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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
G5EDE5
|
RGMB_CAEEL
|
MSIVYLVSITFIFSVFKPITSCRVEECAAWFQKTKDYENLVPKATERYCQVLQTYLKCMNDTQRYCHGNLRFHSSELIMRRHWKEFECEKWESCNDNSHVKRKHVNTCYFNPPPSNRKLKYCSLFGDPHLIMFNGSVQTCSEEGARPLVDNRYFLVQVTNRNVRGEALTTTVTKVTVLVRKHNCTASLRYEASSDEEGLPRGFVDGTTFQMTSKHSVEVLWQDDNYVEIALHFIHSSIHIRRQGPYLSVSVRAPTIVLETGGDVARELCWSGCRKSSRIPAELAVEMTKKFAECYRRRVHVPKKVAEDRCKDIGNIGVFFDACVFDLMFTGDDYLVHLSRAAESDFRRLAPHHFQSHVTQQHARFQKENQHKNHINQSEIFKKCIPSKSIRFYPFLAIFFFALLSLLC
| null | null |
BMP signaling pathway [GO:0030509]; mesodermal cell fate specification [GO:0007501]; positive regulation of multicellular organism growth [GO:0040018]; regulation of BMP signaling pathway [GO:0030510]; regulation of dauer larval development [GO:0061065]; regulation of multicellular organism growth [GO:0040014]
|
plasma membrane [GO:0005886]; receptor complex [GO:0043235]; side of membrane [GO:0098552]
|
coreceptor activity [GO:0015026]
|
PF06534;PF06535;
|
3.40.1000.10;
|
Repulsive guidance molecule (RGM) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20534671}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q7TQ33}.
| null | null | null | null | null |
FUNCTION: Probably in association with the cell surface receptor unc-40, positively modulates the BMP-like Sma/Mab signaling pathway through interaction with both the ligand dbl-1 and its type I receptor sma-6 (PubMed:24004951). Regulates body size and this may be through modulation of the Sma/Mab signaling pathway (PubMed:20534671, PubMed:24004951). {ECO:0000269|PubMed:20534671, ECO:0000269|PubMed:24004951}.
|
Caenorhabditis elegans
|
G5EDF0
|
GRH1_CAEEL
|
MSFQLDQSTSVIKTAPPGRLEFKNEPIDIASSNIQDLAKMQTLDGYYQQTSLQLPQSQQYHRMYENVYNNQQILYAQTQNFQYPSTLLTNGSLAQTEWRGQQMDTSAYSNTGYSRSSTSQQPQYTQQVTENERIVYKPVDMPSPVDSGIGGDISILNPKEEFFTSADGGSMLERSSERTLSHRDSPLVIPKLYNNLGFQYVLEAPISTSVRRDDDRMTYVNKGQFYTVSLEYTPDLNKCLKSQTVKSQLMVVFREDKTYEEEIKTWQSWHARQHVSKQRILEIDSKNSSGMIGQIEEIGNNAVQFYWNPSDPSGVRISIAVQCLSTDFSTQKGVKGLPLHVQIDTYDGENDKVPFHRGYCQIKVFCDKGAERKLRDEDKRAQKRKVQEYTAGALPGGRKKSDGEYHDQCERSEFYHMRELDKPAALFIAPEEFEPRYVDSTSLSFDMSEIEPIPTKRPRTSERIMLYVRKRDEQIYQPLHVVPASLSGLALAIANKFGADPDKMSGVYKRCAKGITVKVDDEMLRLYCNEDTFIIDVEHATDGSTAATLIEVAPTNPNSYSNS
| null | null |
defense response to bacterium [GO:0042742]; determination of adult lifespan [GO:0008340]; ecdysis, collagen and cuticulin-based cuticle [GO:0042395]; molting cycle, collagen and cuticulin-based cuticle [GO:0018996]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; 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]
|
PF04516;
| null |
Grh/CP2 family, Grainyhead subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor (PubMed:12888489, PubMed:36688410). Binds a motif with the core sequence 5'-C[ACT][TG]G-3' in regulatory elements of target genes (PubMed:12888489, PubMed:36688410). Many putative target genes show oscillating expression levels, perhaps as a result of rhythmic variation in accumulation of grh-1 (PubMed:36688410). Plays a role in proper cuticle formation and/or barrier function and is required repetitively during development, for successful completion of each molt (PubMed:36688410). Involved in modulating lifespan (PubMed:35013237). Plays a role in defense response to bacteria (PubMed:35013237). May act upstream of the p38 MAP kinase / pmk-1 pathway (PubMed:35013237). May act downstream of the insulin/IGF-1 receptor signaling (IIS) pathway (PubMed:35013237). {ECO:0000269|PubMed:12888489, ECO:0000269|PubMed:35013237, ECO:0000269|PubMed:36688410}.
|
Caenorhabditis elegans
|
G5EDF7
|
SEK1_CAEEL
|
MERKGRERKLPGMKIVMPTPVETPTMNLEDRCLIKLTNESEEIEIAATDLVVLEELGKGGYGIVEKMQHRQSGIIMAVKRIKSSINDQSQKQMLNELDACRRSDCCPQMVRFYGAMFREGDVWICMEVMDTSLDKFYRHAYKIGKHIPEPFIGKMALSVIEGLNFMKEQLNLIHRDVKPSNILLNRHGQVKICDFGISGHLTNSMAKTVQAGCKPYMPPERIDGETKSAYDVRADVWSLGITIIEIAVGTHPYANWKTPFEQLKQVVKEPPPKLPMESGFSVDCQYFVKRCLEKDYNERPKYPELLAMPFMEQARNEKQFSMARFINEILDTVWRR
|
2.7.12.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11751572};
|
defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; determination of left/right asymmetry in nervous system [GO:0035545]; innate immune response [GO:0045087]; MAPK cascade [GO:0000165]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; p38MAPK cascade [GO:0038066]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of egg-laying behavior [GO:1901046]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of egg-laying behavior [GO:0046662]; response to nematicide [GO:0093002]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; response to superoxide [GO:0000303]; response to toxic substance [GO:0009636]; stress-activated MAPK cascade [GO:0051403]; turning behavior involved in mating [GO:0034607]
| null |
ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; metal ion binding [GO:0046872]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
| null | null |
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=2.7.12.2; Evidence={ECO:0000269|PubMed:11751572}; 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=2.7.12.2; Evidence={ECO:0000269|PubMed:11751572}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000269|PubMed:11751572};
| null | null | null | null |
FUNCTION: Dual specificity protein kinase which acts as an essential component of the p38 signal transduction pathway which is also composed of upstream effector nsy-1 and downstream effector pmk-1 (PubMed:11751572). May phosphorylate pmk-1 (PubMed:12142542, PubMed:16166371). Downstream of CaMKII unc-43 and adapter protein tir-1, plays a role in determining asymmetric cell fates in olfactory AWC neurons during neuronal development. Activation results in the repression of odorant receptor str-2 expression in one of the 2 AWC neurons (PubMed:11751572, PubMed:12142542). Involved in resistance to pathogenic Gram-positive and Gram-negative bacterial and fungal infection (PubMed:12142542, PubMed:18394898, PubMed:22216003). Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 (PubMed:20062796). Probably by promoting pmk-1-mediated activation of skn-1, involved in the up-regulation of gcs-1 and glutathione-S-transferase gst-4 expression upon bacterial infection (PubMed:22216003). Probably downstream of tir-1, required for the expression of antimicrobial peptide nlp-29 in the epidermis in response to fungal infection or physical injury (PubMed:18394898, PubMed:22308034). Regulates susceptibility of B.thuringiensis pore-forming toxin Cry5B and Cry21A (PubMed:15256590). Involved in the response to oxidative stress (PubMed:15888317, PubMed:22308034). May regulate transcription factor daf-16 localization during oxidative stress (PubMed:15888317). By phosphorylating pmk-1, regulates skn-1 localization during oxidative stress (PubMed:16166371). By phosphorylating and activating pmk-1, plays a role in the stabilization of transcription factor rnt-1 in the intestine during oxidative stress (PubMed:22308034). Up-regulates expression of gcs-1 in intestine upon arsenite treatment (PubMed:16166371). Regulates germline proliferation in response to osmotic stress, starvation and germline apoptosis induced by heavy metals, such as Cu(2+) (PubMed:16729024, PubMed:19497412). In association with mek-1, regulates germline cell apoptosis in response to oxidative, osmotic and heat shock stresses (PubMed:16729024). Plays a role downstream of tir-1/nsy-1 in regulating susceptibility to anoxia (PubMed:21212236). In males, by regulating pqn-41 expression, involved in non-apoptotic death of the linker cell which guides gonad elongation during larval development (PubMed:22363008). Involved in egg laying (PubMed:12142542). {ECO:0000269|PubMed:11751572, ECO:0000269|PubMed:12142542, ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:15888317, ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:16729024, ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:19497412, ECO:0000269|PubMed:20062796, ECO:0000269|PubMed:21212236, ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22308034, ECO:0000269|PubMed:22363008}.
|
Caenorhabditis elegans
|
G5EDJ0
|
FAX1_CAEEL
|
MSDEDEPLNFSTSKATEESKEGILGVRSIFNTPLLFPPPMFNAGVISPHIAAALAMSFNQQRMNASVSPPLDHTTISVNSFPSMGSVKTDSPPTASSPTLCCAVCGDVSSGKHYGILACNGCSGFFKRSVRRRLIYRCQAGTGNCVVDKAHRNQCQACRLKKCLNKGMNKDAVQNERQPRNTATIRPALDMDPQNFFREYAGAVSAIMGHSNMMKREDSPSSASDGKTEDEKKDSLQETTMSQLESVLQWAQQFRLFTVLTNSEKRQIILTQWPRLLCISLCEQAEDVSFDDHLTSLMLKFRRLDVSPAEFNCLKAITIFMKRELSLWRAGWDNRASIITVYPAGERGARLVAAALLLAEHSVMGFGNCVIPLALVFSTKSRYVIQRHAINSLPACVPGGTSAHPVLRCSMGSRREKVI
| null | null |
axon guidance [GO:0007411]; cell differentiation [GO:0030154]; locomotory behavior [GO:0007626]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron fate specification [GO:0048665]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of backward locomotion [GO:0043058]; regulation of forward locomotion [GO:0043059]; regulation of transcription by RNA polymerase II [GO:0006357]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
|
PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10648229, ECO:0000269|PubMed:16183052}. Cell projection, axon {ECO:0000269|PubMed:10648229}. Cytoplasm {ECO:0000269|PubMed:10648229}.
| null | null | null | null | null |
FUNCTION: Orphan nuclear receptor that binds DNA containing an extended core motif half-site sequence 5'-ANGTCA-3' (PubMed:10648229, PubMed:18179707). Required for locomotion, neuron axon pathfinding, and regulation of expression of some peptide neurotransmitter precursors and of NMDA glutamate receptor genes (PubMed:10648229, PubMed:16183052, PubMed:22690911, PubMed:9216999). Involved in specifying interneuron identity, in concert with paired-like homeodomain unc-42 (PubMed:16183052). Plays a role in recognition of the PVPR and PVQL axons by the AVKR and HSNL growth cones (PubMed:9216999). {ECO:0000269|PubMed:10648229, ECO:0000269|PubMed:16183052, ECO:0000269|PubMed:18179707, ECO:0000269|PubMed:22690911, ECO:0000269|PubMed:9216999}.
|
Caenorhabditis elegans
|
G5EDJ4
|
SOC1_CAEEL
|
MSIPDENIILEGSLKRCKKYKLFKTKWVEHYFVLHCRDRERNLFAIDEFKTSRKNDLKKRFKLEFVIRVESNLSVSDPSILCTAGGGHQEESMLNCIFGVGFRFENIVKDLYLVAKNDEEMTLWVNEICKLCKLHRQHDEGDSSHAAESSISGMSMSSQSLDMSIIEQQQYAENIPESKQYHRMHHFKSVISHNSLPSNPNYNNLPDPLESSRSETSSMYSSRRTEDDSVSYTSGPPVPPPRTRHTLNRFVKNGQVGRLHMIPASTSMGQVVKVEDAEDSSGETLKLDTPEQYPESVTSSEGFPVYERNGKTLIRRAPPPVDRSNKPKNLRGEEEAGTRYRNLSRNGVNENGNYSATFSSRTSNYQQSETSKRRNLDYFEPTQMIENSSLSTLAATSTRSPTPSDIEYISVDVDRTLAFKQMRRAAQSTD
| null | null |
dauer larval development [GO:0040024]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]
|
signaling adaptor activity [GO:0035591]
|
PF00169;
|
2.30.29.30;
| null |
PTM: May be phosphorylated. {ECO:0000269|PubMed:11689700}.
| null | null | null | null | null | null |
FUNCTION: Adapter protein which modulates signaling mediated by several receptor tyrosine kinases. Plays a role in fluid homeostasis, probably downstream of receptor egl-15 and upstream of let-60/Ras (PubMed:11689700). Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and levamisole and gamma-aminobutyric acid (GABA)receptor-mediated sensitivity to muscimol (PubMed:15990870). Regulates synaptic levels of nAchR receptor subunit lev-1 and unc-38, and GABA receptor subunit unc-49 in the nerve cord, probably downstream of egl-15 (PubMed:15990870). Regulates motility (PubMed:15990870). During the formation of neuromuscular junctions at the larval stage, down-regulates membrane protrusion from body wall muscles, probably downstream of egl-15 (PubMed:16495308). Promotes vulva induction and down-regulates fertility, probably downstream of receptor let-23 (PubMed:16547100). Down-regulates daf-2-mediated repression of dauer formation and positively regulates daf-2-mediated aging (PubMed:16547100). May be involved in the recruitment of phosphatase ptp-2 to egl-15 (PubMed:11689700). {ECO:0000269|PubMed:11689700, ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100}.
