity [GO:0030600] | PF00756;PF00331; | 3.40.50.1820;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 10 (cellulase F) family | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}; CATALYTIC ACTIVITY: Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for xylanase activity. {ECO:0000269|PubMed:19304844}; | null | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has endo-xylanase activity towards substrates such as oat spelt xylan (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing primarily xylobiose; cannot hydrolyze xylobiose to xylose. Also has feruloyl esterase activity, releasing ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters. Exhibits negligible acetyl esterase activity on sugar acetates. Acts synergistically with Xyl3A to increase the release of xylose from xylan. Does not possess endoglucanase or mannanase activities since it is not able to hydrolyze carboxymethyl cellulose and locust bean gum. {ECO:0000269|PubMed:19304844, ECO:0000269|PubMed:21742923}. | Xylanibacter ruminicola (strain ATCC 19189 / DSM 19721 / CIP 105475 / JCM 8958 / 23) (Prevotella ruminicola) |
D5EY15 | XYL3A_XYLR2 | MKYQLFLSLALCVGLGASAQTLPYQNPNLSAKERAVDLCSRLTLEEKAMLMLDESPAIPRLGIKKFFWWSEALHGAANMGNVTNFPEPVGMAASFNPHLLFKVFDIASTEFRAQYNHRMYDLNGEDMKMRSLSVWTPNVNIFRDPRWGRGQETYGEDPYLTSVMGVQVVKGLQGPEDARYRKLWACAKHYAVHSGPEYTRHTANLTDVSARDFWETYMPAFKTLVKDAKVREVMCAYQRLDDDPCCGSTRLLQQILRDEWGFEYLVVSDCGAVSDFYENHKSSSDAVHGTSKAVLAGTDVECGFNYAYKSLPEAVRKGLLSEKEVDKHVIRLLEGRFDLGEMDDPSLVEWSKIPYSAMSTKASANVALDMARQTIVLLQNKNNILPLKKNAEKIAIIGPNAHNEPMMWGNYNGTPNHTVTILDGVKAKQKKLVYIPGCDLTNDKVMECHLATDCVTPDGKKGLKGTFWNNTEMAGKPFTTEYYTKPVNVTTAGMHVFAPNLPIEDFSAKYETTFTAKEAGEYVVNVESTGHFELYVNGKQQFVNHIWRATPTRTVLKAEKGQKFDIEVRFQTVKTWGASMKIDVARELNIDYQETIAQLKGINKVIFCGGIAPSLEGEEMPVNIEGFKGGDRTSIELPKVQREFLKALKAAGKQVIYVNCSGSAIALQPETESCDAIVQAWYPGQEGGTAVADVLFGDYNPGGKLSVTFYKNDQQLPDYEDYSMKGRTYRYFDDALFPFGYGLSYTTFEVGEAKVEAATDGALYNVQIPVTNTGTKNGSETIQLYIRNLQDPDGPLKSLRGFERLDIKAGKTATANLKLTKESLEFWDAETNTMRTKPGKYEILYGTSSLDKDLKKLTITL | 3.2.1.37; 3.2.1.55 | null | arabinan catabolic process [GO:0031222]; xylan catabolic process [GO:0045493] | null | alpha-L-arabinofuranosidase activity [GO:0046556]; xylan 1,4-beta-xylosidase activity [GO:0009044] | PF14310;PF00933;PF01915;PF07691; | 3.40.50.1700;3.20.20.300;2.60.40.10; | Glycosyl hydrolase 3 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:19304844}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55; Evidence={ECO:0000269|PubMed:19304844}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for pNP-beta-D-xylopyranoside (pNPX) (at 37 degrees Celsius and pH 5.0) {ECO:0000269|PubMed:19304844}; Note=kcat is 9.7 sec(-1) for the beta-xylosidase activity with pNPX as substrate (at 37 degrees Celsius and pH 5.0).; | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:19304844}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:19304844}; | null | FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has beta-xylosidase activity via its capacity to hydrolyze glycosidic linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 to X6), releasing xylose monomers. To a much lesser extent, also has alpha-L-arabinofuranosidase activity. Does not possess beta-D-glucosidase activity. Acts synergistically with Xyn10D-Fae1A to increase the release of xylose from xylan. {ECO:0000269|PubMed:19304844}. | Xylanibacter ruminicola (strain ATCC 19189 / DSM 19721 / CIP 105475 / JCM 8958 / 23) (Prevotella ruminicola) |
D5JWB3 | SARED_ESCCA | MADSSKKLTVLLSGASGLTGSLAFKKLKERSDKFEVRGLVRSEASKQKLGGGDEIFIGDISDPKTLEPAMEGIDALIILTSAIPRMKPTEEFTAEMISGGRSEDVIDASFSGPMPEFYYDEGQYPEQVDWIGQKNQIDTAKKMGVKHIVLVGSMGGCDPDHFLNHMGNGNILIWKRKAEQYLADSGVPYTIIRAGGLDNKAGGVRELLVAKDDVLLPTENGFIARADVAEACVQALEIEEVKNKAFDLGSKPEGVGEATKDFKALFSQVTTPF | 1.3.1.107 | null | response to toxic substance [GO:0009636] | chloroplast [GO:0009507] | oxidoreductase activity [GO:0016491] | PF13460; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=dihydrosanguinarine + NADP(+) = NADPH + sanguinarine; Xref=Rhea:RHEA:41656, ChEBI:CHEBI:17183, ChEBI:CHEBI:17209, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.107; Evidence={ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}; CATALYTIC ACTIVITY: Reaction=dihydrosanguinarine + NAD(+) = NADH + sanguinarine; Xref=Rhea:RHEA:41660, ChEBI:CHEBI:17183, ChEBI:CHEBI:17209, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.107; Evidence={ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}; CATALYTIC ACTIVITY: Reaction=dihydrochelirubine + NAD(+) = chelirubine + NADH; Xref=Rhea:RHEA:41664, ChEBI:CHEBI:17031, ChEBI:CHEBI:17789, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.107; Evidence={ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}; CATALYTIC ACTIVITY: Reaction=dihydrochelirubine + NADP(+) = chelirubine + NADPH; Xref=Rhea:RHEA:41668, ChEBI:CHEBI:17031, ChEBI:CHEBI:17789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.107; Evidence={ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.5 uM for sanguinarine (in the presence of 40 uM NADH) {ECO:0000269|PubMed:17080644}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:17080644}; | null | FUNCTION: Catalyzes the reduction of benzophenanthridines, preferentially sanguinarine, to the corresponding dihydroalkaloids. Involved in detoxifying the phytoalexins produced by plant itself. The sanguinarine produced by intact cells upon elicitation, after excretion and binding to cell wall elements, is rapidly reabsorbed and reduced to the less toxic dihydrosanguinarine. Can work with both NAD(P) or NAD as a hydrogen donor, but at low concentrations, the reaction velocity with NAD(P)H is threefold higher than with NADH. However, chelerythrine shows maximum conversion rates with NADH. The substrate preference is sanguinarine > chelerythrine > chelirubine, macarpine or 10-OH-chelerythrine. No activity with berberine or phenanthridine cations. {ECO:0000269|PubMed:17080644, ECO:0000269|PubMed:20378534}. | Eschscholzia californica (California poppy) |
D5KXD2 | TPS12_SOLLC | MASSSANKCRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFINQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESTVSNLSNNNSLKAEVTEAFSQPIRMTLPRVGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNNAIQRWDINAIDSVPPYLRHAYQALLDIYSEMEQALAKEFKSDRVYYAKYEMKKLVRAYFKEAQWLNNDNHIPKYEEHMENAMVSAGYMMGATTCLVGVEEFISKETFEWMINEPLIVRASSLIARAMDDIVGHEVEQQREHGASLIECYMKDYGVSKQEAYVKFQKEVTNGWMDINREFFCPDVEVPKFVLERVLNFTRVINTLYKEKDEYTNSKGKFKNMIISLLVESVEI | 4.2.3.-; 4.2.3.104; 4.2.3.106; 4.2.3.113; 4.2.3.15; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + gamma-curcumene; Xref=Rhea:RHEA:68784, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:63696; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68785; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019, ChEBI:CHEBI:49238, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:20431087, PubMed:21813655, PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-curcumene and (Z)-gamma-bisabolene (PubMed:20431087, PubMed:21813655, PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene and terpinolene (PubMed:21818683). {ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
D5LGE0 | AIP_HYAAS | MNYLCLVVTLVAVAGAISGEKFSDDNTGYQSTPSLRIRTTPGRRRQTPRTIGPPYTRRTLRTTTDYSTTVENGNLTTPAANSTEKGNGLYGLRRQTPRTIGPPYTRRTLRTTTGYWTTVEKGNGTTPAANSTEKGNRPYGRRRQTPRTIGPPYTRRTTTDYWAAVEKGYLTTPAANSTEKESRPNATQRREISWTFGPLYTWRTTKGYGTTLETTNATSTS | null | null | null | extracellular region [GO:0005576] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20178988}. | null | null | null | null | null | FUNCTION: [Hyalomin-A1]: Suppress host inflammatory response. Exerts significant anti-inflammatory functions, either by directly inhibiting host secretion of inflammatory factors such as tumor necrosis factor-alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-gamma (IFNG) or by indirectly increasing the secretion of immunosuppressant cytokine of interleukin-10 (IL10). Also potently scavenges free radical in vitro in a rapid manner. All tested concentrations of this peptide have little effect on the cell viability. In vivo, inhibits hind paw adjuvant-induced inflammation in mouse in a dose-dependent manner. {ECO:0000269|PubMed:20178988}.; FUNCTION: [Hyalomin-B1]: Suppress host inflammatory response. Exerts significant anti-inflammatory functions, either by directly inhibiting host secretion of inflammatory factors such as tumor necrosis factor-alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-gamma (IFNG) or by indirectly increasing the secretion of immunosuppressant cytokine of interleukin-10 (IL10). Also potently scavenges free radical in vitro in a rapid manner. Low concentrations of this peptide have little effect on the cell viability, whereas high concentrations increase the cell viability by 10-20%. In vivo, inhibits hind paw adjuvant-induced inflammation in mouse in a dose-dependent manner. {ECO:0000269|PubMed:20178988}.; FUNCTION: [Hyalomin-B2]: Not studied but probably similar to Hyalomin-B1. {ECO:0000305}.; FUNCTION: [Hyalomin-B3]: Not studied but probably similar to Hyalomin-B1. {ECO:0000305}. | Hyalomma asiaticum asiaticum (Tick) |
D5MP61 | 3XYN1_VIBSX | MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKSNWQQEIAKGQYINHSETLFETLGYGSTGGGDNGGGDNGGTNPPEPCNEEFGYRYVSDSTIEVFHKNNGWSAEWNYVCLNGLCLQGEIKNGEYVKQFDAQLGSTYGIEFKVADGESQFITDKSVTFENKQCGSTGTPGGGDNGSGGDNGGDNGSGGDNGSGGGTDPSQCSADFGYNYRSDTEIEVFHKDLGWSASWNYICLDDYCVPGDKSGDSYNRSFNATLGSDYKITFKVEDSASQFITEKNITFVNTSCAQ | 3.2.1.32 | null | cellulose catabolic process [GO:0030245]; xylan catabolic process [GO:0045493] | null | polysaccharide binding [GO:0030247]; xylan endo-1,3-beta-xylosidase activity [GO:0033905] | PF11606; | 2.60.40.2450;3.20.20.80; | Glycosyl hydrolase 26 family | null | null | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.; EC=3.2.1.32; Evidence={ECO:0000269|PubMed:15743273}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.4 mM for beta-1,3-xylotetraose {ECO:0000269|PubMed:15743273}; KM=7.5 mM for beta-1,3-xylopentaose {ECO:0000269|PubMed:15743273}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:15743273}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:15743273}; | FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydrolyze beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or p-nitrophenyl-beta-xyloside. {ECO:0000269|PubMed:15743273}. | Vibrio sp |
D5MTF8 | HGL1D_WHEAT | MALLAAATLNPTTHLSLRSRAGRNSENLWLRSAASSQKSKGRFCNLTVRAGTPSKPAEPIGPVFTKLKPWQIPKRDWFDKDFLFGASTSAYQIEGAWNEDGKGPSTWDHFCHKYPERISDGTNGDVAADSYHLYEEDVKALKDMGMKVYRFSISWSRILPNGTGEVNQAGIDYYNKLINSLISHDIVPYVTIWHWDTPQALEDKYGGFLDPQIVDDYKQFAKLCFESFGDRVKNWFTFNEPHTYCCFSYGEGIHAPGRCSPGMDCAVPEGDSLREPYTAGHHILLAHAEAVEMFRTHYNMHGDSKIGMAFDVMGYEPYQDSFLDDQARERSIDYNLGWFLEPVVRGDYPFSMRSLIGDRLPVFTKEEQEKLASSCDIMGLNYYTSRFSKHVDISPDVTPKLNTDDAYASSETTGSDGNDIGPITGTYWIYMYPKGLTDLLLIMKEKYGNPPIFITENGIADVDGDETMPDPLDDWKRLDYLQRHISAVKDAIDQGADVRGHFTWGLIDNFEWGSGYSSRFGLVYIDKNDGFKRKLKKSAKWFSKFNAVPKHLLGTTKPTGQAPV | 3.2.1.182; 3.2.1.21 | null | carbohydrate metabolic process [GO:0005975] | chloroplast [GO:0009507] | beta-glucosidase activity [GO:0008422]; DIMBOA glucoside beta-D-glucosidase activity [GO:0102726]; scopolin beta-glucosidase activity [GO:0102483] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; CATALYTIC ACTIVITY: Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA; Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182; Evidence={ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; CATALYTIC ACTIVITY: Reaction=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA; Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182; Evidence={ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=1.83 mM for DIBOA-beta-D-glucoside (with recombinant enzyme) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.272 mM for DIMBOA-beta-D-glucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.79 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=2.02 mM for HBOA-beta-D-glucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.32 mM for HMBOA-beta-D-glucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=1.7 mM for p-nitrophenyl beta-D-glucopyranoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=1.78 mM for p-nitrophenyl beta-D-galactopyranoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=3.11 mM for p-nitrophenyl beta-D-xyloside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.67 mM for p-nitrophenyl beta-D-fucoside (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; KM=0.24 mM for esculin (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-galactopyranoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with native hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; Note=kcat is 5728 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 330 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme).; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}; | null | FUNCTION: Acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895}. | Triticum aestivum (Wheat) |
D5TM67 | CDAS_BACT1 | MHEWGLSEELKIQTKQMIEIAEKELSIMRNAIDKEDECILCKMEDIHHMLANVQTLAATYYIQAYLSPYTESSSFITTAIQHLSARKHGALIVVERNETLEALIQTGTTLNAHLTAPLLESIFYPGNPLHDGAVLVKNNHIVSAANILPLTKSTEVDPELGTRHRAAIGLSEKSDALILVVSEETGRTSFALNGILYTISL | 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26441857}; | cAMP biosynthetic process [GO:0006171]; sporulation resulting in formation of a cellular spore [GO:0030435] | null | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408] | PF10372;PF02457; | 3.40.1700.10;1.10.287.770; | Adenylate cyclase family, DacB/CdaS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_00838, ECO:0000269|PubMed:26441857}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26441857}; | null | FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this bacteria catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). It has slow DAC activity with ADP as a substrate and may have weak ADPase activity (PubMed:26441857). Required for efficient spore formation, whereas in B.subtilis, it is required for efficient spore germination. It is produced under the control of different sigma factors in the two bacteria. It is also required for parasporal crystal formation (PubMed:26441857). {ECO:0000269|PubMed:26441857}. | Bacillus thuringiensis (strain BMB171) |
D5VRB9 | ELP3_METIM | MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKRGEFKPYREEEAIEVISYAKSIMPKWVRTSRIQRDIPATVIVDGVKKSNLGELVYKYMEKKGLRCRCIRCREVGHVYYKKGILPDPEHIKLVREDYEASGGTEIFLSFEDVKNDILIAFLRLRDPYKPFRKEIDDKTMLVRQLHVFGWEKALTRDIKEVSWQHMGYGRMLMKEAERIAKEEFGKKKILVTSGIGVREYYRKLGYKRVGAYMGKEL | 2.3.1.311 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q02908}; | tRNA acetylation [GO:0051391]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047]; tRNA binding [GO:0000049]; tRNA uridine(34) acetyltransferase activity [GO:0106261] | PF00583;PF04055;PF16199; | 3.40.630.30;3.20.20.70; | ELP3 family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74882; EC=2.3.1.311; Evidence={ECO:0000269|PubMed:25151136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; Evidence={ECO:0000269|PubMed:25151136}; | null | PATHWAY: tRNA modification. {ECO:0000269|PubMed:25151136, ECO:0000269|PubMed:30733442}. | null | null | FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:25151136, PubMed:30733442). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule (PubMed:25151136). Does not show protein lysine acetyltransferase activity (PubMed:30733442). {ECO:0000269|PubMed:25151136, ECO:0000269|PubMed:30733442}. | Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME) |
D6MZJ6 | NSMA5_MOUSE | MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLEWVEEFEAENRQSDEAVAFSVLLGDLNFDNCSQDHAKEQGHKLFSCFQDPCRLGVCQEQPWALGTILNSSMLRHSIACSPEMLRRALRQEKGRRLYLSGPLHGSYPAQSWKGRRLDYITYRRVPGSRLSPEAEQVTFSTAFAGLTDHLAMGLKLQVVCS | 3.1.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20378533}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20378533}; | ceramide biosynthetic process [GO:0046513]; ceramide metabolic process [GO:0006672]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767] | null | 3.60.10.10; | Neutral sphingomyelinase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20378533}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:F1QG30}; Intermembrane side {ECO:0000250|UniProtKB:F1QG30}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20378533}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:20378533}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000305|PubMed:20378533}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-hexadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72959, ChEBI:CHEBI:78646, ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:20378533}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45645; Evidence={ECO:0000305|PubMed:20378533}; | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:20378533}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20378533}; | null | FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000250|UniProtKB:F1QG30}. | Mus musculus (Mouse) |
D6PXE8 | VM3B_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTMTHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQGYCYNRTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCGMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF01562;PF01421; | 3.40.1620.60;3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc protease that inhibits the classical and alternative pathways of complement by cleaving factor B, C6, C7, and C8. Also slowly and selectively degrades alpha-chain of fibrinogen (FGA), and shows edema-inducing activity. {ECO:0000269|PubMed:20837040}. | Naja atra (Chinese cobra) |
D6R8X8 | HYUP_MICLQ | MNSTPIEEARSLLNPSNAPTRYAERSVGPFSLAAIWFAMAIQVAIFIAAGQMTSSFQVWQVIVAIAAGCTIAVILLFFTQSAAIRWGINFTVAARMPFGIRGSLIPITLKALLSLFWFGFQTWLGALALDEITRLLTGFTNLPLWIVIFGAIQVVTTFYGITFIRWMNVFASPVLLAMGVYMVYLMLDGADVSLGEVMSMGGENPGMPFSTAIMIFVGGWIAVVVSIHDIVKECKVDPNASREGQTKADARYATAQWLGMVPASIIFGFIGAASMVLVGEWNPVIAITEVVGGVSIPMAILFQVFVLLATWSTNPAANLLSPAYTLCSTFPRVFTFKTGVIVSAVVGLLMMPWQFAGVLNTFLNLLASALGPLAGIMISDYFLVRRRRISLHDLYRTKGIYTYWRGVNWVALAVYAVALAVSFLTPDLMFVTGLIAALLLHIPAMRWVAKTFPLFSEAESRNEDYLRPIGPVAPADESATANTKEQNQR | null | null | null | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; nucleobase transmembrane transporter activity [GO:0015205] | PF02133; | 1.10.4160.10; | Purine-cytosine permease (2.A.39) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16621827}; Multi-pass membrane protein {ECO:0000305|PubMed:18927357, ECO:0000305|PubMed:20413494}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:16621827}; | null | FUNCTION: Nucleobase-proton symporter that mediates the sodium-dependent binding and uptake of 5-aryl-substituted hydantoin compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5-benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydantoin and for the L isomer over the D isomer (PubMed:16621827, PubMed:24952894). {ECO:0000269|PubMed:16621827, ECO:0000269|PubMed:24952894, ECO:0000305|PubMed:16116274}. | Microbacterium liquefaciens (Aureobacterium liquefaciens) |