|
Caenorhabditis elegans
|
G5EDK5
|
CELR_CAEEL
|
MMLDRIMFLLFFILSLVIGSFSEYLDDKYYSTNSIDVVCKPCAVPSSNSVIWLPASRPPCLHPGQPIIHWPDLSDNLACPVPGLPDSVHSSQISLLEGEGLLLTKERICFFDGPIDFHYDYVCDGKLYRSKMRIGHSIASKKKLETRRTKRWARRRNPDANAVHFQQEKYVKELPEDTPIETIIASVKASHASSQPLYYSMVAPQDSRSQNLFTLDTMSGEIRLAKSMDREVLDKHILKVTAYERVDPTISASTTVVVHVLDVQDNSPIFEKDSYFGEIREDAPIGTTVLSVFARDLDSGENGEIEYSLGEGNGKNLLAINAKSGVIQTAAPLDRETLSLIRLDVIASDKGTPKRESTAMVEITVVDVNDNAPVFASDSYNVTILENITIPAVIATVKATDEDFGTNGKVHYSMASSSGIGGLTIDYSTGEVTLRERIDAKNSPITAVIRAKDGAQPALSSTVPLTINVIDINDHAPTLIAAQKMITLEENVAIGEEVGRVYAIDEDSGPNGIIKYSMEGSEDFIIDEDSGLIKTTKLLDRETTARYSLKVTARDMGTPSLNTSTTIAVVLKDINDNAPTFDKKEYNVTISEEMPRGSQIITLKAVDNDEDQKITYRIEEADREVFSILDIGDQGAILSVSGELKRQDHKVRVEISATDQGGLQGRCVVNVFIDDVNSAPYFNDHPFSVKIPEHSPIGYPVITLKAEDHDRGDNARIVYSIDSSQFFRIDPSSGDISVSSDLDREDRATFSVIVTASDHASPPLNTSTQIEVILDDINDNSPQFTSSSYAATISEDIPVGTSFLQVSAIDADIGPNGIVDYFLNESSSSPSIQLFRLDRTSGTLRVSSKLDREQFAVIVLPIFARDRGTPSLSAASEITLTLSDVNDNAPTFEQLSYDLYIAENSPVGSTVGTIVARDADEGDNADISFRIFGGADAKLFDIEEDAEQNGVVRILTRAEFDYEAKANKFFFELQASSGQLSSTVPVRIHVSDVNDNKPALKDFVILMNRFDNVQMARQIGFIPAFDPDQNATLEYFLEENDLIEAEKYTGKILVKQEWKRNMDVSFKTCVSDGANTECSTCRFIHVLVEPEWLSESFTLSLARMTVDDFWDPLVFQRFRDAMSTLSNWKPSDIHVIGVKQHLDDVIYINIAITDHGRVVRGWRAIELVKESIKKLEKMTLLQVEVIRDESCANEPCSHMAKCRQTQKFVGEMKAHETDNFIARTLNTVNTFVCECPSGFTSSGAHGDCDTRIDECYRGRCSNNSTCVAFENTYQCECKPGWIGRHCEISVHALTCVPGYCMSDSLCELDGNQMKCRHCKYHGEDTDERCRLRSVSFDGEGLLNVNLDLPRTQWTMKFRVSTIAHNGVLVFTGDKRSDFVEVSVVDRVLKVQFSLGGEKIDAKMENDVENRINDGEWHTVALEYSNKQITMSLDDCETNPSLLLNTSPNCAIRAKLNLEKKCEDPTVPCYRYLDISNGLFLGGRPGTSKQIEKAFSGCISDLSVDKEDVDFSTIKEMHKVGQVHEGCKHRKDFCSTSDGQCSATSKCVNRWGGRICSCPQSVHSTGECVGALGTQDLRGHSLFEEESFVLYQPSQVSVPFEVSFEFRTSRADMQVFALEFTQRSVHYNLEVDDGTLKYNIGDSEVELPAPEVTSKHWMNVVIKFEADSVATSINGIYSAEAKASISDMNLESLYFGIAPGTGHPSRFEGCIRNVLVDGRSISVKKKGKTRAGCVVPNRCSVDSICPAESTCHRAWNKHKCKCHKSFVGDTCLPVCSVANVCSSGTCVSSNTTAGYECICPAGKTGKNCQLEAPKQMCPSGWWGTFPRCRRCSCAQTKDYEAQCDKKTGACQCKKSHFSTINGCVKCECGFGADSTECSADGHCKCNGDAVGRRCDRCSRFDHQLDSKTLKCRPVSGKCPSEIEYSIQWPASQKGSIVRQSCPVGESGLATRKCLETGRWSDVNAWNCTRPEYSIMVNKFEILEPSKLLTMVANATNTESSIRGRNQQIAAEALSRLVDYEQSMPMKGRAHIKDMKFTEKLIESLGRVMSEQPADEYSTLISKLWNYAETVAEIHENVNFLSPFFVANDHIVFASDKLDFGNILPKFNNFVDLRPTGFPRVRAIVTGTTQVVYSIVPYPRCNRCENPMIAIVANTSDPVIVEFEIEEDDGWKYPECVRFDEKSGTWTARGAALIGLNLTHAACEYNRIGVFTMFVNDQSSSIVRVAQMDNMTSPAIAGVALFLCFLSILLTLSRRSLKTHSVRIGFILFFAINILNLFFVHKTAINQAYCPVRNAMLSFTSSAPFAWLFLYGLYIYRMLADGSSSPSLTTSLLVGIVFPCLISFTTFFVTDQCSLSPHLWLFWCIILPIGLFLLLSFYAAATSVLVSLHKKYDVFVAKYNVKRAVFQHFILTIFTLGMTLTGLFANQLPLPMEIMEISQSIIYLIAALVIFLWCVCDITTKASDSNPSMWLDNQKSVMAESTMADPQCASPLLSPRHQHHEVPMDSEWVPDVNPSNHYHTSINEPDTPRRLLLPQNRDVINILSSPDQILNEGVGHVYRNNMGSLPRLRSAQDEADDAYYTYTASRKYKNTTSTFNRE
| null | null |
anterior/posterior axon guidance [GO:0033564]; cell-cell adhesion [GO:0098609]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; interneuron axon guidance [GO:0097376]
|
axon [GO:0030424]; dendrite [GO:0030425]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF00028;PF00008;PF02210;
|
2.60.120.200;2.60.40.60;4.10.1240.10;2.10.25.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, LN-TM7 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:20876647}. Cell projection, dendrite {ECO:0000269|PubMed:20876647}. Note=In embryos, localizes to axons in the nerve ring, the tail and along dendrites of sensory neurons. {ECO:0000269|PubMed:20876647}.
| null | null | null | null | null |
FUNCTION: During ventral cord development, required for axon fasciculation and navigation, mediating both pioneer and follower axon extension, guidance and track formation (PubMed:20876647, PubMed:22442082, PubMed:23376536, PubMed:28846083). Acts in CEPsh glia and SubL neurons to guide follower axons into the nerve ring (PubMed:28846083). Promotes motorneuron development by positively regulating the extension of the anterior neurite of ventral D-type GABAergic motorneurons along the anterior-posterior axis of the ventral nerve cord (PubMed:23376536). Plays a role in synaptogenesis by regulating synaptic vesicle accumulation at GABAergic and cholinergic neuromuscular junctions (PubMed:22442082). {ECO:0000269|PubMed:20876647, ECO:0000269|PubMed:22442082, ECO:0000269|PubMed:23376536, ECO:0000269|PubMed:28846083}.
|
Caenorhabditis elegans
|
G5EDM4
|
NHRF1_CAEEL
|
MVHIPSDVTPPRLCVVEKLNGENEYGYNLHAEKGRGQFVGTVDPDSPAERGGLITGDRIFAVNGHSIIGENHKKVVERIKANPNRCEMLVISEEGAKWYNENNVQITLDLPNIERVSPMSKETPVFVPPPPPPTDAMPYLPRLAELNKGTPDQEFGFNLHAERGRGHFIGTVDAGGIGEKAGLEAGQRIVGVNGQLIYPTTGHKEVVALIKKDTMKTTLLVASEDVDKYHKDHNIAYSWDNVERVDTRPVINVETHHHHEEVSVPKSNGYDVPPLNPHSIQVNEEREISKMTTTTRTETITNSNSAYQYKESSTAYDAYATPPVDSNDLMDEVFGRVNLPGVTMSSHTEVLPPTDDISSVSSLSSHRESAVDVPVSHQYVPSYATESHQKHEQHSQTHHHHHQHQQPSPLSNGSSHGYAASSTSGYDDDDIYHLSAREARERLRMKNRKHHLHEMSLNEKYQLVSNM
| null | null |
intracellular amino acid homeostasis [GO:0080144]; L-amino acid transport [GO:0015807]; protein localization to plasma membrane [GO:0072659]
|
amino acid transport complex [GO:1990184]; apical plasma membrane [GO:0016324]; microvillus membrane [GO:0031528]
|
protein-membrane adaptor activity [GO:0043495]; signaling receptor binding [GO:0005102]
|
PF17820;
|
2.30.42.10;
| null |
PTM: Phosphorylated. {ECO:0000269|PubMed:22916205}.
|
SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:22916205}. Apical cell membrane {ECO:0000269|PubMed:22916205}. Note=Co-localizes with aat-6 at the apical cell membrane of intestinal cells. {ECO:0000269|PubMed:22916205}.
| null | null | null | null | null |
FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression (By similarity). Anchors the amino acid transporter protein aat-6 to the apical cell membrane of intestinal cells, particularly in older animals, in order to maintain amino acid homeostasis (PubMed:22916205). May play a role in promoting fertility (PubMed:30560135). {ECO:0000250|UniProtKB:O14745, ECO:0000269|PubMed:22916205, ECO:0000269|PubMed:30560135}.
|
Caenorhabditis elegans
|
G5EDM7
|
DAF5_CAEEL
|
MSDSPIGSSQQVEPEHRTPDLMDIDPLIANLKALHEETRSDDDDDGQPSTSAKRKDSRADGIVIHQKKYSDPGRFLWIWLLGVRVPALSIDGEPHLPIEILDDMLTKKDKKDQMSFQNLLRYKNVYIRMASPSQFRAVMEKSKECENLNITSLSLMSRSDIERIMGELRLESMLTLAEHDNWDISDRVHVVHVNFIDYCSEWLESDDLEEDVMQSGTHGYWYKNRRNMRCIECQHCEGKFTPTDFIMHHHYPIKPSGFVHTGCNSFQWIRLIEVFDKSNENLEAWNKFVLNSHRAGKREYDEAAPHQAPPKRPAMETPVPVAADNGWEADEEEEGEEIVDRDADIEKCKLRNKKKMENLHIADFLGPSGSKGLKPRNKFEAVIIEQLNKMDDAALEALFLKSPEEYNLWVKESDFTHKVVTQQQEWKAKMKDPNFKSRASANFDVSKGEFDNMRHFDNASKATRQEIQQLAEQFANLDRDAKLLTPMEFVLREHALLKNVSADAIRVLCNRPPLPPLPPPPPPPKPKPAPVQPISLGNINFVALAQQLIASGIKLPLPIVTPPVVSTPAPVITPIPAALPISPNSDFLKQQLSTAMSSPALLSLYPKLTAGAYEQLAQFIKTTTVKN
| null | null |
dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of dauer larval development [GO:0061066]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SMAD binding [GO:0046332]
|
PF08782;
|
3.10.390.10;
|
SKI family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681186}.
| null | null | null | null | null |
FUNCTION: Probable component of transcriptional regulatory complex with SMAD protein daf-3 (PubMed:14681186). Required to regulate entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions (PubMed:14681186). Involved in larvae undergoing cell-cycle arrest during the dauer stage (PubMed:14681186). {ECO:0000269|PubMed:14681186}.
|
Caenorhabditis elegans
|
G5EDN0
|
ACC3_CAEEL
|
MIRTRHVFLFAVLLAFASSQTPTPEAKSSEQSLEENKFFPLPPTTPFPTNAVAATDEDGEELCTSDKTIIEKLLNNYKSFRTPSESGVIVWIEVWVQEVNSVNEITSDFDMDIYVTELWMDSALRYEHLNPCKYNLSLNSEILDQIWKPNTVFINSKSANIHKSPFKNVFLMIYPNGTVWVNYRVQVKGPCSMDFSAFPMDQQSCHLTLESFSYNNQEVDMQWMNWTTPLSLLKKEIVLPDFVMSNYSTSLKHEIYPAGVWNELTMTFVFSRRYGWYIFQAYIPTYLTIFISWISFCLGPKMIPARTMLGVNSLLALTFQFGNIMRNLPRVSYVKALDVWMLVCLTFVFCSLLELAIIGSMGARSENRQAQQQKQQDEEATKHQKGRENSTCSHLMSPSSCPNSPRICRNHIPNDVPQSFKSYGSTDPRMRKRLIIASSSTISHAPNANRSEKVLLLDGLEETQFSQVETKFSSMASIKMKKHWTTEEIDRLSMIMFPGLFTLFNIIYWTYYLTVNT
| null | null |
chloride transmembrane transport [GO:1902476]
|
chloride channel complex [GO:0034707]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495]
|
chloride channel activity [GO:0005254]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; neurotransmitter receptor activity [GO:0030594]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15579462}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Probable acetylcholine-gated chloride channel regulatory subunit. Does not have ion channel activity alone as a homopentamer, but forms a functional heteropentameric ion channel with acc-1. {ECO:0000269|PubMed:15579462}.