D6RGH6 | MCIN_HUMAN | MQACGGGAAGRRAFDSICPNRMLALPGRALLCKPGKPERKFAPPRKFFPGCTGGSPVSVYEDPPDAEPTALPALTTIDLQDLADCSSLLGSDAPPGGDLAASQNHSHQTEADFNLQDFRDTVDDLISDSSSMMSPTLASGDFPFSPCDISPFGPCLSPPLDPRALQSPPLRPPDVPPPEQYWKEVADQNQRALGDALVENNQLHVTLTQKQEEIASLKERNVQLKELASRTRHLASVLDKLMITQSRDCGAAAEPFLLKAKAKRSLEELVSAAGQDCAEVDAILREISERCDEALQSRDPKRPRLLPEPANTDTRPGNLHGAFRGLRTDCSRSALNLSHSELEEGGSFSTRIRSHSTIRTLAFPQGNAFTIRTANGGYKFRWVPS | null | null | cell cycle [GO:0007049]; centriole assembly [GO:0098534]; cilium assembly [GO:0060271]; motile cilium assembly [GO:0044458]; multi-ciliated epithelial cell differentiation [GO:1903251]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cilium assembly [GO:1902017]; regulation of DNA-templated DNA replication initiation [GO:0030174]; regulation of mitotic cell cycle [GO:0007346] | nuclear body [GO:0016604]; nucleus [GO:0005634] | identical protein binding [GO:0042802] | PF07412; | 1.20.5.1180; | Geminin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21543332, ECO:0000269|PubMed:25048963}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:21543332}. | null | null | null | null | null | FUNCTION: Transcription regulator specifically required for multiciliate cell differentiation (PubMed:25048963). Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway (PubMed:25048963). Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1 (PubMed:21543332, PubMed:24064211). {ECO:0000250|UniProtKB:Q08B36, ECO:0000269|PubMed:21543332, ECO:0000269|PubMed:24064211, ECO:0000269|PubMed:25048963}. | Homo sapiens (Human) |
D6VTK4 | STE2_YEAST | MSDAAPSLSNLFYDPTYNPGQSTINYTSIYGNGSTITFDELQGLVNSTVTQAIMFGVRCGAAALTLIVMWMTSRSRKTPIFIINQVSLFLIILHSALYFKYLLSNYSSVTYALTGFPQFISRGDVHVYGATNIIQVLLVASIETSLVFQIKVIFTGDNFKRIGLMLTSISFTLGIATVTMYFVSAVKGMIVTYNDVSATQDKYFNASTILLASSINFMSFVLVVKLILAIRSRRFLGLKQFDSFHILLIMSCQSLLVPSIIFILAYSLKPNQGTDVLTTVATLLAVLSLPLSSMWATAANNASKTNTITSDFTTSTDRFYPGTLSSFQTDSINNDAKSSLRSRLYDLYPRRKETTSDKHSERTFVSETADDIEKNQFYQLPTPTSSKNTRIGPFADASYKEGEVEPVDMYTPDTAADEEARKFWTEDNNNL | null | null | cytogamy [GO:0000755]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750] | G protein-coupled receptor homodimeric complex [GO:0038038]; plasma membrane [GO:0005886] | mating-type alpha-factor pheromone receptor activity [GO:0004934]; mating-type factor pheromone receptor activity [GO:0004932]; pheromone binding [GO:0005550] | PF02116; | 1.10.287.920; | G-protein coupled receptor 4 family | PTM: Undergoes hyperphosphorylation of the C-terminal cytoplasmic domain after binding of the alpha-factor, which leads to internalization by endocytosis. {ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:8524302}.; PTM: Monoubiquitination at Lys-337 triggers internalization of STE2. {ECO:0000269|PubMed:9659916}.; PTM: N-glycosylated (PubMed:11583169, PubMed:2839507). N-glycosylation may be involved in the sorting process for misfolded STE2 protein (PubMed:11583169). {ECO:0000269|PubMed:11583169, ECO:0000269|PubMed:2839507}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:14506226, ECO:0000269|PubMed:16313173, ECO:0000269|PubMed:2017168, ECO:0000269|PubMed:28073700, ECO:0000269|PubMed:2839507, ECO:0000269|PubMed:34627767, ECO:0000269|PubMed:35296853, ECO:0000269|PubMed:7935439}; Multi-pass membrane protein {ECO:0000269|PubMed:11112532, ECO:0000269|PubMed:11467956, ECO:0000269|PubMed:11473349, ECO:0000269|PubMed:1653030, ECO:0000269|PubMed:19383463, ECO:0000269|PubMed:2017168, ECO:0000269|PubMed:35296853}. Note=Internalized after binding of alpha-factor (PubMed:8392878). STE2 enters the cell by receptor-mediated endocytosis and is continuously lost and resynthesized in the presence of alpha-factor (PubMed:1330324, PubMed:3015412, PubMed:7935439, PubMed:8392878). {ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:3015412, ECO:0000269|PubMed:7935439, ECO:0000269|PubMed:8392878}. | null | null | null | null | null | FUNCTION: Fungal class D1 G-protein-coupled receptor that acts as an alpha-factor pheromone receptor performing pheromone-dependent signal transduction involved in cellular conjugation, mating projection assembly, and in cell fusion (PubMed:10744981, PubMed:11495900, PubMed:12427030, PubMed:2556384, PubMed:2839507, PubMed:2842059, PubMed:3023832, PubMed:3037311, PubMed:4595644, PubMed:6353246, PubMed:6360378, PubMed:6993497, PubMed:9286665, PubMed:9529386, PubMed:9742115, PubMed:9819407, PubMed:9824658). Following alpha-factor-binding, the signal is transmitted via a tripartite G protein consisting of alpha-, beta- and gamma-subunits (GAP1, STE4 and STE8 respectively) that prepares the cell for conjugation (PubMed:10866688, PubMed:11287148, PubMed:1330324, PubMed:1647971, PubMed:8132618, PubMed:8385135, PubMed:8692892). In the inactive state, the cytoplasmic end of transmembrane domain 7 (TMD7) is unstructured and packs between TMD1-6, blocking the G protein coupling site (PubMed:35296853). Agonist binding results in the outward movement of the extracellular ends of TMD6 and TMD7 by 6 Angstroms (PubMed:35296853). On the intracellular surface, the G protein coupling site is formed by a 20 Angstroms outward movement of the unstructured region in TMD7 that unblocks the site, and a 12 Angstroms inward movement of TMD6 (PubMed:35296853). {ECO:0000269|PubMed:10744981, ECO:0000269|PubMed:10866688, ECO:0000269|PubMed:11287148, ECO:0000269|PubMed:11495900, ECO:0000269|PubMed:12427030, ECO:0000269|PubMed:1330324, ECO:0000269|PubMed:1647971, ECO:0000269|PubMed:2556384, ECO:0000269|PubMed:2839507, ECO:0000269|PubMed:2842059, ECO:0000269|PubMed:3023832, ECO:0000269|PubMed:3037311, ECO:0000269|PubMed:35296853, ECO:0000269|PubMed:4595644, ECO:0000269|PubMed:6353246, ECO:0000269|PubMed:6360378, ECO:0000269|PubMed:6993497, ECO:0000269|PubMed:8132618, ECO:0000269|PubMed:8385135, ECO:0000269|PubMed:8692892, ECO:0000269|PubMed:9286665, ECO:0000269|PubMed:9529386, ECO:0000269|PubMed:9742115, ECO:0000269|PubMed:9819407, ECO:0000269|PubMed:9824658}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
D6WMX4 | PINK1_TRICA | MSVRAVGSRLFKHGRSLIQQFCKRDLNTTIGDKINAVSQATAAPSSLPKTQIPKNFALRNVGVQLGLQARRILIDNVLNRVTNSLSAELRKKATRRILFGDSAPFFALVGVSIASGTGILTKEEELEGVCWEIREAISKIKWQYYDIDESRFESNPITLNDLSLGKPIAKGTNGVVYSAKVKDDETDDNKYPFALKMMFNYDIQSNSMEILKAMYRETVPARMYYSNHDLNNWEIELANRRKHLPPHPNIVAIFSVFTDLIQELEGSKDLYPAALPPRLHPEGEGRNMSLFLLMKRYDCNLQSFLSTAPSTRTSLLLLAQLLEGVAHMTAHGIAHRDLKSDNLLLDTSEPESPILVISDFGCCLADKTNGLSLPYTSYEMDKGGNTALMAPEIICQKPGTFSVLNYSKADLWAVGAIAYEIFNCHNPFYGPSRLKNFNYKEGDLPKLPDEVPTVIQALVANLLKRNPNKRLDPEVAANVCQLFLWAPSTWLKPGLKVPTSGEILQWLLSLTTKVLCEGKINNKSFGEKFTRNWRRTYPEYLLISSFLCRAKLANVRNALHWIQENLPELD | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:29991771}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:29991771}; | autophagy [GO:0006914]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of free ubiquitin chain polymerization [GO:1904544]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein ubiquitination [GO:0031398]; protein autophosphorylation [GO:0046777]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (TcasGA2_TC013516). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM). {ECO:0000250|UniProtKB:Q0KHV6}.; PTM: Autophosphorylated on Ser-205, which activates kinase activity and is required for substrate recognition (PubMed:22645651, PubMed:26784449, PubMed:28980524, PubMed:29475881, PubMed:29991771). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation at Ser-205 (By similarity). Autophosphorylation is sufficient and essential for selective recruitment of park to depolarized mitochondria, likely via Pink1-dependent phosphorylation of polyubiquitin chains (PubMed:24751536). Also autophosphorylated at Ser-377, Thr-386 and possibly Thr-530 (PubMed:29991771). Another report found evidence of autophosphorylation at Ser-154, Thr-186, Thr-218, Ser-267 and Thr-530, as well as a number of other minor sites, but determined that phosphorylation at these sites is not required for enzyme activity and may not occur in vivo (PubMed:29475881). {ECO:0000250|UniProtKB:Q0KHV6, ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q0KHV6}. Note=Localizes mostly in mitochondrion, and the smaller proteolytic processed fragment localizes in the cytosol as well (By similarity). When mitochondria are damaged, defective and/or enriched with deleterious mtDNA mutations, Pink1 import is arrested which induces its accumulation on the outer mitochondrial membrane where it acquires kinase activity (By similarity). {ECO:0000250|UniProtKB:Q0KHV6}. | 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:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771, ECO:0000269|PubMed:32484300}; 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:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771, ECO:0000269|PubMed:32484300}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=287.5 uM for Drp1 (at 30 degrees Celsius) {ECO:0000269|PubMed:32484300}; KM=84.4 uM for ubiquitin (at 30 degrees Celsius) {ECO:0000269|PubMed:32484300}; KM=391 uM for ubiquitin (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29475881}; KM=36 uM for ubiquitinated rat Prkn (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29475881}; Note=kcat is 4.6 sec(-1) for phosphorylation of Drp1 (at pH 7.5 and 30 degrees Celsius) (PubMed:32484300). kcat is 20.9 sec(-1) for phosphorylation of ubiquitin (at pH 7.5 and 30 degrees Celsius) (PubMed:32484300). kcat is 18 min(-1) for phosphorylation of ubiquitin (at pH 7.5 and 30 degrees Celsius) (PubMed:29475881). kcat is 7.8 min(-1) for phosphorylation of ubiquitinated rat Prkn (at pH 7.5 and 30 degrees Celsius) (PubMed:29475881). {ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:32484300}; | null | null | null | FUNCTION: Acts as a serine/threonine-protein kinase (PubMed:24751536, PubMed:25474007, PubMed:26116755, PubMed:26784449, PubMed:28980524, PubMed:29475881, PubMed:29991771, PubMed:32484300). Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine (PubMed:22645651). Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 (PubMed:22645651). Critical to mitochondrial homeostasis it mediates several pathways that maintain mitochondrial health and function (By similarity). Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as park and likely Drp1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:24751536, PubMed:25474007, PubMed:26116755, PubMed:28980524, PubMed:29991771, PubMed:32484300). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (By similarity). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (By similarity). Mediates the translocation and activation of park at the outer membrane (OMM) of dysfunctional/depolarized mitochondria (PubMed:25474007, PubMed:26116755). At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains, the Pink1-phosphorylated polyubiquitin then recruits park from the cytosol to the OMM where park is fully activated by phosphorylation at 'Ser-80' by Pink1 (PubMed:24751536, PubMed:25474007, PubMed:26116755, PubMed:29475881, PubMed:29991771). When cellular stress results in irreversible mitochondrial damage, functions with park to promote the clearance of dysfunctional and/or depolarized mitochondria by selective autophagy (mitophagy) (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria, by phosphorylating and thus promoting the park-dependent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo (By similarity). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Also likely to promote mitochondrial fission independently of park and Atg7-mediated mitophagy, via the phosphorylation and activation of Drp1 (PubMed:32484300). Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (By similarity). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (By similarity). Involved in mitochondrial biogenesis by promoting the park-dependent ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Functions with park to promote localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (By similarity). During oogenesis, phosphorylates and inactivates larp on the membrane of defective mitochondria, thus impairing local translation and mtDNA replication and consequently, reducing transmission of deleterious mtDNA mutations to the mature oocyte (By similarity). Phosphorylates the mitochondrial acyl-CoA dehydrogenase Mcad, and appears to be important for maintaining fatty acid and amino acid metabolism via a mechanism that is independent of it's role in maintaining production of ATP (By similarity). {ECO:0000250|UniProtKB:Q0KHV6, ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771, ECO:0000269|PubMed:32484300}. | Tribolium castaneum (Red flour beetle) |
D6XZ22 | GGP_BACIE | MHEIGEHLTTNTGWDIIKNRYEAAQAITEGSNFMIGNGFMGYRGTFAEDGKDAYAACIVTDTWDKADGKWEELSTVPNALLTLLHVDGEPFIMSEEAASFERTLDLSQGVTSRKVSQRMKNGATITIHEEKFASYRKKHAVLMKYTVESDQDTDAVLDTGIDYDVWSINGDHLQGHHYFSHPTGDGVTAKTVSYEDTVTVVETCSLDADASEEDYQNPDGSGRTFSLSLEAGKPVTLEKAMIIYSSNDVDNPQDEALLEAKHMQSYEEEKAANRLEWDNLWSHYDVTIQNNIIDQVALRFNIYHAIIATPVHKSLPIGARGLSCQAYQGAAFWDQEIYNMPMYLYSNPEIARNILKYRHRTLDGARRKAKRLGYEGAYYAWISGKTGDELCPDFFFKDVLSGRDIRNHFNDWQIHISPDIAYAVKKYHQVTGDDAFIRDYGAEMIFEIARFLASHAVYKPMRGRYEFMRVQGPDEYHENVDNNAFTNHQAMFTLQAADELLQTLDEKTLSAVKEKIGLSDDEISLWRDMLANTYVPKPDKHGIIEQFDGYYDLETIIPAKKVTERLIKEDEYYGYPNGVTVRTQCIKQADVIQLFVLHPHLYDRKTVELNYEFYEPRTLHFSSLSPSSYAIVAAQIDKVEEAYRNFRKSVMIDLLNTNEAVSGGTFIGGIHTAANGASWQMVVNGFGGLSVHGDDIHLSPRLPDAWDGYTFKAIVKGQTLEVDVTKEQITITNKSEDRKPLTLHIFGEKSVLDSERITKSR | 2.4.1.332 | null | trehalose catabolic process [GO:0005993] | cytosol [GO:0005829] | alpha,alpha-trehalase activity [GO:0004555]; carbohydrate binding [GO:0030246]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; protein-glucosylgalactosylhydroxylysine glucosidase activity [GO:0047402] | PF03633;PF03632;PF03636; | 1.50.10.10;2.70.98.40;2.60.420.10; | Glycosyl hydrolase 65 family | null | null | CATALYTIC ACTIVITY: Reaction=2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = beta-D-glucose 1-phosphate + glycerol; Xref=Rhea:RHEA:43060, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57684, ChEBI:CHEBI:82766; EC=2.4.1.332; Evidence={ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for 2-O-alpha-D-glucopyranosyl-sn-glycerol {ECO:0000269|PubMed:24466148}; KM=0.57 mM for phosphate {ECO:0000269|PubMed:24466148}; Note=kcat is 95 sec(-1) with 2-O-alpha-D-glucopyranosyl-sn-glycerol. {ECO:0000269|PubMed:24466148}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:24466148}; | null | FUNCTION: Catalyzes both the (1) reversible phosphorolysis of 2-O-alpha-D-glucopyranosyl-sn-glycerol (GG) from beta-D-glucose 1-phosphate (betaGlc1P) and glycerol and (2) the hydrolysis of betaGlc1P. the betaGlc1P hydrolysis is a glucosyl-transfer reaction to an acceptor water molecule that produces an anomer-inverted alpha-glucose, not a phosphatase-type reaction. In the absence of glycerol produces alpha-D-glucopyranose and phosphate from beta-D-glucopyranose 1-phosphate. {ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502}. | Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) |
D7A5Q8 | YDDG_ANCN5 | MSRSSATLIGFTAILLWSTLALATSSTGAVPPFLLTALTFTIGGAVGIAAGLARGVGLSVLRQPWPVWVHGIGGLFGYHFFYFSALKLAPPAEAGLVAYLWPLLIVLFSAFLPGERLRPAHVAGALMGLAGTVVLLGARAGGFGFAPEYVPGYLAAAACAVIWSVYSVASRRFARVPTEVVAGFCLATAALSALCHILFEPSVWPVGSEWLAVVALGIGPVGIAFYTWDIGMKRGDVRLLGVLSYAAPVLSTLLLVVAGFAAPSGALAIACALIVGGAAVATLLARR | null | null | amino acid transport [GO:0006865] | plasma membrane [GO:0005886] | null | PF00892; | null | Drug/metabolite transporter (DMT) superfamily, Aromatic amino acid/paraquat exporter (ArAA/P-E) (TC 2.A.7.17) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:27281193}; Multi-pass membrane protein {ECO:0000269|PubMed:27281193}. | CATALYTIC ACTIVITY: Reaction=L-threonine(in) = L-threonine(out); Xref=Rhea:RHEA:35019, ChEBI:CHEBI:57926; Evidence={ECO:0000305|PubMed:27281193}; CATALYTIC ACTIVITY: Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939, ChEBI:CHEBI:57844; Evidence={ECO:0000305|PubMed:27281193}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000305|PubMed:27281193}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000305|PubMed:27281193}; | null | null | null | null | FUNCTION: Amino acid transporter with broad substrate specificity (PubMed:27281193). Can transport various amino acids, including L-threonine, L-methionine, L-lysine and L-glutamate (PubMed:27281193). {ECO:0000269|PubMed:27281193}. | Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456) (Starkeya novella) |
D7A6E5 | SOXA_ANCN5 | MRRFAAGCLALALLVLPFVLTGARAAEDESEKEIERYRQMIEDPMANPGFLNVDRGEVLWSEPRGTRNVSLETCDLGEGPGKLEGAYAHLPRYFADTGKVMDLEQRLLWCMETIQGRDTKPLVAKPFSGPGRTSDMEDLVAFIANKSDGVKIKVALATPQEKEMYAIGEALFFRRSSINDFSCSTCHGAAGKRIRLQALPQLDVPGKDAQLTMATWPTYRVSQSALRTMQHRMWDCYRQMRMPAPDYASEAVTALTLYLTKQAEGGELKVPSIKR | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Note=Contains a mononuclear Cu(II) center. {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | copper ion binding [GO:0005507]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; protein heterodimerization activity [GO:0046982]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792] | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-236. {ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:21592966}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689, Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963, ChEBI:CHEBI:140664; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.49 mM for glutathione (at pH 6.0) {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; KM=0.19 mM for glutathione (at pH 7.0) {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Vmax=0.124 uM/min/mg enzyme (copper-free) at pH 6.2 {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Vmax=1.54 uM/min/mg enzyme (copper-loaded) at pH 6.2 {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; Note=kcat is 8.72 sec(-1) and 5.7 sec(-1) for glutathione at pH 6.0 and pH 7.0, respectively. {ECO:0000269|PubMed:18552405}; | null | null | null | FUNCTION: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation. {ECO:0000269|PubMed:14645228, ECO:0000269|PubMed:15848194, ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}. | Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456) (Starkeya novella) |