|
Caenorhabditis elegans
|
G5EDN3
|
TIM_CAEEL
|
MNVLVQGAVHALGYYEDGKYSREPDCYESIRDLIRYLREDGDDHTARIECGRHNLVEQDLVPMVKCEDLTDDEFDIAIRLMVNLCQPAISTMRGKPPADRDQWKMYWELEENLRRAKTAFSDAHFFTAIKKRIDNYFIDTEYEDRDERLRLVVERIVLLIKYVFSINPDTSEGRRTRIEDSSHDRVIIAFLESGIDKTLMHIANQPREKEFHVTILDIFALILKEQTAEDLATKSEEVSTAEQKKTEEEFRKIIENHVVKETQKRKSFSRFGGSYTIKGLKGISANSSQVVFKPIQNVEKHNFLDDRKAKKRAPRNRRPFEIDTNSHFASSEVRGMLRDMVIRIIETCFNRLMKSSKTTVFVQVQKTSQINYFFLIKFVLRFVRLSRQDHLLERISECIGVEAFHENNVQLTEYVENATTLKGVEAKSHGLKAQYALGAYNELVLLHRYIYEHAKEENERKFAKRALEHIVNVEEYRELPIFIIKKFSSSVLSNNFLRELVLTTHHYMKLVERFVKTGALKKVTKKVKVRKATKKSKMSEEDVRSEFDGMSKKDLDRLWEESKGLVLQILKKEVPEMRGMNPIDSQLDVPVDAQQKFAKLSIQRSLRSRGFPAAVGLYHASRALWPESFKRGLTDFQDSPGEEDQLQELEQLLKADMKKVAKDLKKAESCKTCDEDPAYKKYDKMDATALQSLWEQSTDTLARILSHELPESESTSPVNWQLDITPDVQQKFAMLAIQRALRARDLPAAVGLYHTSRKLWPGDEAIFGAPGIGVEEEIAELKAILEADLHEVAREMKVAEDRAEDPDEEDPAEPYDSEQEEEEEVPAWKVEEIDFQFDSYVCKFSNVDVLKWYVFLLNDFSKNSTELNQALVKMLHRIAFDLKLPIKLYQVSLFQVFSKVNEHFTHLSKDLRKSSRLYELYQFGFHLLKKFFSKFTGDLAIEALFWKGPRECFEIENGYGSWVKSREADIRVWTEDLEIELRNLYEEYRTMETRDGIDVLDFIEHNLSRARSRKKVAKKLIEFGFDLLGAKWKNSDKARMDSVLPIGDIQKWYDEWKEAGARGDLVNVLQEKLNEDLGMEISRKKILKQLAHMDILYEKPKKEKPLPQWDTGLIEELKKLKEQYDDIPDALNMLGVNIVRYVMKRLSEKKPTRQVERHLESLGATIPERSKKSEKNGKKFDDFLNDDDDDSENDVGGGSEDDEEEEIVMKSKRIIPDSEDEEEHIEQEEAQKKLEKVAEKPNTLMGMIAGRKRKLAQLESDSSDESDDDDSAEKEEKKLPAAEDDSDLEEDAVIYKRSYVDALLTGGSIAGNGITETRRDTSEEREDDDDEDPFTKKLTFKRRIVMSDNEDEA
| null | null |
cell division [GO:0051301]; DNA repair [GO:0006281]; DNA replication checkpoint signaling [GO:0000076]; embryo development ending in birth or egg hatching [GO:0009792]; entrainment of circadian clock [GO:0009649]; meiotic cell cycle [GO:0051321]; meiotic sister chromatid cohesion [GO:0051177]; mitotic sister chromatid cohesion [GO:0007064]; regulation of sister chromatid cohesion [GO:0007063]; replication fork arrest [GO:0043111]
|
nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]
|
PF04821;
| null |
Timeless family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10550049, ECO:0000269|PubMed:12827206}.
| null | null | null | null | null |
FUNCTION: Plays an important role in chromosome cohesion during both mitosis and meiosis (PubMed:12827206). In prophase of meiosis, it is involved in the formation of the synaptonemal complex (SC) and specifically, in the diplotene and diakinesis phases of prophase, it stabilizes the association of homologous chromosomes during synapsis and sister chromatid cohesion (PubMed:12827206). It regulates cohesin subunits to promote meiotic chromosome cohesion and localizes non-SMC (structural maintenance of chromosome) cohesin subunits to chromatin prior to or during pre-meiotic S phase (PubMed:12827206). Implicated in influencing either the stability or loading of meiotic-specific cohesin subunit, rec8 (PubMed:12827206). Controls cell cycle exit and cell fusion to prevent the premature differentiation into adult cells (PubMed:15691769). Specifically, regulates hypodermal seam cell identity (PubMed:15691769). {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:15691769}.
|
Caenorhabditis elegans
|
G5EDN6
|
CANB_CAEEL
|
MGADASLPMEMCSNFDAYELRRLTRRFKKLDVDGSGSLSVEEFMSLPELQQNPLVQRVIDIFDEDGNGEVDFREFIQGISQFSVKGDKNTKLKFAFRIYDMDRDGFISNGELFQVLKMMVGNNLKDSQLQQIVDKTILFHDKDGDGKISFQEFCDVVEHTEVHKKMVLENI
| null | null |
calcineurin-mediated signaling [GO:0097720]; endocytosis [GO:0006897]
|
calcineurin complex [GO:0005955]; endoplasmic reticulum [GO:0005783]; sarcomere [GO:0030017]; striated muscle dense body [GO:0055120]
|
calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine phosphatase regulator activity [GO:0008597]; phosphatase binding [GO:0019902]
|
PF13499;
|
1.10.238.10;
|
Calcineurin regulatory subunit family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12221132}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of tax-6/calcineurin A, a calcium-dependent, calmodulin-stimulated protein phosphatase (PubMed:12221132). Confers calcium sensitivity (PubMed:12221132). Plays a role in egg-laying, fertility, growth, movement and cuticle development (PubMed:12221132, PubMed:12684004). Plays a role in sensitivity to CO2 levels (PubMed:18524955). Regulates expression of tax-6 inhibitor rcn-1 (PubMed:12684004). Negatively regulates nicotinic acetylcholine receptor (nAChR) sensitivity to nicotine (PubMed:15990870). Negatively regulates lifespan (PubMed:19279398). Involved in endocytic processes including coelomocyte endocytosis, intestine apical endocytosis and synaptic vesicle recycling (PubMed:20803083, PubMed:21345307). May negatively regulate autophagy (PubMed:19279398). {ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:12684004, ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:18524955, ECO:0000269|PubMed:19279398, ECO:0000269|PubMed:20803083, ECO:0000269|PubMed:21345307}.
|
Caenorhabditis elegans
|
G5EDP2
|
NLTP2_CAEEL
|
MTPTKPKVYIVGVGMTKFCKPGSVPGWDYPDMVKEAVTTALDDCKMKYSDIQQATVGYLFGGTCCGQRALYEVGLTGIPIFNVNNACASGSSGLFLGKQIIESGNSDVVLCAGFERMAPGSLENLAAPIDDRALSVDKHISVMSETYGLEPAPMTAQMFGNAAKEHMEKYGSKREHYAKIAYKNHLHSVHNPKSQFTKEFSLDQVINARKIYDFMGLLECSPTSDGAAAAVLVSEKFLEKNPRLKAQAVEIVGLKLGTDEPSVFAENSNIKMIGFDMIQKLAKQLWAETKLTPNDVQVIELHDCFAPNELITYEAIGLCPVGQGHHIVDRNDNTYGGKWVINPSGGLISKGHPIGATGVAQAVELSNQLRGKCGKRQVPNCKVAMQHNIGIGGAGVVGLYRLGFPGAAQSKI
|
2.3.1.176
| null |
acyl-CoA metabolic process [GO:0006637]; ascaroside biosynthetic process [GO:1904070]; dauer entry [GO:0043053]; dauer exit [GO:0043054]; lipid transport [GO:0006869]; negative regulation of lipid storage [GO:0010888]; olfactory learning [GO:0008355]; pheromone biosynthetic process [GO:0042811]; positive regulation of developmental growth [GO:0048639]; positive regulation of nematode larval development [GO:0061063]; regulation of chemotaxis [GO:0050920]; response to pheromone [GO:0019236]; very long-chain fatty acid metabolic process [GO:0000038]
|
peroxisome [GO:0005777]
|
acyltransferase activity [GO:0016746]; lipid binding [GO:0008289]; propanoyl-CoA C-acyltransferase activity [GO:0033814]; propionyl-CoA C2-trimethyltridecanoyltransferase activity [GO:0050632]
|
PF02803;PF00108;
|
3.40.47.10;
|
Thiolase-like superfamily, Thiolase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}. Note=Punctate localization in the cytoplasm. {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}.
|
CATALYTIC ACTIVITY: Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; Evidence={ECO:0000269|PubMed:9151950};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 uM for 3-ketooctanoyl-CoA (at 25 degrees Celsius) {ECO:0000269|PubMed:9151950}; KM=0.7 uM for CoA (at 25 degrees Celsius) {ECO:0000269|PubMed:9151950}; Vmax=0.1 mmol/min/mg enzyme {ECO:0000269|PubMed:9151950};
| null | null | null |
FUNCTION: Catalyzes the thiolytic cleavage of 3-ketoacyl-CoA with 8-16 carbon residues in the acyl group using a ping-pong mechanism whereby binding to 3-ketooctanoyl-CoA results in the release of acetyl-CoA and the subsequent addition of CoA produces 3-ketohexanohyl-CoA (PubMed:9151950). Involved in the biosynthesis of the dauer pheromone by providing short chains of fatty acid that are attached to the ascarylose sugars of the pheromone (PubMed:19174521, PubMed:19496754). {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754, ECO:0000269|PubMed:9151950}.
|
Caenorhabditis elegans
|
G5EDR3
|
2AB1_CAEEL
|
MVMEVDEPAVAATTSQNQPQEHANDFDMDTSEGPIENDETFEPVDQINWKFNQVKGNIDADVHTEADVISCVEFSHDGEYLATGDKGGRVVIFQRDQSGKYVKGVRSREYNVYSTFQSHEPEFDYLKSLEIDEKINQIRWLKKKNAANFILSTNDKTIKLWKISERERKIGDDAWNLPRTNRINTSSFRGRLQIPSIVPMELIVEASPRRVYGNAHTYHVNSISVNSDQETFLSADDLRVNLWNLEITNESFNIVDIKPANMEELTEVITAAEFHPTQCNWFVYSSSKGSIRLCDMRDRALCDAYAKIFEEPEDPQSRSFFSEIIASVSDVKFSHNGRYLLTRDYLTVKVWDLNMESQPVETYPVHNYLRTKLCALYENDSIFDKFECDWSGDDKHILTGSYHNLFRSYARGNNQDAKTWEARPQEPHSQLRSRFVVPSAKRKRNNLSSSGETTEEDLSSDQLQFDRKILHTAWHPKDNIIALAATNNLYIFSDV
| null | null |
centriole assembly [GO:0098534]; embryo development ending in birth or egg hatching [GO:0009792]; nematode larval development [GO:0002119]; positive regulation of vulval development [GO:0040026]; regulation of vulval development [GO:0040028]
|
cytosol [GO:0005829]; protein phosphatase type 2A complex [GO:0000159]
|
protein phosphatase regulator activity [GO:0019888]
|
PF00400;
|
2.130.10.10;
|
Phosphatase 2A regulatory subunit B family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21497766}.
| null | null | null | null | null |
FUNCTION: Probable regulatory subunit of serine/threonine phosphatase let-92. Together with let-92 and constant regulatory subunit paa-1, positively regulates centriole duplication during early embryonic cell divisions by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:21497766). In addition, during vulva development, may play a role with phosphatase let-92 and regulatory subunit paa-1 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation (PubMed:10521400, PubMed:14724126). In intestinal epithelial cells, may play a role in the late secretory pathway probably by regulating the exocyst, a protein complex involved in targeting secretory vesicles to the plasma membrane (PubMed:24192838). {ECO:0000269|PubMed:10521400, ECO:0000269|PubMed:14724126, ECO:0000269|PubMed:21497766, ECO:0000269|PubMed:24192838}.
|
Caenorhabditis elegans
|
G5EDR5
|
FUTA_CAEEL
|
MTARSIKLFFARWKYLMFACCITYLLVIYAPISKSEQKDWKEGEIELSNDHELDVPILQKEELKPQQRPSFEENVPKKKTFNFNPVGKEPFDVEEVLTSSDIKLEERMTATVIPGQKRLILSWNAGHSQDNLQGCPDWNCEFTQVRARAPDADAVLIAHMDNDFVPKPNQYVVYFSQESPANSGIQIPRPDYINMTLGFRHDTPAGSPYGYTVKLGAKSRKTGQVVDANLVNGKAKGAAWFVSHCQTNSKREDFVKKLQKHLQIDIYGGCGPMKCARGDSKCDTMLDTDYHFYVTFENSICEDYVTEKLWKSGYQNTIIPLVLKRKLVEPFVPPNSFIAIDDFKSVKEMGDYLNYLMNNKTAYMEYFEWRHDYKVVFLDGSHHDVLERPWGFCQVCRMAWTEPRQKVLIPNWDAYWRQTCEKDGTLVDSIPLD
|
2.4.1.214
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}; Note=Can also use Co(2+) or Ca(2+) in vitro. {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584};
|
carbohydrate biosynthetic process [GO:0016051]; fucosylation [GO:0036065]; protein glycosylation [GO:0006486]
|
Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]
|
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity [GO:0017060]; alpha-(1->3)-fucosyltransferase activity [GO:0046920]; fucosyltransferase activity [GO:0008417]; glycoprotein 3-alpha-L-fucosyltransferase activity [GO:0018392]; metal ion binding [GO:0046872]
|
PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
|
PTM: N-glycosylated (PubMed:17369288, PubMed:21515584). Glycosylation is important for enzymatic activity (PubMed:21515584). {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
|
CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc(1->3)]-beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:24444, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13529, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60651, ChEBI:CHEBI:137182; EC=2.4.1.214; Evidence={ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for GDP-fucose (at pH 7.5 and 23 degrees Celsius) {ECO:0000269|PubMed:21515584}; KM=400 uM for Man-alpha-1-6(Man-alpha-1-3)Man-alpha-1-6(Man-alpha-1-3)Man-beta-1-4GlcNAc-beta-1-4GlcNAc (at pH 7.5 and 23 degrees Celsius) {ECO:0000269|PubMed:21515584};
|
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:9675224}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. No detectable activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288};
|
FUNCTION: Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the first GlcNAc residue (with or without alpha 1,6-linked fucose), next to the peptide chains in N-glycans (PubMed:15364955, PubMed:17369288, PubMed:21515584, PubMed:9675224). Unlike in mammals, does not require the prior action of N-acetylglucosaminyltransferase I to generate complex N-glycans (PubMed:15364955). {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:21515584, ECO:0000269|PubMed:9675224}.