D7EZN2 | LIPR2_PIG | MLPSWTIGLLLLATVRGKEICYQPFGCFSDETPWARTCHWPFKLFPWAPKDIDTHFLLYTNENPNNFQLINITNLDTIEASNFQLDRKTRFIIHGFIDKGEDSWPSEMCKKMFKVEKVNCICVDWRRGALTRYTQAVHNTRVVGAEIAFLIQGLSTKFDYNPENVHLIGHSLGAHTAAEAGRRLGGHVGRLTGLDPAQPCFQNTPEEVRLDPSDAMFVDVIHTDSAPFIPFLGFGMSQKVGHLDFYPNGGKEMPGCQKNTLSTIVDVDGIWEGIEDFAACNHLRSYKYYSSSIFSPDGFLGYPCASYDEFQEEENKCFPCPAEGCPKMGHYADQFQGKTSAVGQTFFLNTGDSGNFTRWRYRVSVTLAGKRNVHGYIRIALYGSNANSKQYNIFKGSLQPNARYTHDIDVDLNVGKVQKVKFLWYNHIIDLFHPELGASQVMVQSGEDKTEHKFCGSDTVRENILQTLNPC | 3.1.1.26; 3.1.1.3 | null | phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; triglyceride catabolic process [GO:0019433] | extracellular space [GO:0005615]; neuron projection [GO:0043005]; zymogen granule membrane [GO:0042589] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; galactolipase activity [GO:0047714]; metal ion binding [GO:0046872]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:23770034}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+); Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:23770034}; CATALYTIC ACTIVITY: Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956; Evidence={ECO:0000250|UniProtKB:P54317}; 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:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+) + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153, ChEBI:CHEBI:88155; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000305|PubMed:23770034}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) + octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865; Evidence={ECO:0000305|PubMed:23770034}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol + H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol; Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+); Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+); Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396, ChEBI:CHEBI:28868, ChEBI:CHEBI:90310; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359; Evidence={ECO:0000250|UniProtKB:P54317}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + a monoacyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465; Evidence={ECO:0000269|PubMed:23770034}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665; Evidence={ECO:0000305|PubMed:23770034}; | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000269|PubMed:23770034}.; PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:23770034}. | null | null | FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:23770034). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:23770034). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:23770034). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency (By similarity). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:23770034). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54317, ECO:0000250|UniProtKB:P54318, ECO:0000269|PubMed:23770034}. | Sus scrofa (Pig) |
D7PC76 | S26A5_TURTR | MDHVEETEILAATQRYYVERPIFSHPVLQERLHKKDKISESIGDKLKQAFTCTPKKIRNIIYMFLPITKWLPAYRFKEYVLGDIVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNSTEARDALRVKVAMSVTLLTGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFSLHESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGLCNSTGSLFQTFAISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALMTVIYRTQSPSYIVLGQLPDTDVYIDIDAYEEVKEVPGIKIFQINAPIYYANSDLYSSALKRKTGVNPAFILGARRKAMKKYAKEVGNANMANATVVKVDAEVDAEDGTKPEEEEDEIKYPPIVTKSTLPEELQRFMPPGDNVHTIILDFTQVNFMDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVSDLTQNQFFENPALLDLLFHSIHDAVLGSQVREALAEQEATAAPPQEDSEPNATPEA | null | null | cochlear outer hair cell electromotile response [GO:0099129]; regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605] | plasma membrane [GO:0005886] | bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmembrane transporter activity [GO:0008271] | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34695838}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9EPH0}; | null | null | null | null | FUNCTION: Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ (PubMed:34695838). Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane (PubMed:34695838). The nature of the voltage sensor is not completely clear, and two models compete (By similarity). In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (By similarity). However, the effective voltage sensor may be the result of a hybrid voltage sensor assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion) (PubMed:34695838). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization (PubMed:34695838). The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (By similarity). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state (PubMed:34695838). In addition, can act as a weak Cl(-)/HCO3 (-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). Moreover, supports a role in cardiac mechanical amplification serving as an elastic element to enhance the actomyosin- based sarcomere contraction system (By similarity). {ECO:0000250|UniProtKB:P58743, ECO:0000250|UniProtKB:Q99NH7, ECO:0000250|UniProtKB:Q9EPH0, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34695838}. | Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) |
D7PDD4 | G6B_MOUSE | MALVLPLLPLLLSKVQGNPEVSLEGSPGDRVNLSCIGVSDPTRWAWAPSFPACKGLSKGRRPILWASTRGTPTVLQHFSGRLRSLDNGIKRLELLLSAGDSGTFFCKGRHENESRTVLQVLGDKAGCRPAGSTHGYEYPKVLIPLLGVGLVLGLGVAGVVWRRRRLSPPPPPPPPPGPLPTFAPVINAEPQRPLEQESKISGHLDQEPSLHYADLDHSVLGRHRRMSTVVSGDASTVYAVVV | null | null | blood coagulation [GO:0007596]; erythrocyte differentiation [GO:0030218]; integrin-mediated signaling pathway [GO:0007229]; megakaryocyte development [GO:0035855]; megakaryocyte differentiation [GO:0030219]; negative regulation of signal transduction [GO:0009968]; platelet formation [GO:0030220] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | null | PF15096; | null | null | PTM: N-glycosylated. {ECO:0000269|PubMed:23112346}.; PTM: May be O-glycosylated. {ECO:0000250|UniProtKB:O95866}.; PTM: Phosphorylated. {ECO:0000269|PubMed:23112346}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23112346}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O95866, ECO:0000255}. | null | null | null | null | null | FUNCTION: Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production (PubMed:23112346). Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (By similarity). This regulation of megakaryocate function as well as platelet production ann activation is done through the inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling (PubMed:23112346). Appears to operate in a calcium-independent manner (By similarity). {ECO:0000250|UniProtKB:O95866, ECO:0000269|PubMed:23112346}. | Mus musculus (Mouse) |
D7PF45 | SHIP2_PIG | MASACGAPGPGAGPGAALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVERERELDPPDERDASDGEDEKPPLPPRSGTSVSAPLGPSSPPAAPEPPTPAVESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLAASCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQNPPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPVQPSTRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKERTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDEPDMISVFIGTWNMGSVPPPRNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLGAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSHPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTADQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNVNFLKVQWSSRQLPTLKPILDIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKSKAPSVSRGSQEPRSGSRKPAPAEASCPLSKLFEEPEKPPPTGRPPAPPRAAPREEPLTPRLKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPPATKNKVAITVPAPQLGRHRPPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSREPLPGPGVRGRSGGEARALPPPKAHPRPPLPPGPLPPGTFLGEAAGGDDRSCSVLQVAKKLSEVDSAPPGPGRCLLLPGPLELQPARALPSDYGRPLSFPPPRIRESVQEDLAEEAPCPQAGRTGGLGEAGMGAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK | 3.1.3.86 | null | establishment of mitotic spindle orientation [GO:0000132]; immune system process [GO:0002376]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of actin filament organization [GO:0110053]; regulation of immune response [GO:0050776]; regulation of protein localization [GO:0032880] | basal plasma membrane [GO:0009925]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922] | inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; SH3 domain binding [GO:0017124] | PF00536;PF00017; | 3.60.10.10;3.30.505.10;1.10.150.50; | Inositol 1,4,5-trisphosphate 5-phosphatase family | PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-988 following cell attachment and spreading. Phosphorylated at Tyr-1164 following EGF signaling pathway stimulation. {ECO:0000250|UniProtKB:O15357}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15357}. Cytoplasm, cytoskeleton. Membrane {ECO:0000250|UniProtKB:O15357}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Basal cell membrane {ECO:0000250|UniProtKB:F1PNY0}. Nucleus {ECO:0000269|PubMed:12847108}. Nucleus speckle {ECO:0000269|PubMed:12847108}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:F1PNY0}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring. {ECO:0000250|UniProtKB:O15357}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000269|PubMed:12847108}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529; Evidence={ECO:0000305|PubMed:12847108}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43548, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83417; Evidence={ECO:0000250|UniProtKB:O15357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43549; Evidence={ECO:0000250|UniProtKB:O15357}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43556, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83422; Evidence={ECO:0000250|UniProtKB:O15357}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43557; Evidence={ECO:0000250|UniProtKB:O15357}; | null | null | null | null | FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:12847108). Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (By similarity). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (By similarity). Part of a signaling pathway that regulates actin cytoskeleton remodeling (By similarity). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (By similarity). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading (By similarity). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (By similarity). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (By similarity). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (By similarity). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (By similarity). Involved in EGF signaling pathway (By similarity). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (By similarity). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (By similarity). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity). {ECO:0000250|UniProtKB:F1PNY0, ECO:0000250|UniProtKB:O15357, ECO:0000250|UniProtKB:Q6P549, ECO:0000250|UniProtKB:Q9WVR3, ECO:0000269|PubMed:12847108}. | Sus scrofa (Pig) |