|
Caenorhabditis elegans
|
G5EDS1
|
VAB3_CAEEL
|
MSDAGHTGVNQLGGVFVNGRPLPDATRQRIVDLAHKGCRPCDISRLLQVSNGCVSKILCRYYESGTIRPRAIGGSKPRVATSDVVEKIEDYKRDQPSIFAWEIRDKLLADNICNNETIPSVSSINRVLRNLAAKKEQVTMQTELYDRIRIVDNFPYNSSWYGQWPIPMNGAVGLNPFVPAPLIEPKTEGEFEKDEDQKPPTEPEDDAAARMRLKRKLQRNRTSFTQVQIESLEKEFERTHYPDVFARERLAQKIQLPEARIQVWFSNRRAKWRREEKMRNKRSSGTMDSSLSNGTPTPTPGSVTGSNMTNPIGSPASTPNRFPSNNSANLPTTNFVPQTSQMYAGLSQPAMDPYSFGIANGFSMAPYPQVTDFQPHHMFQGRSPYDFPYPRMPTNGHGFQQSMSPATTAVGDIPTLSSGMSLPVSAVLNSIDPSLTHSQMHELSDLTQEHYWRPQ
| null | null |
anterior/posterior pattern specification [GO:0009952]; cell fate commitment [GO:0045165]; negative regulation of distal tip cell migration [GO:1903355]; nematode male tail mating organ morphogenesis [GO:0090597]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of glial cell differentiation [GO:0045687]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell adhesion [GO:0030155]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
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]
|
PF00046;PF00292;
|
1.10.10.60;1.10.10.10;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:7659159}.; SUBCELLULAR LOCATION: [Isoform b]: Nucleus {ECO:0000269|PubMed:7659160, ECO:0000269|PubMed:9858725}. Cytoplasm {ECO:0000269|PubMed:9858725}. Note=Nuclear localization is temporally and spatially regulated in two sets of neuronal sublineages. {ECO:0000269|PubMed:9858725}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds a motif with the core sequence 5'-GCGTA-3' in the promoter of various genes (PubMed:11476572, PubMed:30890567). During development, required for cell fate specification probably by promoting or repressing expression of genes involved in specific cell fate (PubMed:11476572, PubMed:30890567, PubMed:7649393). Involved in head epidermal morphogenesis (PubMed:7659159). Involved in gonadal distal tip cell (DTC) migration, during which modulates expression of the integrin alpha genes, pat-2 and ina-1 (PubMed:10388818, PubMed:15579687, PubMed:17606640). Regulates ventral and dorsal cephalic sheath (CEPsh) glia differentiation and expression of transcription factor hlh-17 in CEPsh glia (PubMed:18508862). Plays a role in establishing unequal cytokinesis and cell fate specification in male-specific postembryonic blast cell B (PubMed:7649393). May cooperate with the phosphatase eya-1 and transcription factor ceh-32 to regulate the transcription factor ets-5 (PubMed:30890567). {ECO:0000269|PubMed:10388818, ECO:0000269|PubMed:11476572, ECO:0000269|PubMed:15579687, ECO:0000269|PubMed:17606640, ECO:0000269|PubMed:18508862, ECO:0000269|PubMed:30890567, ECO:0000269|PubMed:7649393, ECO:0000269|PubMed:7659159}.; FUNCTION: [Isoform a]: Transcription factor involved in head epidermal morphogenesis and required for normal cell fate in anterior lateral epidermal blast (seam) cells (PubMed:15579687, PubMed:7659159). Required for the generation or differentiation of neurons of the anterior ganglion, probably acting upstream of unc-86 (PubMed:8647436). Represses BAG sensory neuron fate in non-BAG cells, probably through cooperation with the phosphatase eya-1 and transcription factor ceh-32 (PubMed:30890567). May be involved in regulating the generation of dopaminergic neurons (PubMed:21079745). May cooperate with hlh-17 to preferentially regulate expression of hlh-17 in ventral CEPsh glia (PubMed:18508862). {ECO:0000269|PubMed:15579687, ECO:0000269|PubMed:18508862, ECO:0000269|PubMed:21079745, ECO:0000269|PubMed:30890567, ECO:0000269|PubMed:7659159, ECO:0000269|PubMed:8647436}.; FUNCTION: [Isoform b]: Transcription factor that acts within the male-specific genital sensilla (simple sense organs) known as rays to determine their identity (PubMed:15579687, PubMed:1782863, PubMed:7659160). Promotes BAG sensory neuron fate in a cell-autonomous manner (PubMed:30890567). Required for function of chemosensory BAG neurons (PubMed:30890567). {ECO:0000269|PubMed:15579687, ECO:0000269|PubMed:1782863, ECO:0000269|PubMed:30890567, ECO:0000269|PubMed:7659160}.
|
Caenorhabditis elegans
|
G5EDT1
|
LIN35_CAEEL
|
MPKRAADEPGTSTTDPFHEQSPFDAVLAGTETTDTICEEPPAKRIDLDIKQEFNGGVQSGGLIKNESELTQMTIKQETEGNINEARREEEDEEQDEDSRTSMPPALGEDDDYEEDDADSFIDKTNTPPPSQSFLEGCRAANLPNDIVTGAWETYNHAVQRVSLEGSESAWQLSAIYYYLLSKGIKRRGKTIRILIQPFPVSILTIANSFDISVAEMLDKTARFVEIIHSRKIRRYQEYIRRIQEGLAVSCVIFKKFCRIFCKIFEEIKVGSENCPSSHELFTVLWTSFLVMKSRMTVDDLISNYQLLFSILDQVYTEMCSMKEGIVHHLNQKFVEDLLENDCTIIRALCTQFGGSVLDARHFSDHTFKKMEKTGIPSTWNFQEFRDLIMNVPKTAYENYLLQRGSIDERIFIPSVEDFSKIFQSPDTYSVADILKVSYSGRRFRDAEFLTKISNNHCLEKLALGGKVASEKLVTQSKEQPRVPCVEYNLELGNYPDDLESNNQSLYNRLTKIIGSWKLENSKLEEVCGTMSDSPMATILLKSDEMTNKFERTLSAELGETINENIPKYHYNVRKELELVFLIFMEKIIVAELKKKVREEDLLNVIRREEFLDSVFCFCVELILVSNGYDRPFPWSAELCGVHPFMFHKVIDLMITHEKQLSRQMVQHFSRIEETVIEYFSWKSDSPLWPMVVRCPFAHFQEFGEDWADKLNSYSPIKFTPIKKPDDLRDELGRPIVPQNQTSRTLRIFLKRTYFTAARRLQDLTDRVSMGARAKSQCWSLFDYLLRNDTLIFMDRHLDQILLCCVFVIMKINESSMLFTEIMAQYRRQSANSLLVYRSVTVFQEQLNPENPQAVNTKETILERLEGPQKEKTTVDIIKYYNIEFRDRIKYIIGQIDSASDEDLMEMPVATESGLMPVRVYLTHKLSIQTLPKTKHGESKQERAIANLEKSGITIAMERSGD
| null | null |
cell cycle [GO:0007049]; cell differentiation [GO:0030154]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; gonad development [GO:0008406]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of DNA endoreduplication [GO:0032876]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of transcription by RNA polymerase I [GO:0016479]; negative regulation of vulval development [GO:0040027]; nematode larval development [GO:0002119]; positive regulation of brood size [GO:0090727]; positive regulation of multicellular organism growth [GO:0040018]; regulation of cell cycle G1/S phase transition [GO:1902806]; regulation of cell division [GO:0051302]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; reproduction [GO:0000003]
|
chromatin [GO:0000785]; DRM complex [GO:0070176]; nucleus [GO:0005634]; Rb-E2F complex [GO:0035189]; transcription regulator complex [GO:0005667]
|
RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF11934;PF01858;PF01857;
|
1.10.472.140;1.10.472.10;
|
Retinoblastoma protein (RB) family
|
PTM: Phosphorylated by the cyclin dependent kinase cdk-4. Phosphorylation inhibits the transcriptional repressor activity of lin-35 and allows for progression through the G1 phase of the cell cycle during postembryonic development. {ECO:0000269|PubMed:25562820}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621535, ECO:0000269|PubMed:23347407, ECO:0000269|PubMed:25562820, ECO:0000269|PubMed:9875852}. Note=Expressed in dividing cells, but decreased expression after cell cycle exit. {ECO:0000269|PubMed:25562820}.
| null | null | null | null | null |
FUNCTION: Key regulator of cell division which acts as a transcriptional repressor and negatively regulates cell cycle progression in its active unphosphorylated form, but allows cell cycle progression when phosphorylated (PubMed:11684669, PubMed:12062054, PubMed:16287966, PubMed:17466069, PubMed:25562820). When unphosphorylated and in its active form, interacts with E2F transcription factors such as efl-1 to repress their transcriptional activity and negatively regulate the progression through the G1 phase of the cell cycle during postembryonic development (PubMed:11684669, PubMed:12062054, PubMed:15238519, PubMed:17466069, PubMed:25562820). May furthermore act with cell cycle regulator cki-1 to negatively regulate cell cycle progression (PubMed:11684669). Acts redundantly with lin-53, fzr-1 and lin-23 to control cell cycle progression by regulating the expression of G1 phase cyclins (PubMed:11850412, PubMed:25562820). In particular, negatively regulates the expression of the cyclin E homolog cye-1, which is essential for the G1/S phase transition (PubMed:16287966, PubMed:17466069). Regulates cell division in the intestinal lineage, repressing the expression of genes such as cdc-25.2, which are required for intestinal cells to transition from the karyokinesis cell cycle (also known as nuclear division) to endoreplication, a specific growth pathway in the intestinal epithelium required for feeding and gut development in growing larvae during the L1 stage molt (PubMed:17466069, PubMed:27104746). Its role as a transcriptional repressor in the regulation of intestinal cell division during postembryonic development is most likely in complex with an E2F cell cycle regulatory transcription factor efl-1 and its binding partner the synthetic multivulva class B protein dpl-1 (PubMed:17466069). Synthetic multivulva (synMuv) class B protein (PubMed:11850412, PubMed:9875852). SynMuv proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription (PubMed:17075059, PubMed:9875852). Together with synMuv class B protein lin-53, and redundantly with synMuv class A protein lin-15A, represses transcription to control vulval development, most likely through antagonization of the Ras-signaling pathway in the major hypodermal syncytium hyp7 (PubMed:15621535, PubMed:16624904, PubMed:26100681, PubMed:9875852). Acts redundantly with the transcriptional corepressor spr-1 and the zinc finger protein zfp-2 to play a role in vulval morphogenesis, promote germline proliferation and somatic gonad development (PubMed:17070797, PubMed:17417969). Acts redundantly with ubc-18 in the regulation of pharyngeal morphogenesis during embryonic develpment by negatively regulating the expression of proteins such as sup-35 (PubMed:12783801, PubMed:19521497, PubMed:24214340). Functions with the SWI/SNF complex and proteins such as pha-1 to regulate larval development (PubMed:15196946, PubMed:15280233). Functions redundantly with xnp-1 to regulate somatic gonad development (PubMed:15328017, PubMed:15649460). Acts redundantly with slr-2 to regulate the expression of intestinal genes required for nutrient utilization (PubMed:18437219, PubMed:22542970). Regulates transcription in response to starvation (PubMed:23664972). Furthermore, in response to starvation, promotes germ cell programmed cell death by negatively regulating the expression of the anti-apoptotic protein ced-9 (PubMed:17881492, PubMed:24752899). Conversely, in conjunction with mcd-1, efl-1 and the synthetic multivulva class B proteins dpl-1, lin-37 and lin-52, may also regulate transcription to promote programmed cell death independently of ced-1, ced-8 and ced-9 cell death pathways (PubMed:17237514). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation (PubMed:23347407). In particular, negatively regulates the expression of mes-4, a histone methyltransferase that controls the expression of germline specific genes (PubMed:23347407). May play a role in double strand break formation during meiosis (PubMed:15315757). May suppress sensitivity to RNAi (PubMed:16507136, PubMed:17417969). May play a role in the response to endoplasmic reticulum (ER) stress (PubMed:24715729). {ECO:0000269|PubMed:11684669, ECO:0000269|PubMed:11850412, ECO:0000269|PubMed:12062054, ECO:0000269|PubMed:12783801, ECO:0000269|PubMed:15196946, ECO:0000269|PubMed:15280233, ECO:0000269|PubMed:15328017, ECO:0000269|PubMed:15621535, ECO:0000269|PubMed:15649460, ECO:0000269|PubMed:16287966, ECO:0000269|PubMed:16624904, ECO:0000269|PubMed:17070797, ECO:0000269|PubMed:17075059, ECO:0000269|PubMed:17237514, ECO:0000269|PubMed:17417969, ECO:0000269|PubMed:17466069, ECO:0000269|PubMed:17881492, ECO:0000269|PubMed:18437219, ECO:0000269|PubMed:19521497, ECO:0000269|PubMed:22542970, ECO:0000269|PubMed:23347407, ECO:0000269|PubMed:23664972, ECO:0000269|PubMed:24214340, ECO:0000269|PubMed:24752899, ECO:0000269|PubMed:25562820, ECO:0000269|PubMed:26100681, ECO:0000269|PubMed:27104746, ECO:0000269|PubMed:9875852, ECO:0000305|PubMed:15315757, ECO:0000305|PubMed:16507136, ECO:0000305|PubMed:24715729}.
|
Caenorhabditis elegans
|
G5EDT6
|
JKK1_CAEEL
|
MENVCFQQRLRDLETRVRKWKFLKLGLTEVRLRPRDRRSTSVDQKHKECSSTSSSPQHQRPNNIGYLTSPMERKFTPLSMKPSPSRRDTEKDALEYEFLEGYKKSGTLEIDGEKQVVDPNEIHIISLLGSGSCGVVESATVRSKLMAVKTMYKNDNKENLKRILRDVRIMSMCNSPFIVTSYGYFMFDSSVKICMQIMSACCEKLLRRIYHSKLDFFPEFVAGHIVYSAISALDYLKEKHSIIHRDIKPSNILFDDSGNVKLCDFGISGFMTDSMAHSKSAGCPPYMAPERLTIETNSKYDVRSDVWSLGITVYQLVTGLYPFPLNDMEFTTLTIIANLNLPSPSLREETKRSFSPLFIEFLDLCLRKDVRERPEYRQLMKHDFYLDYDPASGSAYKFKAINGKCNQVADWFVDVIRLSKTEDELKSIPNTPCVN
|
2.7.12.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O14733};
|
hyperosmotic response [GO:0006972]; locomotion [GO:0040011]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]
|
ATP binding [GO:0005524]; exonuclease activity [GO:0004527]; JUN kinase kinase activity [GO:0008545]; MAP kinase kinase activity [GO:0004708]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10393177}. Perikaryon {ECO:0000269|PubMed:10393177}. Cell projection, axon {ECO:0000269|PubMed:10393177}.
|
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=2.7.12.2; Evidence={ECO:0000269|PubMed:10393177}; 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=2.7.12.2; Evidence={ECO:0000269|PubMed:10393177}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000269|PubMed:10393177};
| null | null | null | null |
FUNCTION: Dual specificity protein kinase which acts as an essential component of the JNK signal transduction pathway. May phosphorylate jnk-1 (PubMed:10393177, PubMed:15767565, PubMed:17894411). Plays a role in coordinating locomotion via D-type GABAergic motoneurons and in regulating synaptic vesicle transport downstream of adapter protein unc-16 and probably by activating jnk-1 (PubMed:10393177, PubMed:11738026). Positively regulates lifespan (PubMed:15767565). Upon environmental stress such as heat stress regulates daf-16 nuclear translocation probably by activating jnk-1 (PubMed:15767565). Regulates germline cell apoptosis in response to heavy metals such as Cu(2+) and to arsenite (PubMed:18597494, PubMed:19497412). {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026, ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:18597494, ECO:0000269|PubMed:19497412}.
|
Caenorhabditis elegans
|
G5EDU6
|
OVOLH_CAEEL
|
MDSRVWLPLIGAHLLPRDISVITQMIANNNNTSISRSSTNSSKPEEKNSKKFLIERFLDDDPSPPASILSPSPKAAIPSPIINPAVEFVNGGYGVKNPLAPLISSFETTSIPCSTVSPSSLISSSKDEFQDSLTCHICGKKFGLQRLLNRHIKCHSDLKRYLCTFCGKGFNDTFDLKRHTRTHTGVRPYKCEQCEKSFTQRCSLESHLRKVHGVTHQYAYKERRSKVFVCEDCGYTDEKFEVYLSHIKVVHPFSAAYLRFTQLQKKNSSMKPEQLSKISL
| null | null |
animal organ morphogenesis [GO:0009887]; epidermal cell differentiation [GO:0009913]; hindgut morphogenesis [GO:0007442]; nematode male tail tip morphogenesis [GO:0045138]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to salt stress [GO:0009651]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;
|
3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11532910}.
| null | null | null | null | null |
FUNCTION: Transcription factor (By similarity). Involved in development of the hindgut, the male tail, and the excretory duct cell (PubMed:10511553, PubMed:11532910, PubMed:12231624). Involved in modulating function of excretory duct cells (PubMed:14758362). Plays a role in left/right patterning of cell fates in the hindgut (PubMed:10511553, PubMed:11532910). {ECO:0000250|UniProtKB:Q9BRP0, ECO:0000269|PubMed:10511553, ECO:0000269|PubMed:11532910, ECO:0000269|PubMed:12231624, ECO:0000269|PubMed:14758362}.
|
Caenorhabditis elegans
|
G5EDW2
|
LPLT1_CAEEL
|
MRRNKTTYSLLQTILVACLLTVTPTFASNKPTTDESGTISHTICDGEAAELSCPAGKVISIVLGNYGRFSVAVCLPDNDIVPSNINCQNHKTKSILEKKCNGDSMCYFTVDKKTFTEDPCPNTPKYLEVKYNCVVPATTTTTTTTTSTTTTDSSLIVDEEEEAQKDALNSDVIKPVKKKEDVFCSATNRRGVNWQNTKSGTTSSAPCPEGSSGKQLWACTEEGQWLTEFPNSAGCESNWISSRNSVLSGVISSEDVSGLPEFLRNLGSETRRPMVGGDLPKVLHLLEKTVNVIAEESWAYQHLPLSNKGAVEVMNYMLRNQEIWGSWDVTKRKEFASRFILAAEKAMVASAKGMMTSAESNVIVQPAITVEISHKIKMSSQPTDYILFPSAALWNGQNVDNVNIPRDAILKINKDETQVFFSSFDNLGAQMTPSDVTVAIAGTDQTEVRKRRVVSRIVGASLIENGKERRVENLTQPVRITFYHKESSVRHLSNPTCVWWNHHELKWKPSGCKLSYHNKTMTSCDCTHLTHFAVLMDVRGHDLNEIDQTLLTLLTYVGCIISIICLLLTFFAYLIFSRNGGDRVFIHENLCLSLAIAEITFLAGITRTEDSLQCGIIAVALMYMFLSALTWMLLEGYHIHRMLTEVFPSDPRRFTYLLVGYIPPAIITLVAYLYNSDGFGTPDHCWLSTQNNFIWFFAGPACFIFCANSLVLVKTLCTVYQHTSGGYLPCRHDVDSGRSIRNWVKGSLALASLLGVTWIFGLFWVEDSRSIVMAYVFTISNSLQGLFIFLFHVVFAEKMRKDVGHWMYRRGCGGSSNSSPNHKRHNVQRDLMSPGVNSSTGSDFLYNTNDKYLTNSDTTNRLVYNGIMNHPNQMSVYQQHPHHQIYEQQPGTYDYATIAYGDMMPGHRVAAPPAYQRLAVAEGRYGSQHQLYQGWHHRPPPEFSPPPPPLSTGPPNSRHYGTGSSGRRPPSSKMSDDSAYSDGSSSMLTTEVTPQGQTVLRIDLNKPSMYCQDL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; anterior/posterior pattern specification [GO:0009952]; cell surface receptor signaling pathway [GO:0007166]; embryo development ending in birth or egg hatching [GO:0009792]; self proteolysis [GO:0097264]; sexual reproduction [GO:0019953]
|
plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; endopeptidase activity [GO:0004175]; G protein-coupled receptor activity [GO:0004930]; transmembrane signaling receptor activity [GO:0004888]
|
PF00002;PF16489;PF02140;PF01825;PF02793;
|
2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, LN-TM7 subfamily
|
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19853563}; Multi-pass membrane protein {ECO:0000269|PubMed:19853563}.
| null | null | null | null | null |
FUNCTION: Has a role in the establishment of anterior-posterior polarity in tissues during embryogenesis. Required for the alignment of the mitotic spindles and division planes. May have a role in cell death events. Required for normal defection and oocyte fertilization. Involved in sperm function. Operates in pharyngeal pumping during feeding. {ECO:0000269|PubMed:14594448, ECO:0000269|PubMed:15296755, ECO:0000269|PubMed:17583712, ECO:0000269|PubMed:19853563, ECO:0000269|PubMed:22938866}.
|
Caenorhabditis elegans
|
G5EDW5
|
ADM2_CAEEL
|
MTDTLDLKLSSRRQWNPVRCPVRLEVDGSAQTPTSLVQTALNNPSFDLVIAAPNGQNVYIPFTEDRKLFTANIADDPSTSSLISHCHFEGVTEDGRHALSLCDPGEITGLLMTQTNRFGLSTSNNGSFVLIPYVENNCDLGSLVHSSSRKKRQIGKQNTVIDRNPSYIREHLDGRKRFVELALVADYSVYTKYDSDEKKVNDYMQQTMNILNSLYFPLNIRITLVHSEIWKKGDQISVIPDSKETLNNFMEYKKIMLKDHFFDTGYLMTTLKFDEGVVGKAYKGTMCSYDYSGGIYVDHNNDTVETVATFAHELGHTFGMDHDPNDKDVCYCPMPRCIMNPQSGHMEVWSECSVKNLASGFNRGIDLCLFNEPGKKPSDAKCGNGIVEPGEECDCGPLKCDNHCCNGSTCKLIGEAECASGDCCDLKTCKPKPRATVCRAAIGICDLDEYCNGETNDCPADFFVQNAALCPGKENEFCYEGGCGSRNDQCAKLWGPTGKNGDENCYRKNTEGTFHGNCGTNAHTKEIKKCETENAKCGLLQCETQAERPVFGDPGSVTFSHSTVYSSLKRDDKKFCYVFKSAYGGLNAPDPGLVPDGAICGEEQMCIGQKCHKKEKISKVTAQCLDNCNFRGVCNNVGNCHCERGFGGIACEIPGYGGSVNSNEAYRFRGITLSSTFLVFFCLFGIFIGGLCVYYRVKRKRNLVSEWWSVVKKKFDLHGDLVPVRKAPPPPYAQRIRQSFTAMWGEDHSHVAVAQPAHPRNCYNSCCRQPPRFDPPSIPMVTLKNPNLASPTPLLNPAEKEEQNQERATHQHVELYPVAESFRSDSAASFNTRTGSFRPNVQPPPVPRPSDDVLSKLNEDLAKEKNAKFDRLNKTLPLPPPLPKEKPKTASSTSLRRNESIRPEQAPPPPPPAHAKPTLPTKQPKVSEDAAATEEKVDVRSMAAIFDQKLKK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9BZ11}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9BZ11};
|
membrane protein ectodomain proteolysis [GO:0006509]
|
endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF08516;PF00200;PF01421;
|
3.40.390.10;4.10.70.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35639786}; Single-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:35639786}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:35639786}; Single-pass membrane protein {ECO:0000255}. Note=Localization and lysosomal targeting is influenced by components of the nekl-2/mlt-2/mlt-4 and nekl-3/mlt-3 complexes. {ECO:0000269|PubMed:35639786}.
| null | null | null | null | null |
FUNCTION: Metalloprotease that cleaves and releases a number of molecules (By similarity). Negative regulator of lrp-1 protein levels, potentially by influencing its endosomal trafficking (PubMed:35639786). Involved in regulating the molting process (PubMed:35639786). {ECO:0000250|UniProtKB:Q61072, ECO:0000269|PubMed:35639786}.
|
Caenorhabditis elegans
|
G5EDW7
|
LIN8_CAEEL
|
MSKIKTHSTGSKRTVPFYKLPPPVPLPPLPPPDPTRYFSTEKYIALSKDEKFKFDDYDVNDETLKKVVLNEIGKCPDIWSSRSQAAIMEHYPIVATETYRRTGLLLSIKSLKQIYKCGKDNLRNRLRVAIVSKRLTPAQVEAYMWRWEFYGFIRYYRDYTQRWEADLLKDLDVVLGLEARRASKNMEKVDSGELMEPMEPMDSTMDEMCVEEEPYEETGSNWSDPAPEPSQSKSQSPEAKYPQAYLLPEADEVYNPDDFYQEEHESASNAMYRIAFSQQYGGGGSPAVQKPVTFSAQPAPAPVREAPSPVVENVSSSSFTPKPPAMINNFGEEMNQITYQAIRIAREQPERLKLLRKALFDVVLAFDQKEYADVGDLYRDLAQKNS
| null | null |
negative regulation of vulval development [GO:0040027]
|
nucleus [GO:0005634]
| null |
PF03353;
| null |
Lin-8 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16020796}.
| null | null | null | null | null |
FUNCTION: Acts as a synthetic multivulva class A (synMuvA) protein and redundantly inhibits lin-3/EGF expression to prevent inappropriate vulva induction. {ECO:0000269|PubMed:16020796, ECO:0000269|PubMed:16678779}.
|
Caenorhabditis elegans
|
G5EDY0
|
PIKI1_CAEEL
|
MSDDEELQLAIEISKKTFKDEQKLRSNDLDLIRFESPDEPARQRKINQIKQLYEANSPGPSSYSGSLATSPIDFRPVYNEPRAGPIPHSQSYPRNYFQDWSAIASTSQPPAFPPPPRPPKPEQYKFPPAPSVPLLHDRYFVPPPPPVPPRHSRVQQSPPVPIHPTPPVSSTPLRHSAPSFASDSQQFLSPIKPFEISFNSTVDTSSNQTGSHDHSIQYQPLTHLYVPYVMHSLNSSYGALLNGDLIDLSAFEDSSNASQDEIRKEFDPLFISTYSTDTPSPDNSMPAVNAYFSKPIDEPECVGGAKLIQENIEFPSSSFCLIDCPNGIEEQVKKLCKRNLIRKDMTPDFFIAPTVDYMVTTASTVKVVVYKDHSWKANKSNGKAMICAIDEKMDIITTQALSLFDSELPTDKEYGLKIYGLNQFLSSDSLLGSNLYTGHCLLNGDDVKLDLGVFAPNSRIYEQTLESWNLMKSQVKYSTVVDKEDVENTLGHLASEMSQYEIAFNDGSTLKLSSSSQRVKQVIMLLCKCLHGIVPEKLYNEMQKYLASTTEDQLVHHRNDFLREIHSFLELYCRCTVSRYNIPPLQIITKPKVEVLSKMDFLQIMLNSVHSIPEHWQSQYSEFYMSLDLYHGTQVLDGFSNKVPKTIKNDHFFPRIPLDLYAKFKRLNLCQYPRETRIVVSISGTVRNSAQAANEYNPDIVMLGYCSVPLYDENLFMRQGPLFLPLTLLKKQPMLKPFGPYPYIKDARDPILIMSFKIWDTEIYFPNVVIDMQCIPQDFATLDIETQEYLLELIENQDTSTLETDDQDLIWQKRLHLTNQPEALPLVLSSLQDWSFGFVMRVYQILEEWAPLRPEIAMEFLLPKYPDERIRAHAVQSLARGSTDFLYHTIPQFIEALRFELYEKSALADFILELSFVSLDFTFEIYWQLQQRVDHCAVDDLPYAIRCQNLQQKMIDEHENPNLKTDIKLQHELLNELDSIQDDLRSKSGDSEIERLHRLRTRLGILDSKLLQNKVRLPICPAFDCTGVRIEECSVFNSNAKPLKIVFRGLNMNYSIIHKRDDDMRQDAFVMKMLNEMDRIWKSNGLDLRMITFRIMPVGYRRGMGELVLNCATLMEIQKEEGLRGVLNDEILRKWLMKHNSDEFAYKEAQENFIRSCAGWCIVTYVLGIGDRHNDNILFTKNGHVFHIDFGKYMGDWQMAAGFRRDRVPFVFTTEMFHVINNGRAPTQYNQKFIDYCCKAFNHLRRNKNTLTNLLRIMACSDIPGINMDSLAFVENNLMLDLSDTDATVQFTAMIQNSLGSAFVRLNFVAHTVAQFISSRPSFSKQDPNKLSFVPELYTENSDGRISRVTVLKFEKHCIPNKIYMYKVEVHRKNVAVSSFIYRSFAEFEELHTKLRARFPMMAVSLNTISNLRSNVRAVAQKRIIHVQKFLIYLFNQVDEICHCDLVYTFFHSILRDNKCDTYIDESLDMPSQCQIYLKIEYNSVKETLSVFIGHAKYLALLQNNQQPDPYVKTYVRPDLRNQSKQKTQVVRGTRHPTFNQDLNYTEFPIEILSTRVLEVSIWNNGGYLVKHKMYMLCIPLLKVKKLAESRKNCRTLEGWFNCEKCV
|
2.7.1.137
| null |
autophagosome assembly [GO:0000045]; nematode larval development [GO:0002119]; phagosome maturation involved in apoptotic cell clearance [GO:0090386]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of phagocytosis, engulfment [GO:0060100]
|
cytoplasm [GO:0005737]; early phagosome [GO:0032009]; endosome [GO:0005768]; peroxisome [GO:0005777]; phagocytic cup [GO:0001891]; phagocytic vesicle membrane [GO:0030670]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; phosphatidylinositol binding [GO:0035091]
|
PF00168;PF00454;PF00613;PF00787;
|
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
|
PI3/PI4-kinase family
| null |
SUBCELLULAR LOCATION: Cell projection, phagocytic cup {ECO:0000269|PubMed:22272187}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:22272187}; Peripheral membrane protein {ECO:0000269|PubMed:22272187}. Cytoplasm {ECO:0000269|PubMed:22272187}. Note=Localizes transiently to pseudopods and nascent phagosomes during cell corpse engulfment. {ECO:0000269|PubMed:22272187}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000305|PubMed:22272187};
| null | null | null | null |
FUNCTION: Phosphatidylinositol 3-kinase involved in clearance of apoptotic cell corpses by phagosomes. Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab-5, rab-2 and rab-7. The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse. Unlike vps-34, not involved in the formation of PI3P in early endosomes. {ECO:0000269|PubMed:22272187}.