D7RF80 | POLG_KFDV | MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRKTVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCDDSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEGWVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKPSVDVWLDDIHQENPAKTREYCLHAKLANSKVAARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKFSCEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVVLELDKTAEHLPKAWQVHRDWFEDLSLPWRHGGAQEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGSKYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLITPNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGMLSSVGKALHTAFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWREVTDWYDGYAFHPESPSVLAASLKEAYEEGICGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDKRDPSDYRGGKVGTLRRSGKEMKTSWKGWSQSFVWSVPEAPRRFMVGVEGAGECPLDKRRTGVFTVAEFGMGMRTKVFLDLRETASSDCDTGVMGAAVKSGHAVHTDQSLWMRSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPAGLAGPRSHYNHIPGYAEQVKGPWSQTPLRVVREPCPGTAVKIDQSCDKRGASLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQGGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGSSVVWCGMVVLGLVVTGLVTIEGLCRYVVAVGILMSMELGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVATYFLLLVLELGFPEASLSNIWKWADSLAMGALILQACGQEGRTRVGYLLAAMMTQKDMVIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLAGLLGGEGVGLRLLAFRKLAERRNRRSFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLTAEWCGEVEWNPDLVNEGGEVNLKVRQDAMGNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAVWTLFEMLGSGRRSELVFSGQETRTERNRPFEIKDGAYRIYSPGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVDEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQETHQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPEIPLSVQGTGWMSKGQITVLDMHPGSGKTHRVLPELVRQCADRGMRTLVLAPTRVVLKEMERALAGKKVRFHSPAVEGQTTAGAIVDVMCHATYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGEWREGFDWITEYEGRTAWFVPSISKGGAVARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVIDGRTNIKPEEVDGKVELTGTRKVTTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVATFYGPEQVKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEENAIDGADGDLVRFKTPGGSERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAPEAFLTIVEVAVLGVATLGILWCFVARASVSRMFLGTVVLFAALFLLWIGGVDYGHMAGIALIFYTLLTVLQPEPGKQRSSDDNRLAYFLLGLFSLAGLVTANEMGMLDKTKADLAGLVWRGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQLQTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPMSLGLGVALAAFHLAIVASGLEAELTQRAHRVFFSAMVKNPMVDGDVINPFPDGETKPALYERRMSLILAIALCMGSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTMPMACGMAGLVRGSFWGLLPMGHRLWLRTTGTRRGGAEGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDKARELLKRGETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFRTGMDVYSLEAHRADTILCDIGESSPDPLAEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGLVRVPFSRNSTHEMYFSTAISGNIINSVNTQSRKLLARFGDQRGPTKVPEVDLGTGTRCVVLAEDKVREADVAERIAALKTQYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQVGTKIIMRAVNDWIFERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWPNAREAVEDPEFWRLVDEERERHLGGRCAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGTSLNYLGWHLKKLSELEGGLFYADDTAGWDTRITNADLEDEEQILRYLEGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVVTYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEHGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAKVRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMGDKGKVREWRDIPYLPKSQDGLCSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}. | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}. | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; 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; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}. | Kyasanur forest disease virus (KFDV) |
D7SFH9 | LRL26_ARATH | MNSQQSTRTKQMLQQSSTHLLCGVVLLQLFAAQVDAQRSTSPWQTLSGDAPLVIARGGFSGLFPDSSLAAYQFAMVVSVADVVLWCDVQLTKDGHGICFPDLNLANASNSEEVYPNRQKSYPVNGVTTKGWFPIDFSLTELQKVLFSLIRGILSRSGKFDENGYSISTVQNVATQMKPALFWLNVQHDEFYEQHNLSMSSFLLSTSRTVSIDFISSPEVNFFRKIAGGFGNNGPSFVFQFMGKEDFEPTTNRTYGSILSNLSFVKTFASGILVPKSYILPLDDKQYLLPHTSLVQDAHKAGLKLYASGFANDVDIAYNYSWDPVSEYLSFVDNGNFSVDGMLSDFPLTASASVDCFSHIGRNATKQVDFLVISKNGASGEYPGCTKLAYEKAIKDGSDVIDCPVQMSSDGIPFCSSSIDLVNSTTVGQTHLRNRSIIVPEISSVAGIFTFSLTWHEIQSLTPAISNPFRENGMSRNPNERNSGNLISLYEFLNLAKNSTSLSGILISLENVVYLREKKGLDVVKVVLNRLTETGYIVGTLKVMIQSTTRLVLVDFKNQSTYKTVYKIKETIGNITDSAIEDIKKFANAVVINKASVFPNSDSFLTGQTTNVLERLQKFQLPVYVELFQNEFVSQPFDFFADETVEINAYIFGAGINGTITEFPYTAARYKRNRCLGREEVPPYMLPVNPGGVLTLISTSSLPPAQDPNPIFTHDDVTEPPLPPVIAKSPTSTLGTPSTIAKPLRNFLKVIRIVSWSVAGVVLFLVLLTLVFCFHRKRETRLRQQKLKALIPLEHYTYAQVKRITKSFAEVVGRGGFGIVYKGTLSDGRVVAVKVLKDTKGNGEDFINEVATMSRTSHLNIVSLLGFCSEGSKRAIIYEFLENGSLDKFILGKTSVNMDWTALYRIALGVAHGLEYLHHSCKTRIVHFDIKPQNVLLDDSFCPKVSDFGLAKLCEKKESILSMLDTRGTIGYIAPEMISRVYGNVSHKSDVYSYGMLVLEIIGARNKEKANQACASNTSSMYFPEWVYRDLESCKSGRHIEDGINSEEDELAKKMTLVGLWCIQPSPVDRPAMNRVVEMMEGSLEALEVPPRPVLQQIPISNLHESSILSEDVSVYTEG | 2.7.11.1; 3.1.4.46 | null | cellular defense response [GO:0006968]; defense response [GO:0006952]; glycerol metabolic process [GO:0006071]; innate immune response [GO:0045087]; lipid metabolic process [GO:0006629]; phosphorylation [GO:0016310] | mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; glycerophosphodiester phosphodiesterase activity [GO:0008889]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03009;PF07714; | 3.20.20.190;1.10.510.10; | Glycerophosphoryl diester phosphodiesterase family; Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20508139}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597, ChEBI:CHEBI:83408; EC=3.1.4.46; Evidence={ECO:0000250|UniProtKB:Q7Y208}; 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; 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; | null | null | null | null | FUNCTION: Atypical receptor-like kinase involved in disease resistance. {ECO:0000269|PubMed:20508139}. | Arabidopsis thaliana (Mouse-ear cress) |
D7SSD8 | MJE1_VITVI | MEKRERHFVLVHGACHGAWCWYKVTTFLRSAGHKVTALDLAAAGANGKRLDELNSISDYHEPLMKFMTSLVAGEKVILVAHSLGGVSVSVAMERFPQKISVAVFVSAYMPGPDFNLSTVYQELHQRRQGASKDTQYTFDRGSNNPPTSIIFSPEDLAAKLYQLSPPEDLTLATTLMRPTKLFRGENLLKETTVTREKYGTVRRVYIVCDKDNILKEDFQRWMIKNNPSDEVKVIMGSDHMPMFSKPLDLCAYLQEIVESYS | 3.1.1.- | null | jasmonic acid metabolic process [GO:0009694]; oxylipin biosynthetic process [GO:0031408]; response to cold [GO:0009409]; response to UV-B [GO:0010224]; salicylic acid metabolic process [GO:0009696] | null | methyl indole-3-acetate esterase activity [GO:0080030]; methyl jasmonate esterase activity [GO:0080032]; methyl salicylate esterase activity [GO:0080031] | PF12697; | 3.40.50.1820; | AB hydrolase superfamily, Methylesterase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol; Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431; Evidence={ECO:0000269|PubMed:26934101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373; Evidence={ECO:0000269|PubMed:26934101}; CATALYTIC ACTIVITY: Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate; Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832; Evidence={ECO:0000269|PubMed:26934101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612; Evidence={ECO:0000269|PubMed:26934101}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.9 uM for methyl jasmonate {ECO:0000269|PubMed:26934101}; | PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:26934101}.; PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:26934101}. | null | null | FUNCTION: Methylesterase that catalyzes the hydrolysis of methyl jasmonate (MeJA) into jasmonate (JA) (PubMed:26934101). Can also use methyl salicylate (MeSA) as substrate with a lower efficiency (PubMed:26934101). {ECO:0000269|PubMed:26934101}. | Vitis vinifera (Grape) |
D7UNT2 | LCDH_RHISP | MSFITKAACVGGGVIGGAWVARFALAGIDVKIFDPHPEAERIIGEVMANAERAYAMLTMAPLPPKGKLTFCKSIEEAVEGADWIQESVPERLELKRGVITKIDAAARPDALIGSSTSGLLPSDLQSEMHHPERMFVAHPYNPVYLLPLVELVGGKKTSKATIERAMQGVEQIGMKGVVIAKEIEAFVGDRLLEALWREALWLIQDDICHTETLDNVMRYSFGMRWAQMGLFETYRIAGGEAGMRHFLAQFGPCLKWPWTKFTDVVDLDDALVEKIGAQSDAQAAGRSIRELERIRDENLVGIMHALKSGNGGEGWGAGKLLADFEAKLWANARKPEADLGDVKPLRILDTKVSAAWVDYNGHMTEHRYLQVFGDTSDGVLRLIGVDLDYVRDGHSYYTVETHIRNLGDEASGEALYSTCQILSSDEKRLHIFSTIYNAATNEAVATAEQMMLHVDSKAGKAVAAPEAVLSKLRAITEAHAQLQTPDGAGRFVGQKRA | 1.1.1.108 | null | carnitine catabolic process [GO:0042413]; fatty acid metabolic process [GO:0006631] | cytoplasm [GO:0005737] | carnitine 3-dehydrogenase activity [GO:0047728]; L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF13279; | 3.10.129.10;3.40.50.720; | 3-hydroxyacyl-CoA dehydrogenase family, L-carnitine dehydrogenase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}. | CATALYTIC ACTIVITY: Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH; Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126, ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945; EC=1.1.1.108; Evidence={ECO:0000269|PubMed:20530902}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for L-carnithine {ECO:0000269|PubMed:20530902}; KM=0.087 mM for NAD(+) {ECO:0000269|PubMed:20530902}; KM=1.2 mM for 3-dehydrocarnitine {ECO:0000269|PubMed:20530902}; Vmax=18.9 umol/min/mg enzyme {ECO:0000269|PubMed:20530902}; | PATHWAY: Amine and polyamine metabolism; carnitine metabolism. | null | null | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation pathway that allows Rhizobium sp. YS-240 to grow on L-carnitine as the sole source of carbon and nitrogen. {ECO:0000269|PubMed:20530902}. | Rhizobium sp |