|
Caenorhabditis elegans
|
G5EDZ2
|
UMPS_CAEEL
|
MSSLTDKTRNGALKRNLLRQMLKASVFKFGEFQLKSGQISPIYIDLRECFGHPGLLMLISEAISKQVEISEVQYAGVLGIPYAALPYASVAAGNYLKKPLLIVRKEAKSYGTKKLIEGLYQPNDRLILIEDVVTTGGSILDVVKVLHTENLVASDVFCILDREQGGRQKLQDAGVTLHSLLDMQTVLTFLYSTGAIGDEQWHGIVQALNLPYTSPTKLEINSELENLSSLPYVENVRTPLAERESLTESALIKKILGIMRRKKSNLCLAVDYTTVEQCLQMIELAGPFVLAIKLHADAITDFNEEFTRKLTTMANDMDFIIFEDRKFGDTGNTNLLQLTGAQKIANWADVVTVHAVQGSDSIAGVFRKLAKDPTYRLSGVLLIAQLSTKGSLTALEGYTETAVKIANENRDVISGFITQTRVSACSDLLNWTPGVNLDAKSDSAGQQWRGVDEAIEVQQNDIIIVGRGVTSSSEPVQQLKRYRQIAWDALTRSDDSI
|
2.4.2.10; 4.1.1.23
| null |
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; determination of adult lifespan [GO:0008340]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; lysosome organization [GO:0007040]; nematode larval development [GO:0002119]; positive regulation of brood size [GO:0090727]; positive regulation of multicellular organism growth [GO:0040018]; pyrimidine nucleobase biosynthetic process [GO:0019856]; reproduction [GO:0000003]; response to gamma radiation [GO:0010332]; response to organic cyclic compound [GO:0014070]; response to UV [GO:0009411]; response to UV-C [GO:0010225]; response to X-ray [GO:0010165]; UMP biosynthetic process [GO:0006222]
|
cytoplasm [GO:0005737]
|
orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590]
|
PF00215;
|
3.40.50.2020;3.20.20.70;
|
Purine/pyrimidine phosphoribosyltransferase family; OMP decarboxylase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20148972}. Note=Localizes near the apical surface of the embryonic intestine. Appears not to localize to gut granules. {ECO:0000269|PubMed:20148972}.
|
CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000269|PubMed:19645718}; CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000269|PubMed:19645718};
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. {ECO:0000269|PubMed:19645718}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. {ECO:0000269|PubMed:19645718}.
| null | null |
FUNCTION: Bifunctional enzyme which catalyzes the formation of UMP from orotate in the de novo pathway of pyrimidine biosynthesis (PubMed:19645718). May also form UMP from uracil (PubMed:19645718). Regulates the size of gut granules during embryonic development (PubMed:20148972). Involved in resistance to DNA damaging agents including UV-C and X-ray radiation (PubMed:24262006). {ECO:0000269|PubMed:19645718, ECO:0000269|PubMed:20148972, ECO:0000269|PubMed:24262006}.
|
Caenorhabditis elegans
|
G5EE01
|
PTEN_CAEEL
|
MVTPPPDVPSTSTRSMARDLQENPNRQPGEPRVSEPYHNSIVERIRHIFRTAVSSNRCRTEYQNIDLDCAYITDRIIAIGYPATGIEANFRNSKVQTQQFLTRRHGKGNVKVFNLRGGYYYDADNFDGNVICFDMTDHHPPSLELMAPFCREAKEWLEADDKHVIAVHCKAGKGRTGVMICALLIYINFYPSPRQILDYYSIIRTKNNKGVTIPSQRRYIYYYHKLRERELNYLPLRMQLIGVYVERPPKTWGGGSKIKVEVGNGSTILFKPDPLIISKSNHQRERATWLNNCDTPNEFDTGEQKYHGFVSKRAYCFMVPEDAPVFVEGDVRIDIREIGFLKKFSDGKIGHVWFNTMFACDGGLNGGHFEYVDKTQPYIGDDTSIGRKNGMRRNETPMRKIDPETGNEFESPWQIVNPPGLEKHITEEQAMENYTNYGMIPPRYTISKILHEKHEKGIVKDDYNDRKLPMGDKSYTESGKSGDIRGVGGPFEIPYKAEEHVLTFPVYEMDRALKSKDLNNGMKLHVVLRCVDTRDSKMMEKSEVFGNLAFHNESTRRLQALTQMNPKWRPEPCAFGSKGAEMHYPPSVRYSSNDGKYNGACSENLVSDFFEHRNIAVLNRYCRYFYKQRSTSRSRYPRKFRYCPLIKKHFYIPADTDDVDENGQPFFHSPEHYIKEQEKIDAEKAAKGIENTGPSTSGSSAPGTIKKTEASQSDKVKPATEDELPPARLPDNVRRFPVVGVDFENPEEESCEHKTVESIAGFEPLEHLFHESYHPNTAGNMLRQDYHTDSEVKIAEQEAKAFVDQLLNGQGVLQEFMKQFKVPSDNSFADYVTGQAEVFKAQIALLEQSEDFQRVQANAEEVDLEHTLGEAFERFGHVVEESNGSSKNPKALKTREQMVKETGKDTQKTRNHVLLHLEANHRVQIERRETCPELHPEDKIPRIAHFSENSFSDSNFDQAIYL
|
3.1.3.16; 3.1.3.48; 3.1.3.67
| null |
cell motility [GO:0048870]; chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; dauer larval development [GO:0040024]; dephosphorylation [GO:0016311]; determination of adult lifespan [GO:0008340]; learning or memory [GO:0007611]; negative regulation of cell population proliferation [GO:0008285]; phosphatidylinositol dephosphorylation [GO:0046856]; positive regulation of dauer larval development [GO:0061066]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of positive chemotaxis [GO:0050927]; protein import into nucleus [GO:0006606]; regulation of chemotaxis [GO:0050920]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; response to heat [GO:0009408]; response to salt [GO:1902074]
|
axon [GO:0030424]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein phosphatase inhibitor complex [GO:0062049]
|
lipid binding [GO:0008289]; myosin phosphatase activity [GO:0017018]; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [GO:0016314]; protein tyrosine phosphatase activity [GO:0004725]
|
PF10409;PF00102;
|
2.60.40.1110;3.90.190.10;
|
PTEN phosphatase protein family
|
PTM: Phosphorylated by vab-1 on tyrosine residues which may promote daf-18 degradation. {ECO:0000269|PubMed:19853560}.
|
SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:22069193}. Cell membrane {ECO:0000269|PubMed:22916028}; Peripheral membrane protein {ECO:0000269|PubMed:22916028}. Cell projection, axon {ECO:0000269|PubMed:22069193}. Cell projection, dendrite {ECO:0000269|PubMed:22069193}. Cytoplasm {ECO:0000269|PubMed:22916028}. Nucleus {ECO:0000269|PubMed:22916028}. Note=During vulva development, localizes to the cytoplasm and the nucleus of vulva precursor cells and of vulva cells at the Pn.p stage of L2 larvae. From the Pn.px to Pn.pxx stage of L3/L4 larvae, localization increases at the plasma membrane and becomes maximal at the Pn.pxxx stage of L4 larvae. {ECO:0000269|PubMed:22916028}.
|
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-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000305|PubMed:15637588}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:19853560}; 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-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484}; 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-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484};
| null | null | null | null |
FUNCTION: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins (By similarity). Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate (PubMed:15637588). By dephosphorylating PtdIns(3,4,5)P3 antagonizes PtdIns(3,4,5)P3 production by age-1/PI3K and thus, negatively regulates daf-2-mediated processes including dauer formation, longevity, fat metabolism, chemotaxis towards salt, thermotolerance and axon guidance (PubMed:10077613, PubMed:10209098, PubMed:10377431, PubMed:16950159, PubMed:19249087, PubMed:20207731, PubMed:22916022, PubMed:23995781, PubMed:9885576). Similarly, promotes apoptosis during embryonic development by suppressing the recruitment of the prosurvival kinases akt-1/2 to the plasma membrane (PubMed:25383666). In addition, regulates Z2/Z3 germline precursor cell cycle by maintaining them arrested at the G2 stage and by controlling their growth during L1 diapause (PubMed:16631584). After sperm depletion in larvae and adult hermaphrodites, promotes germline stem cell quiescence and oocyte accumulation (PubMed:26552888). By dephosphorylating ephrin-like receptor vab-1 on tyrosine residues, negatively regulates oocyte maturation downstream of vab-1 and upstream of mpk-1, independently of daf-2 (PubMed:19853560). Plays a role in postembryonic muscle arm extensions (PubMed:18436204). Required for neurite outgrowth during AIY interneuron embryonic development (PubMed:22069193). Mainly independently of daf-2, negatively regulates vulva induction probably by inhibiting mpk-1 phosphorylation (PubMed:22916028). Both lipid and protein phosphatase activities are required for the regulation of vulva induction (PubMed:22916028). Plays a role in gonad and germline development following the L1 diapause (PubMed:24746511). {ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:10077613, ECO:0000269|PubMed:10209098, ECO:0000269|PubMed:10377431, ECO:0000269|PubMed:16631584, ECO:0000269|PubMed:16950159, ECO:0000269|PubMed:18436204, ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:19853560, ECO:0000269|PubMed:20207731, ECO:0000269|PubMed:22069193, ECO:0000269|PubMed:22916022, ECO:0000269|PubMed:22916028, ECO:0000269|PubMed:23995781, ECO:0000269|PubMed:24746511, ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:26552888, ECO:0000269|PubMed:9885576, ECO:0000303|PubMed:15637588}.
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Caenorhabditis elegans
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G5EE06
|
FUTD_CAEEL
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MKHNTLRAVFQFSFFIGICTFIMIAGYSYQINYNQRMGIFYGGNITFKKVPKVVIYTATPFFDVPIENSILRDCSEKIKNSCTVTSNNKTFPIADAIVFHSRDINETKLSFFNKNRRYDIPYIMMAMENPFFAGLTVYHNFFNWTMTYRTDSDIFHPYGAFVKSYVPAEVNYSEIWNSKTKETLWMVSNGNAQNKRKELVEKLIKKGMSIDLYGQLYKKEPAECPRRRGPPGCDVKFHSPYKFAIAFENSNCKDYVTEKFWKKAGIYKTVPIVMSRKIYRDLGIPDSMYIAVDDYPNLEEFVHHIQNVTSNEEEYMKYHKWRKQFKIVDTNEGNIGFCQLCQKLAGYKRKLVPHKVYENLNSWHSTSTCDNSFATRFL
|
2.4.1.65
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17369288};
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fucosylation [GO:0036065]; protein glycosylation [GO:0006486]
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Golgi cisterna membrane [GO:0032580]
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3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity [GO:0017060]; metal ion binding [GO:0046872]
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PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:17369288}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304; EC=2.4.1.65; Evidence={ECO:0000269|PubMed:17369288};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:17369288}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. Vey low activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288};
|
FUNCTION: Catalyzes the addition of fucose in alpha 1-3 linkage to GalNAc-beta-1->4-GlcNAc-beta-1->3-Gal-beta-1->4-Glc (LDNT)acceptor. Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2-Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (GnM3F6) acceptors. {ECO:0000269|PubMed:17369288}.
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Caenorhabditis elegans
|
G5EE07
|
XBP1_CAEEL
|
MSNYPKRIYVLPARHVAAPQPQRMAPKRALPTEQVVAQLLGDDMGPSGPRKRERLNHLSQEEKMDRRKLKNRVAAQNARDKKKERSAKIEDVMRDLVEENRRLRAENERLRRQNKNLMNQQNESVMYMEENNENLMNSNDACIYQNVVYEEEVVGEVAPVVVVGGEDRRAFESAAFINEPQQWEQARSTSINNNISNQLRRMDSKKNNTISVDMYLTIISILCNHMDRNKKMDTSNKSSNISRAQAESSIDSLLATLRKEQTVMQRLVQADPCTHLQKRVKHFRRIP
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; IRE1-mediated unfolded protein response [GO:0036498]; lipid homeostasis [GO:0055088]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to endoplasmic reticulum stress [GO:0034976]; response to heat [GO:0009408]; response to topologically incorrect protein [GO:0035966]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF07716;
|
1.20.5.170;
| null |
PTM: [Isoform 2]: Sumoylated (PubMed:24933177). Sumoylation may negatively modulate the transcription of genes involved in the ER-stress-response (PubMed:24933177). {ECO:0000269|PubMed:24933177}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
| null | null | null | null | null |
FUNCTION: Required for transcriptional regulation of the unfolded protein response (UPR) in the endoplasmic reticulum (ER) under stressed conditions, acting downstream of ire-1, and also maintaining ER homeostasis via a negative feedback loop, in parallel with ER kinase pek-1 (PubMed:11779465, PubMed:11780124, PubMed:16184190, PubMed:22125500). May also regulate Golgi protein trafficking distal to the ER (PubMed:16184190). Protects the host organism from the detrimental effects of mounting an innate immune response to microbes, such as the Gram-negative bacterium P.aeruginosa, probably by modulating the UPR (PubMed:20182512, PubMed:22125500). {ECO:0000269|PubMed:11779465, ECO:0000269|PubMed:11780124, ECO:0000269|PubMed:20182512, ECO:0000269|PubMed:22125500}.; FUNCTION: [Isoform 1]: Plays a role in the unconventional cytoplasmic splicing processing of its own mRNA triggered by the endoplasmic reticulum (ER) transmembrane endoribonuclease ire-1: upon ER stress, the emerging xbp-1 polypeptide chain, as part of a mRNA-ribosome-nascent chain (R-RNC) complex, cotranslationally recruits its own unprocessed mRNA through transient docking to the ER membrane and translational pausing, therefore facilitating efficient ire-1-mediated xbp-1 mRNA isoform 2 production. {ECO:0000250|UniProtKB:P17861}.; FUNCTION: [Isoform 2]: Functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE) (By similarity). Plays a role in modulation of the UPR, lipid metabolism, proteostasis, and lifespan (PubMed:23791175, PubMed:31303493, PubMed:31315038, PubMed:31570707). In neurons, rescues stress resistance, increases longevity, and, drives expression of lysosomal genes in the intestine and activates the UPR in distal, non-neuronal cell types through a cell-nonautonomous mechanism (PubMed:23791175, PubMed:31303493, PubMed:31315038). In neurons or intestine, plays a role in protection against proteotoxicity, acting via positive modulation of genes involved in lysosomal function, including lipases and the fatty-acid desaturase fat-6 (PubMed:31303493, PubMed:31315038). Protection against proteotoxicity in neurons is dependent upon the transcription factor atf-6 (PubMed:31570707). {ECO:0000250|UniProtKB:P17861, ECO:0000269|PubMed:23791175, ECO:0000269|PubMed:31303493, ECO:0000269|PubMed:31315038}.
|
Caenorhabditis elegans
|
G5EE18
|
CEH28_CAEEL
|
MQSTQISSTTVILPSEVIQPPQQSAVPSEFKNTLPSRLNLFEGFDQSFSELTNPYQPVIPLMQRESLLGASSYYSSPSQNQRSYQNHRQHSNPDTINLRSQQQKRKPRVLFTQHQVNELEERFKKQRYVTATEREELAQCLGLTATQVKIWFQNRRYKCKRLAQDRTLQLSQIPFNPMFASAFPFGINSFGTAPSSSSSGS
| null | null |
cell differentiation [GO:0030154]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neuron differentiation [GO:0045664]; regulation of synapse organization [GO:0050807]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription elongation by RNA polymerase II [GO:0034243]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
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]
|
PF00046;
|
1.10.10.60;
|
NK-2 homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor that regulates neuronal differention, including synapse assembly of the cholinergic motor neuron M4 (PubMed:24690231, PubMed:25474681). Activates expression of growth factor, neuropeptide and transcription factor genes, such as TGF-beta dbl-1, FMRFamide-like flp-5 and transcription repressor zag-1, in the M4 neuron (PubMed:24690231, PubMed:25474681). Required for pharynx peristalsis (PubMed:18161854). {ECO:0000269|PubMed:18161854, ECO:0000269|PubMed:24690231, ECO:0000269|PubMed:25474681}.
|
Caenorhabditis elegans
|
G5EE56
|
SRC1_CAEEL
|
MGCLFSKERRSGGSDMGVSERIDVSRFQTPQQQTVFHVNNGGNEGTISQLNGTSDGMMGNGRGGGGGGGAQERETLVALYPYDSRADGDLSFQKGDAMYLLDHSNCDWWYVRHQRTGQTGYVPRNFVAKQQTIESEEWYAGKIPRNRAERLVLSSHLPKGTFLIREREADTREFALTIRDTDDQRNGGTVKHYKIKRLDHDQGYFITTRRTFRSLQELVRYYSDVPDGLCCQLTFPAPRLAPTRPDLSHDTQQNWEIPRNQLHLKRKLGDGNFGEVWYGKWRGIVEVAIKTMKPGTMSPEAFLQEAQIMKQCDHPNLVKLYAVCTREEPFYIITEYMINGSLLQYLRTDGSTLGIQALVDMAAQIANGMMYLEERKLVHRDLAARNVLVGDKISGVPVVKVADFGLARKLMEEDIYEARTGAKFPIKWTAPEAATCGNFTVKSDVWSYGILLYEIMTKGQVPYPGMHNREVVEQVELGYRMPMPRGCPEQIYEEVLLKCWDKTPDRRPTFDTLYHFFDDYFVSTQPNYAPPSA
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:20226672}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20226672};
|
anterior/posterior axis specification, embryo [GO:0008595]; cell differentiation [GO:0030154]; commissural neuron axon guidance [GO:0071679]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; endodermal cell fate specification [GO:0001714]; establishment of mitotic spindle orientation [GO:0000132]; gonad morphogenesis [GO:0035262]; innate immune response [GO:0045087]; left/right axis specification [GO:0070986]; phosphorylation [GO:0016310]; positive regulation of embryonic development [GO:0040019]; positive regulation of locomotion [GO:0040017]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell projection [GO:0042995]; contractile fiber [GO:0043292]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; phagocytic cup [GO:0001891]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; netrin receptor binding [GO:1990890]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]
|
PF07714;PF00017;PF00018;
|
3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
|
PTM: May be phosphorylated on Tyr-528 by csk-1. {ECO:0000269|PubMed:12527374}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20226672}; Lipid-anchor {ECO:0000255}; Cytoplasmic side {ECO:0000269|PubMed:20226672}. Cell projection, phagocytic cup {ECO:0000269|PubMed:20226672}. Note=Co-localizes with ina-1 at the site of the phagosomal cup formation during apoptotic cell engulfment. {ECO:0000269|PubMed:20226672}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548, ECO:0000269|PubMed:20226672, ECO:0000269|PubMed:35929733};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine-protein kinase which plays a role in endoderm development by controlling spindle orientation in EMS blastomere, probably downstream of receptor mes-1. Also involved in embryonic body morphogenesis, especially in the formation of the pharynx and the intestine (PubMed:12110172, PubMed:12527374, PubMed:19210548). May be dispensable for pharyngeal muscle organization in the adult (PubMed:19210548). Probably phosphorylates netrin receptor unc-5, to regulate distal tip cell (DTC) migration during gonad development and in axon repulsion (PubMed:16024786, PubMed:16251208). Plays a role in the migration of the QR neuroblast, a precursor of the AVM neuron, and in the migration of the axon cone of AVM, ALM, CAN and PVM neurons (PubMed:16251208, PubMed:22293500). May act downstream of migratory protein mig-13 to control AVM neuron migration (PubMed:22293500). Probably downstream of integrin ina-1/pat-3, plays a role in the clearance of apoptotic cells during mid-embryogenesis (PubMed:20226672). Phosphorylates ced-1 at 'Tyr-1019' which promotes ced-1 proteasomal degradation, maintaining appropriate ced-1 levels for apoptotic cell clearance (PubMed:35929733). {ECO:0000269|PubMed:12110172, ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:16024786, ECO:0000269|PubMed:16251208, ECO:0000269|PubMed:19210548, ECO:0000269|PubMed:20226672, ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:35929733}.
|
Caenorhabditis elegans
|
G5EE72
|
MRP5_CAEEL
|
MPSDSEEVCLQQSGTGVYENVVYSKETSDRAKRYAGDTNRKTIGRYSAAVQNLIPLRTTERNKNNGGSRIDDAGLFSFVTYSWVFPYLYQAVRGKLDRNQVWGCSFYDSCGLNMARLEVLWEDEKKANAKSPSLFKVIYRFISTRLWFSCAVFFFCLIFGFIGPTCFIRRLIAFAENPERDEQSRIVYSYGIALVAAISVVEFARVLSYGATWAVSYRTGIRVRGAVLALLYKNVLNSKDLCGKTESDVINIFANDGQRLFDAVTFAPLVLVGPLVLVGGIGYLLMVIGRWSLLGILVFFVFDVIQFGLGKSMVACRNLAIVKTEKRISMMAEIIKYIRIVKMNGWEQIFSAKIDQFRKEEKVQIRKSGYAQSLAIACGPVVPVVAAILTFVGVVLAGNDLLASDAFSAITVYFVMLFGIRMIPYGSRYLAEAVVAMRRIQEYLLLEQYAPYPVTNAEDVVLDCQGATYTYQPKAAKAPVDETKEPTENEVIVVETPVFTCSFDKLSIKRGEHIAVIGAVGCGKSAILKAISGHMFTTDDALSVDRSQTVYVPQKAWIFNGTVQDNILFGDKMNSERYYKAVNGCQLTEDLTTLSVGDRTEVGERGATLSGGQKARVALARAVFQTKNLYLFDDIFASLDKKVANKIHEEIIQKLLKKKALMMVTNNMELLHHFDRVLFVEGGNIVADGNHDILYEKNDAYKTFVDACETYQATSGATSPCGDGPAQPAPLDAEILRNSSEDLKGDADKLISDEEDMGNSTIAWRIYKQYIHAAGGWPIWTCLVIGFIVNVVSNIFSTYWLSRWLKKGHDETTTITNGTEFLEMKTSLADSPVTGFYAAVYLVALVVLTISGLFKACVFVKVSLTAATRLHDRMFQAVIHGATSFFDSTPTGRILNRFSKDMDEIDVKLPFTAEVFLQNMITCLGFLVVITSVFPYFLLFAIPLFVVFVVFVSCFRAGIRNLKRSEHISRSPLYDHVSASLEGITTIHTFQQSNRFLEVLKKHLDCNSGAIFMFQSAMRWLAVWLDLLVVVMTAIVALLTVMLTGTVSPADAGMAIAFAVQMSGIFQFAVRTQTELEAKMTSVERVSYYADNIPEDGEWNTRQGLDIESSWPANGQINFSEVNLRYRKSHPLALNDITFEIKGGEKVGIIGRTGSGKSSLANLIFRLYPVTNGTIYIDGVDIRTVGLVKLRRGISAIAQDPSLFSGTVRFNLDPSLEYSDSMIWEALEKCHLKTLVQSLDKKLEADVSHGGNNFSVGERQLFCLARALLMKSRIVILDEATASVDAGTDKLIQEVIKTVFADATVIIIAHRLDNVRNMDRIMHLKNGKLINFTTPQEMFKDDWSVYKLEDKDDDQHSAVVVGENSEHSMEKSSQGSSQESDDIVKVENEQKDSSDDVVHIESGDDDVKADSSEVKETSSDTDIEVVQ
| null | null |
cobalamin transport [GO:0015889]; transmembrane transport [GO:0055085]
|
basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]
|
ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:24836561}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Heme transporter required for the export of intestinal heme to different tissues and subcellular compartments (PubMed:24836561, PubMed:28581477). Also, required for the export of vitamin B12 from the intestine of the mother to the embryo to support embryonic development (PubMed:29562169). {ECO:0000269|PubMed:24836561, ECO:0000269|PubMed:28581477, ECO:0000269|PubMed:29562169}.
|
Caenorhabditis elegans
|
G5EE86
|
TTX3_CAEEL
|
MYFQSLSADPLDSVNTTTDFNQLAQLLLMLTNSSSKETIATHVVTNSVPSAFQFDWSSHFKEEYDLVEKLNSPQYTNLTSISPSSSTDSNNLILRQIQIPKIEPALLNQCCLCTFAIVDKEISVVDGKYYHNNCLRCQMCDIPFEYSDKCYVRDGVFLCRADHAKRYQKCCRKCEIPLNREDMVMKAKEMIFHHACFVCFICGIKLNPGDYYTMSPQGHLYCHAHYNAVRSTVLCEEAAVATVPAVVAPPPPPPTTTTAPPPAAPEQPPREASTEAEASTDEDGNGSGSQRSKRMRTSFKHHQLRAMKTYFALNHNPDAKDLKQLAAKTNLTKRVLQVWFQNARAKYRRELHDGGRSSSPLCVSAPLASMDMNPPLSSSSSGHSTDGYQLNTPPLSSEIYSPNSNYTHL
| null | null |
associative learning [GO:0008306]; axonogenesis [GO:0007409]; dauer larval development [GO:0040024]; negative adaptation of signaling pathway [GO:0022401]; neuron differentiation [GO:0030182]; olfactory learning [GO:0008355]; positive regulation of dauer larval development [GO:0061066]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of axon extension [GO:0030516]; regulation of axon guidance [GO:1902667]; regulation of DNA-templated transcription [GO:0006355]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357]; thermosensory behavior [GO:0040040]; thermotaxis [GO:0043052]
|
axon [GO:0030424]; nucleus [GO:0005634]; perikaryon [GO:0043204]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;PF00412;
|
2.10.110.10;1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11493519, ECO:0000269|PubMed:9292724}. Perikaryon {ECO:0000269|PubMed:11493519, ECO:0000269|PubMed:9292724}. Cell projection, axon {ECO:0000269|PubMed:11493519, ECO:0000269|PubMed:9292724}.
| null | null | null | null | null |
FUNCTION: Transcription factor (PubMed:15177025, PubMed:19386265). Binds to a sequence motif, 5'-TTATTGGCTTCGTTAA-3', which may be involved in AIY interneuron function, in the regulatory elements of target genes; binding is more efficient, in vitro, together with homeobox protein ceh-10 (PubMed:15177025). Required for specification of the AIA and AIY interneurons and the NSM neurons (PubMed:11493519, PubMed:24353061). Positively regulates the expression of a number of genes including ceh-10, ceh-23, kal-1, hen-1, ser-2, unc-17 and sra-11 in AIY neurons, and cat-4, flp-4, bas-1, ptps-1 and mgl-1 in NSM neurons (PubMed:11493519, PubMed:15177025, PubMed:19386265, PubMed:24353061). In concert with WNT/beta-catenin signaling, initiates expression of homeobox ceh-10 in AIY, but not in the sister cells, SMDD motor neurons (PubMed:19386265). Also acts in an autoregulatory feedback loop to maintain its own expression (PubMed:19386265, PubMed:9292724). Plays a role in the thermotactic response, olfactory imprinting, regulation of longevity, control of dauer formation and axon outgrowth and pathfinding (PubMed:16051801, PubMed:21055415, PubMed:24353061, PubMed:9292724). Not required for normal chemosensory behavior (PubMed:9292724). {ECO:0000269|PubMed:11493519, ECO:0000269|PubMed:16051801, ECO:0000269|PubMed:21055415, ECO:0000269|PubMed:24353061, ECO:0000269|PubMed:9292724, ECO:0000305|PubMed:19386265}.