D7UPN3 | RLK10_ORYSJ | MFSLPALLIGACAFAAAAVAASGDGCRAGCSLAIAAYYFSEGSNLTFIATIFAIGGGGYQALLPYNPAITNPDYVVTGDRVLVPFPCSCLGLPAAPASTFLAGAIPYPLPLPRGGGDTYDAVAANYADLTTAAWLEATNAYPPGRIPGGDGRVNVTINCSCGDERVSPRYGLFLTYPLWDGETLESVAAQYGFSSPAEMELIRRYNPGMGGVSGKGIVFIPVKDPNGSYHPLKSGGMGNSLSGGAIAGIVIACIAIFIVAIWLIIMFYRWQKFRKATSRPSPEETSHLDDASQAEGIKVERSIEFSYEEIFNATQGFSMEHKIGQGGFGSVYYAELRGEKTAIKKMGMQATQEFLAELKVLTHVHHLNLVRLIGYCVENCLFLVYEFIDNGNLSQHLQRTGYAPLSWATRVQIALDSARGLEYLHEHVVPVYVHRDIKSANILLDKDFRAKIADFGLAKLTEVGSMSQSLSTRVAGTFGYMPPEARYGEVSPKVDVYAFGVVLYELLSAKQAIVRSSESVSESKGLVFLFEEALSAPNPTEALDELIDPSLQGDYPVDSALKIASLAKSCTHEEPGMRPTMRSVVVALMALTANTDLRDMDYHPF | 2.7.11.1 | null | innate immune response [GO:0045087]; phosphorylation [GO:0016310]; response to chitin [GO:0010200] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {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=2.7.11.1; 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; | null | null | null | null | null | Oryza sativa subsp. japonica (Rice) |
D7UQM5 | AURK_PATPE | MTPTGPSHHSMAPKRVLPAASQSNMYGNIRSASTTSTTASTSSQALRLLQNAKTSKNADNRIAHAERQGPPSAHPAAMQKPAARVAPSNENRPDPAARQHQHQQQLQQQKATGHDRVLKESQAGNSTTTTMTSTQSKEANKWSLANFDIGRPLGKGKFGNVYLAREKKSKFIVALKVLFKSQLQKAKVEHQLRREIEIQSHLRHDHILRLYGYFYDDTRVYLILEYAARGELYKEMQAQKAGHFDEDRSAVYIYQLAKALLYCHEKKVIHRDIKPENLLLDLKGDLKIADFGWSVHAPSSRRATLCGTLDYLPPEMIEGKTHDEKVDLWSLGVLCYEFLVGKPPFESQGNTETYRKITKVEFTFPKHVSEGARDLICKLLKHNPSHRLSLEGVIAHAWIQEKISQRS | 2.7.11.1 | null | cell division [GO:0051301]; meiotic cell cycle [GO:0051321]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; regulation of cytokinesis [GO:0032465] | centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21048162}. Midbody {ECO:0000269|PubMed:21048162}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21048162}. Nucleus {ECO:0000269|PubMed:21048162}. Chromosome {ECO:0000269|PubMed:21048162}. Chromosome, centromere {ECO:0000269|PubMed:21048162}. Note=Localized to cytoplasm in immature oocytes. After 1-methyladenine-induced oocyte maturation during meiosis I, becomes localized initially to the chromosomes, then to both chromosomes and the meiotic spindle, and subsequently relocates from the chromosomes to the midzone at anaphase onset. {ECO:0000269|PubMed:21048162}. | 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:O14965}; 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:O14965}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase that contributes to the regulation of cell cycle progression. Involved in meiotic apparatus formation and polar body extrusion. Contributes to Plk1 activation and phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required for accurate progression of early embryonic M phase. Involved in chromosome alignment and cleavage furrow formation during early embryonic cycles. May be involved in mitotic spindle formation and cytokinesis. {ECO:0000269|PubMed:21048162}. | Patiria pectinifera (Starfish) (Asterina pectinifera) |
D7URM0 | LCDH_PSESP | MPFITHIKTFAALGSGVIGSGWVARALAHGLDVIAWDPAPGAEQALRQRVANAWPALEKQGLAAGAAQHRLSFVSSIEECVRDADFIQESAPERLDLKLDLHAKISAAAKPDAIIASSTSGLLPSEFYESSSHPERCVVGHPFNPVYLLPLVEIVGGRHTAPEAIEAAKGIYTELGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALKLPWTYLPAPELTERLIDEVVDGTAAQVGERSIAELERYRDDTLLAVLEAIGTSKAKHGMTFSE | 1.1.1.108 | null | carnitine catabolic process [GO:0042413]; fatty acid metabolic process [GO:0006631] | cytoplasm [GO:0005737] | carnitine 3-dehydrogenase activity [GO:0047728]; L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403] | PF00725;PF02737; | 3.40.50.720; | 3-hydroxyacyl-CoA dehydrogenase family, L-carnitine dehydrogenase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530902}. | CATALYTIC ACTIVITY: Reaction=carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH; Xref=Rhea:RHEA:19265, ChEBI:CHEBI:15378, ChEBI:CHEBI:17126, ChEBI:CHEBI:57540, ChEBI:CHEBI:57885, ChEBI:CHEBI:57945; EC=1.1.1.108; Evidence={ECO:0000269|PubMed:20530902, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for L-carnithine {ECO:0000269|Ref.2}; KM=8.5 mM for L-carnithine {ECO:0000269|PubMed:20530902}; KM=0.25 mM for NAD(+) {ECO:0000269|Ref.2}; KM=0.24 mM for NAD(+) {ECO:0000269|PubMed:20530902}; KM=1.71 mM for 3-dehydrocarnitine {ECO:0000269|Ref.2}; KM=4.5 mM for 3-dehydrocarnitine {ECO:0000269|PubMed:20530902}; KM=0.04 mM for NADH {ECO:0000269|Ref.2}; Vmax=21.9 umol/min/mg enzyme {ECO:0000269|PubMed:20530902}; Note=Part of the values are for the recombinant protein expressed in E.coli (PubMed:20530902). Other values are for the wild-type protein (Ref.2).; | PATHWAY: Amine and polyamine metabolism; carnitine metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5 for the oxidation reaction and 6.5 for the reduction reaction. {ECO:0000269|Ref.2}; | null | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates since D-carnitine, other carnitine analogs such as choline and betaine, and NADP(+) are not substrates. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation pathway that allows Xanthomonas translucens to grow on L-carnitine as the sole source of carbon and nitrogen. {ECO:0000269|PubMed:20530902, ECO:0000269|Ref.2}. | Pseudomonas sp |
D7Y2H2 | CDNC_ECOM1 | MSTEHVDHKTIARFAEDKVNLPKVKADDFREQAKRLQNKLEGYLSDHPDFSLKRMIPSGSLAKGTALRSLNDIDVAVYISGSDAPQDLRGLLDYLADRLRKAFPNFSPDQVKPQTYSVTVSFRGSGLDVDIVPVLYSGLPDWRGHLISQEDGSFLETSIPLHLDFIKARKRAAPKHFAQVVRLAKYWARLMKQERPNFRFKSFMIELILAKLLDNGVDFSNYPEALQAFFSYLVSTELRERIVFEDNYPASKIGTLSDLVQIIDPVNPVNNVARLYTQSNVDAIIDAAMDAGDAIDAAFYAPTKQLTVTYWQKVFGSSFQG | 2.7.7.-; 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31932165}; | defense response to virus [GO:0051607]; nucleotide metabolic process [GO:0009117] | cytosol [GO:0005829]; membrane [GO:0016020] | 2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872] | null | 1.10.1410.20;3.30.460.10; | CD-NTase family, A01 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=3 ATP = 3',3',3'-c-tri-AMP + 3 diphosphate; Xref=Rhea:RHEA:72755, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192523; Evidence={ECO:0000269|PubMed:31932165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72756; Evidence={ECO:0000305|PubMed:31932165}; CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000269|PubMed:31932165}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35656; Evidence={ECO:0000305|PubMed:31932165}; | null | null | null | null | FUNCTION: Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (PubMed:31932165). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:31932165, ECO:0000303|PubMed:32839535}.; FUNCTION: Cyclic nucleotide synthase that upon activation catalyzes the synthesis of 3',3',3'-cyclic AMP-AMP-AMP (3',3',3'-c-tri-AMP or cAAA) as the major product, and 3',3'-c-di-AMP as a minor product. Cannot use GTP as a substrate. {ECO:0000269|PubMed:31932165}.; FUNCTION: Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death, which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation. {ECO:0000269|PubMed:31932165}. | Escherichia coli (strain MS 115-1) |
D7Y2H4 | CAP6_ECOM1 | MNVKPSLDELFERRINFPDFEPQERLARLVGLDEHKDRLSKILGLLVNPYGIQEWAKKYHPDARAAVDTVLRRPPLVVLAGDVGSGKTELAETIGDAVARQEDIDITLYPLSLATRGQGRVGEMTQLVSAAFDYTIEAADKLKNTNGKARGAVLLLIDEADALAQSRENAQMHHEDRAGVNAFIRGIDRIANQKLPAAVLMCTNRLKALDPAVQRRAAEILTFSRPNDEQRHYLLHSKLTGLGLNSTAVEELVRLTGPRDPNSPGFTFSDITQRLIPSIILAAYPYNAVSVHSALQVVNKMTPTPAFIDRQ | null | null | defense response to virus [GO:0051607] | microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00004; | 3.40.50.300; | AAA ATPase family | null | null | null | null | null | null | null | FUNCTION: Regulates complex assembly in a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:31932165, ECO:0000303|PubMed:32839535}.; FUNCTION: Binds and disassembles an active CdnC:Cap7 (Cap7 is also called HORMA) complex, inhibiting the complex's ability to synthesize cyclic nucleotide second messengers (PubMed:31932165). An AAA+-ATPase remodeler, in the absence of foreign threat Cap6 (also called Trip13) probably maintains the Cap7 protein in its open, inactive state. Once activated (presumably by a bacteriophage protein) Cap7 binds to and activates its cognate CD-NTase (CdnC in this bacteria) to synthesize cAAA, a cyclic nucleotide second messenger. cAAA activates the NucC endonuclease which degrades all DNA in the infected cell, causing cell death and abortive phage infection (Probable). {ECO:0000269|PubMed:31932165, ECO:0000305|PubMed:31932165}.; FUNCTION: Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible E.coli strain it confers bacteriophage lambda cI- immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death, which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation. {ECO:0000269|PubMed:31932165}. | Escherichia coli (strain MS 115-1) |
D7Y2H5 | NUCC_ECOM1 | MSDWSLSQLFASLHEDIQLRLGTARKAFQHPGAKGDASEGVWIEMLDTYLPKRYQAANAFVVDSLGNFSDQIDVVVFDRQYSPFIFKFNEQIIVPAESVYAVFEAKQSASADLVAYAQRKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESDWSPALGMSFDKALNGDLSDGRLDMGCVASHGHFYFNNIDSKFNFEHGNKPATAFLFRLIAQLQFSGTVPMIDIDAYGKWLAN | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31932164, ECO:0007744|PDB:6P7O}; | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF20247; | null | NucC endonuclease family | null | null | null | null | null | null | null | FUNCTION: Effector DNase of a CBASS antivirus system (PubMed:31932164, PubMed:31932165). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:31932164, ECO:0000269|PubMed:31932165, ECO:0000303|PubMed:32839535}.; FUNCTION: A cyclic nucleotide-activated dsDNase. In the presence of 3',3',3'-cyclic AMP-AMP-AMP (cAAA), and to a lesser extent 3',3',3'-cyclic AMP-AMP-GMP (cAAG) and cyclic-di-AMP (c-di-AMP), endonucleolytically degrades dsDNA (PubMed:31932164, PubMed:31932165). Binds one cAAA in a pocket on one surface of the trimer; cAAA binding promotes hexamerization, which is necessary for nuclease activation. Also binds c-diAMP or linear di-AMP with lower affinity. The nuclease digests dsDNA to about 50 bp lengths with a 2-base 3' overhang and a consensus recognition site of 5'-Axx|T-3'. DNA has been modeled to contact a pair of juxtaposed active sites (one from each layer of the hexamer), accounting for cleavage on both strands and the 2-base overhang (PubMed:31932164). {ECO:0000269|PubMed:31932164, ECO:0000269|PubMed:31932165}.; FUNCTION: Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation. {ECO:0000269|PubMed:31932164, ECO:0000269|PubMed:31932165}. | Escherichia coli (strain MS 115-1) |
D8LQS7 | HPB_ECTSI | MQRVGAASPTCSSLQAPAAAPPILTISPHHRVKTAETAAEPDLLEPTGVHHPFHSLSPLTEARAWAAREGQYFNGLIEANGGASVSKGHPDLAVTFLTDHASCEWFFSQRQEVLDRQDGAYFGPLKCKKQYIGESLPTLASNQKESHQVLREHKLRVFRSRVPFAQSAMTNATDTFYKNLRDNGTGDYTVVYDFFLQQTIHFLHEWIYGLGVEGGQPLPPFKDFMNANPLDVSVLLELEMDTPVANLAAKLAQRSKKPSAEQLASVESIAEAIRSSDVWAGFVEMLEDSNVNTKDLERSFMFTTNFQSAGAIAKGMMPVVATLTNNPEFLEKLRKEVDGKDLTFQSIRGAENFPLLDSFHWEINRMFPAPAFTVKEAKMDLVVPTSSGKKYKVKKGELLMMEQALGQMDPSVFGPDAREFNPERFVDNPELKKKVFAYGYVDHDKVDGQWGCAAHAIGMLDGILKIIYGRWVQEAEWELTSVPVISPDEFLAEVGPADMSFAKVTSRKKM | 4.2.1.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | fatty acid biosynthetic process [GO:0006633]; oxylipin biosynthetic process [GO:0031408]; sterol metabolic process [GO:0016125] | mitochondrion [GO:0005739] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; lyase activity [GO:0016829]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = plasmodiophorol A; Xref=Rhea:RHEA:75603, ChEBI:CHEBI:58757, ChEBI:CHEBI:194366; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75604; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = plasmodiophorol B; Xref=Rhea:RHEA:75607, ChEBI:CHEBI:58757, ChEBI:CHEBI:194367; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75608; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = ectocarpin A + H2O; Xref=Rhea:RHEA:75599, ChEBI:CHEBI:15377, ChEBI:CHEBI:58757, ChEBI:CHEBI:194362; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75600; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate = ectocarpin B + H2O; Xref=Rhea:RHEA:75615, ChEBI:CHEBI:15377, ChEBI:CHEBI:194363, ChEBI:CHEBI:194369; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75616; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate = ectocarpin C; Xref=Rhea:RHEA:75619, ChEBI:CHEBI:194364, ChEBI:CHEBI:194369; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75620; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + H2O = ectocarpin D; Xref=Rhea:RHEA:75627, ChEBI:CHEBI:15377, ChEBI:CHEBI:194365, ChEBI:CHEBI:194369; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75628; Evidence={ECO:0000269|PubMed:35835431}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate = 14-oxo-15-hydroxy-(5Z,8Z,11Z,17Z)-eicosatetraenoate; Xref=Rhea:RHEA:75623, ChEBI:CHEBI:194369, ChEBI:CHEBI:194370; Evidence={ECO:0000269|PubMed:35835431}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75624; Evidence={ECO:0000269|PubMed:35835431}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=133.3 uM for 13-HPOTE {ECO:0000269|PubMed:35835431}; KM=183 uM for 15-HPEPE {ECO:0000269|PubMed:35835431}; Note=kcat is 1446.7 sec(-1) with 13-HPOTE as substrate (PubMed:35835431). kcat is 1134.7 sec(-1) with 15-HPEPE as substrate (PubMed:35835431). {ECO:0000269|PubMed:35835431}; | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000269|PubMed:35835431}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:35835431}; | null | FUNCTION: Cytochrome P450 hydroperoxide bicyclase involved in the metabolism of oxylipins 'ectocarpins' natural products, such as hybridalactone, ecklonilactones and derivatives (PubMed:35835431). Isomerizes the hydroperoxides into epoxyalcohols via epoxyallylic radical (PubMed:35835431). Can use alpha-linolenic acid 13(S)-hydroperoxide (13-HPOTE) and eicosapentaenoic acid 15(S)-hydroperoxide (15-HPEPE) as preferred substrate to produce corresponding heterobicyclic oxylipins, such as plasmodiophorol A (6-oxabicyclo[3.1.0]hexane), plasmodiophorol B (2-oxabicyclo[2.2.1]heptane) and plasmodiophorol C (4-hydroxymethyl-1,2-dihydroxycyclopentane) as well as ectocarpin A (3-propenyl-6-oxabicyclo[3.1.0]hexane) formed at about 15:3:3:1 ratio for 13-HPOTE, and analogous to plasmodiophorols A and B including ectocarpin B (3-[(1'E)-propenyl]-6-oxabicyclo[3.1.0]hexane), ectocarpin C, 14-oxo-15-hydroxy-5,8,11,17-eicosate-traenoic acid and ectocarpin D for 15-HPEPE (PubMed:35835431). Barely able to use linoleic acid 13-hydroperoxide (13-HPODE), linoleic acid 9-hydroperoxide (9-HPODE), eicosapentaenoic acid 15-hydroperoxide (15-HPEPE), and alpha-linolenic acid 9-hydroperoxide (9-HPOTE) as substrates (PubMed:35835431). {ECO:0000269|PubMed:35835431}. | Ectocarpus siliculosus (Brown alga) (Conferva siliculosa) |
D8QTR2 | MGH1_SELML | MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATGACTDESEIRGWTARANVAFDTLFDVEAGLYRCKDQLTGQFLPAATSAGFLPLFAGVASGEKASAVARTLGRWLDDVAYGIPSCDPRDPQFEALRYWRGPVWLIVNWMVSEGLKRYGYGELAQRVERDSYELVKNGGIFEYYCPLTGMGAGGGCFSWTAAMCLAWLFKT | 3.2.1.170 | null | mannosylglycerate metabolic process [GO:0051478]; oligosaccharide metabolic process [GO:0009311]; protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum membrane [GO:0005789] | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [GO:0004573]; glucosylglycerate hydrolase activity [GO:0102547]; mannosylglycerate hydrolase activity [GO:0102546] | null | 1.50.10.10; | Glycosyl hydrolase 63 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + D-mannose; Xref=Rhea:RHEA:58456, ChEBI:CHEBI:4208, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:57541; EC=3.2.1.170; Evidence={ECO:0000269|PubMed:23179444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58457; Evidence={ECO:0000269|PubMed:23179444}; CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510; Evidence={ECO:0000269|PubMed:23179444}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32060; Evidence={ECO:0000269|PubMed:23179444}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.8 mM for 2-O-(alpha-D-mannosyl)-glycerate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; KM=5.9 mM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; Vmax=40.5 umol/min/mg enzyme with 2-O-(alpha-D-mannosyl)-glycerate as substrate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; Vmax=7.3 umol/min/mg enzyme with 2-O-(alpha-D-glucopyranosyl)-D-glycerate as substrate (at 40 degrees Celsius) {ECO:0000269|PubMed:23179444}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.50. {ECO:0000269|PubMed:23179444}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23179444}; | FUNCTION: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose (PubMed:23179444). Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency (PubMed:23179444). {ECO:0000269|PubMed:23179444}. | Selaginella moellendorffii (Spikemoss) |
D8VPP5 | AL11A_OLEEU | MSCIAVEAVLLGILLYIPIVLSDDRAPIPSNSAQLNSWFDGIIQPVAVRKATMDPALVTAEGQTKVIKLKSDGSGDFKSINEAIKSIPDDNTKRVILSLAPGNYSEKVKIGMYKHYITFYGEDPNNMPILVFGGTAAEYGTVDSATLIVESNYFSAVNLKIVNSAPRPDGKRVGAQAAALRISGDKASFYNVKIYGFQDTLCDDKGKHFYKDCYIEGTVDFIFGSGKSIFLNTELHAVPGDQPAIITAQARKTDSEDTGYYFVNCRVTGGGAFLGRSWMPAAKVVFAYTEMVDAIHPEGWILVKPEHESTVRFSEYNNKGPGANMEKRAKFVKRLSDAEAKQSISLGSIEASKWLLPPRVVGLP | 3.1.1.11 | null | cell wall modification [GO:0042545]; pectin catabolic process [GO:0045490] | extracellular region [GO:0005576] | aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599] | PF01095; | 2.160.20.10; | Pectinesterase family | PTM: Glycosylated. {ECO:0000269|PubMed:20491902}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20491902}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11; Evidence={ECO:0000269|PubMed:20491902}; | null | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:20491902}; | null | FUNCTION: Catalyzes the demethylesterification of homogalacturonan components of pectin. May be involved in pollen tube development. {ECO:0000269|PubMed:20491902}. | Olea europaea (Common olive) |
D9I2F9 | NL1A1_RAT | MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSNDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of pyroptosis [GO:0140639]; programmed necrotic cell death [GO:0097300]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981]; response to muramyl dipeptide [GO:0032495]; self proteolysis [GO:0097264]; stress-activated protein kinase signaling cascade [GO:0031098] | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor activity [GO:0038187]; peptidase activity [GO:0008233]; protein domain specific binding [GO:0019904]; protein self-association [GO:0043621]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 1]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: (Microbial infection) Cleavage by B.anthracis lethal toxin (LT) endopeptidase promotes ubiquitination and degradation of the N-terminal part, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000305|PubMed:20502689}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:33731929). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:20502689, PubMed:31383852, PubMed:33731929). In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). {ECO:0000250|UniProtKB:Q2LKU9, ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:20502689, ECO:0000269|PubMed:31383852, ECO:0000269|PubMed:33731929}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a allele 1]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome (PubMed:33731929). In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:33731929}. | Rattus norvegicus (Rat) |
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