|
Caenorhabditis elegans
|
G5EE96
|
DIC_CAEEL
|
MAEDKTKRLGRWYFGGVAGAMAACCTHPLDLLKVQLQTQQQGKLTIGQLSLKIYKNDGILAFYNGVSASVLRQLTYSTTRFGIYETVKKQLPQDQPLPFYQKALLAGFAGACGGMVGTPGDLVNVRMQNDSKLPLEQRRNYKHALDGLVRITREEGFMKMFNGATMATSRAILMTIGQLSFYDQIKQTLISSGVAEDNLQTHFASSISAASVATVMTQPLDVMKTRMMNAAPGEFKGILDCFMFTAKLGPMGFFKGFIPAWARLAPHTVLTFIFFEQLRLKFGYAPPVKA
| null | null |
lipid transport [GO:0006869]; malate transmembrane transport [GO:0071423]; oxaloacetate transport [GO:0015729]; phosphate ion transmembrane transport [GO:0035435]; succinate transmembrane transport [GO:0071422]; sulfate transport [GO:0008272]; thiosulfate transport [GO:0015709]
|
mitochondrial inner membrane [GO:0005743]
|
antiporter activity [GO:0015297]; malate transmembrane transporter activity [GO:0015140]; oxaloacetate transmembrane transporter activity [GO:0015131]; succinate transmembrane transporter activity [GO:0015141]; sulfate transmembrane transporter activity [GO:0015116]; thiosulfate transmembrane transporter activity [GO:0015117]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9QZD8}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + phosphate(out) = (S)-malate(out) + phosphate(in); Xref=Rhea:RHEA:71607, ChEBI:CHEBI:15589, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + malonate(out) = (S)-malate(out) + malonate(in); Xref=Rhea:RHEA:71611, ChEBI:CHEBI:15589, ChEBI:CHEBI:15792; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589, ChEBI:CHEBI:30031; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in); Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + 2 thiosulfate(out) = (S)-malate(out) + 2 thiosulfate(in); Xref=Rhea:RHEA:71619, ChEBI:CHEBI:15589, ChEBI:CHEBI:33542; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=malonate(out) + phosphate(in) = malonate(in) + phosphate(out); Xref=Rhea:RHEA:71623, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + succinate(out) = phosphate(out) + succinate(in); Xref=Rhea:RHEA:71627, ChEBI:CHEBI:30031, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in); Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + 2 thiosulfate(out) = phosphate(out) + 2 thiosulfate(in); Xref=Rhea:RHEA:71635, ChEBI:CHEBI:33542, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=malonate(out) + succinate(in) = malonate(in) + succinate(out); Xref=Rhea:RHEA:71667, ChEBI:CHEBI:15792, ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:Q9QZD8};
| null | null | null | null |
FUNCTION: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:9733776). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, by supplying the substrates for the different metabolic processes (By similarity). {ECO:0000250|UniProtKB:Q9QZD8, ECO:0000269|PubMed:9733776}.
|
Caenorhabditis elegans
|
G5EEA1
|
LIM4_CAEEL
|
MDAHLVQAKKTSTASELSDSSLTFPFIGDYLSSPSLTTSDYVSDCSNLTVEGPVPANQEFSSSDESSVYISSALRLADYAFTPDDNIRIKPDAVIVICTQCQHQIQDKFFLSIDGRNYHENCLQCSTCENPLSNKCFYKDKTFYCKGCYFRTHVTSTASSCRELGPKCASCDRTIQATDWVRRARNYVYHLACFSCNQCKRQLSTGEEYALQEGNLLCKQHFLELVEGDSGVSSQKAKTKRVRTTFAEDQLSVLQTYFNRDSNPDGADLEKIASMTGLSKRVTQVWFQNSRARQKKWHQKSEGDNGDSQRSSVGPSSPSQKSDSSSEMMYPTSVTTSVEDAIPDSIVILGSLQFD
| null | null |
cell fate specification [GO:0001708]; forebrain neuron development [GO:0021884]; neuron differentiation [GO:0030182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357]; serotonin biosynthetic process [GO:0042427]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;PF00412;
|
2.10.110.10;1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to the promoter of target genes (PubMed:16168406, PubMed:26305787, PubMed:26341465). Regulates genes involved in serotonin synthesis and release in serotonergic ADF neurons (PubMed:16168406, PubMed:26305787). Involved in specification of neuron cell fate, olfactory receptor expression, locomotion, and foraging behavior (PubMed:10421632, PubMed:26305787). Required in AWB olfactory neurons to repress AWC cell fate and promote the AWB cell fate during early development (PubMed:10421632). Cooperates with additional factors to direct the differentiation of the olfactory neurons, functioning with the transcription factor sox-2 to suppress AWC terminal differentiation and promote AWB neuron differentiation (PubMed:26341465). Involved in regulating terminal specification and maintenance of the SMB sensory/inter/motor neurons (PubMed:26305787). Plays a role in regulation of RID motor neuron differentiation, but is dispensable for motor axon outgrowth in the dorsal nerve cord (PubMed:14568548). May regulate its own expression (PubMed:10421632, PubMed:26305787). {ECO:0000269|PubMed:10421632, ECO:0000269|PubMed:14568548, ECO:0000269|PubMed:16168406, ECO:0000269|PubMed:26305787, ECO:0000269|PubMed:26341465}.
|
Caenorhabditis elegans
|
G5EEB1
|
FPR18_CAEEL
|
MESQQLMACAILVIVLVGIFGNSLSFILFSRPHMRSSSVNVLLCALSFFDFSLLTLSIPIFVIPNLDLWANDLSLSTYMAYILKLIYPINLMMQTCSVYIMVMITLERWVAVCRPLQVRVWCTPRKSRNAILVIIVSAFLYNFVRFFEYRFVVTESGALYEKWLRDPGKHRWYYVGYYTILYIVTHFLVPFSVMAFANGHVIVAMCKLSKTRQMLTRQQQREQSTTVMLLIVTFVFAICNTLPFLLNVSESIFPTLFQDESTRGLAYWLNDLSNLLVVLNSGTTFIIYFTFSEKYRQTLVFILKNGCCATVSDYNNYTAMSRTASMRISSETGGQIQRQGSKMSNSSRSSDVLLKPIYMQKRSERFSSEYNERTCKHLAPFEEHKLPKLPSEKRKKKLHKMSAVEHRGMPEITITFSEDLPDGEPDSPCQPC
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of protein secretion [GO:0050714]; signal transduction [GO:0007165]; sleep [GO:0030431]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for flp-2 neuropeptides (PubMed:15809090, PubMed:24533288). May act through the G(q) alpha type of G proteins (PubMed:15809090, PubMed:24533288). Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity, and working in concert with neuropeptide pdf-1 (PubMed:27585848). {ECO:0000269|PubMed:15809090, ECO:0000269|PubMed:24533288, ECO:0000269|PubMed:27585848}.
|
Caenorhabditis elegans
|
G5EEC2
|
FLP7_CAEEL
|
MLGSRFLLLALGLLVLVLAEESAEQQVQEPTELEKSGEQLSEEDLIDEQKRTPMQRSSMVRFGRSPMQRSSMVRFGKRSPMQRSSMVRFGKRSPMQRSSMVRFGKRSPMERSAMVRFGRSPMDRSKMVRFGRSSIDRASMVRLGKRTPMQRSSMVRFGKRSMEFEMQSNEKNIEDSE
| null | null |
negative regulation of locomotion [GO:0040013]; neuropeptide signaling pathway [GO:0007218]
|
extracellular space [GO:0005615]
|
neuropeptide receptor binding [GO:0071855]
|
PF01581;
| null |
FARP (FMRFamide related peptide) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28128367}. Note=Secreted from the ASI sensory neurons in response to serotonin or octopamine. {ECO:0000269|PubMed:28128367}.
| null | null | null | null | null |
FUNCTION: FMRFamide-like neuropeptides (PubMed:16377032, PubMed:28128367). Stimulates serotonin-induced fat loss by binding to and activating the npr-22 receptor which leads to induction of the atgl-1 lipase and subsequent fat loss (PubMed:33078707). Together with atfs-1, negatively regulates the expression of the transcription regulator hlh-11, to promote expression of atgl-1, and thus atgl-1-dependent fat oxidation in response to mitochondrial stress (PubMed:33078707). {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28128367, ECO:0000269|PubMed:33078707}.; FUNCTION: TPMQRSSMVRF-amide: Acts as a ligand for the npr-22 receptor in vitro. {ECO:0000269|PubMed:16377032}.; FUNCTION: SPMQRSSMVRF-amide: Acts as a ligand for the npr-22 receptor in vitro. {ECO:0000269|PubMed:16377032}.; FUNCTION: [SPMERSAMVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. {ECO:0000269|PubMed:16377032}.; FUNCTION: [SPMDRSKMVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. {ECO:0000269|PubMed:16377032}.
|
Caenorhabditis elegans
|
G5EEC5
|
HAM1_CAEEL
|
MTYLAVVLNGPKAKNGRKVFDSFLEQNRQMFWNRELTSACESITYMGFMRPGTLFVSGPASQLTVLKDAWARRILKPAMGYTITSLGDLGAIQQVEQMHFVPLGDVICDAVAQLNRQGLAATEQAIRQYVARHCPHVAPPGIEMVRQTITSLLSTGFVYKMADHYFVSVPTNSPMRPPAKAATKTTKTTVECQTGASMMCPQQTSTSSDEHVIEPAKKDHKKCQNSNRRSIFARLFSRGMKPQTIMPSASPIHVGGPPTPPPAAMLPTKNKYPTYHHDLNEECQRKARRRNHPRRGETQKLLSSSSECLKYYPVDMPETRPTRRRARMASPLRSSTPNNSDSAYSISPPHTDSNEEAGSISDSEINHTYININKFRRQNFDSTQFEDLTGATATTSEEPEILGRHIRGVLISNL
| null | null |
anterior/posterior pattern specification [GO:0009952]; asymmetric neuroblast division [GO:0055059]; asymmetric protein localization involved in cell fate determination [GO:0045167]; cell fate determination [GO:0001709]; dopaminergic neuron differentiation [GO:0071542]; neuron apoptotic process [GO:0051402]; neuron migration [GO:0001764]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to actomyosin contractile ring [GO:1990179]; regulation of cell size [GO:0008361]; spindle localization [GO:0051653]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF10264;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:15979607, ECO:0000269|PubMed:26703426}. Nucleus {ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}. Cytoplasm {ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}. Note=Distributed asymmetrically in the cell cortex in some embryonic cells, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB) neuroblast (PubMed:15979607, PubMed:26703426). Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts (PubMed:23946438). {ECO:0000269|PubMed:15979607, ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor (PubMed:23946438). Required for asymmetric cell division in neuroblasts, perhaps acting by regulating spindle positioning and myosin polarization, and thus the position of the cleavage plane (PubMed:15979607, PubMed:18505863, PubMed:23946438, PubMed:26703426, PubMed:3200316, PubMed:8951066). Required to produce daughter cell size asymmetry in neuroblasts undergoing asymmetric cell division, usually giving rise to one precursor cell and one apoptotic cell (PubMed:15979607, PubMed:23946438, PubMed:29668718). Positively modulates expression of the serine/threonine kinase pig-1/MELK during asymmetric division of the Q.a neuroblast (PubMed:23946438). Plays a role in neural fate specification in several dopaminergic lineages, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB), acting in concert with the kinase, ham-1, and the T-box protein tbx-2 and the homeobox protein egl-5 (PubMed:18505863, PubMed:23946438, PubMed:28659600, PubMed:3200316, PubMed:8951066). {ECO:0000269|PubMed:15979607, ECO:0000269|PubMed:18505863, ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426, ECO:0000269|PubMed:28659600, ECO:0000269|PubMed:29668718, ECO:0000269|PubMed:3200316, ECO:0000269|PubMed:8951066}.
|
Caenorhabditis elegans
|
G5EED4
|
NIPI3_CAEEL
|
MARTKCKTKTVANPRTGVRKTAKDLSEPVRQDAVSRRRPTTLPFVGNTSSRPRVFYDVLAKKNVVFPNVKAEYHYRVRNAPKIDPKNFGTTLPICYSSIGPAKTLELRPLGRLPPHIIKALNDHYVQLTRGSMVPAADLYNNGDHPAEQRIPTMLNENEYLRLIQELEEEEKSKQFSATSSSAPHVNPYSAQHLVNGEIIGIFVIYGTGLVTRAVCSQTREMFTAHVLPEWKASKVIDVIRRLQIPTDISSMTADEIRLSELCISKRMEIIKSNDRYILMNPCESATIHSYATERLDEITENDVMSIYQKVVEIVRFCHSRKVILQNFKPRSFYLKKDAHNKWVVRPCFLQDMSCEEDQSEAQFTRRSVCVPFMAPEMLTAESRTHHSYSTELWGLGVLLYILLTGKYPFHENSMPLLFRTIKFKQHRWPFNFISSKSRNIVNMLLKKAPATRMNLEDLWNQVNGDFPEIRCRSNIILKKQDMIVKMDLFEMYYNTYKDRLLPKNVLPMYEEMKACRNDSTILTEMAKRDFRSIQEQMKRRIETKPTEYQTLVMQVRLQQINQLFFEKEVSQAQKQHRAPRLVQLKCSDISKELLLPGDIYPISEHYHPSQQPVDKVVYKLLSDANSLAFPTVMKGTVPKSYPPPVFKGLDISPS
| null | null |
defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of gene expression [GO:0010468]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; mitogen-activated protein kinase kinase binding [GO:0031434]; protein kinase activity [GO:0004672]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27927209}.
| null | null | null | null | null |
FUNCTION: Adapter protein that regulates different signaling pathways (By similarity). Required for larval development and viability (PubMed:27927209). Involved in negatively modulating pmk-1 p38/MAPK signaling (PubMed:27927209). Involved in innate immunity, acting either in a manner dependent upon, or independent of, the pmk-1 or pmk-3 p38/MAPK pathways (PubMed:18394898, PubMed:27927200, PubMed:34407394). Has a protective role in response to infection by the Gram-negative bacterium P.aeruginosa, acting by negatively modulating expression of cebp-1, and regulating the pmk-1 p38/MAPK pathway, leading to activation of transcription factor skn-1 (PubMed:27927200, PubMed:34407394). Required to prevent P.aeruginosa toxin ToxA-mediated lethality, probably acting via modulating the effects of translational inhibition caused by the toxin (PubMed:27927200). By regulating the up-regulation in the epidermis of antimicrobial peptides nlp-29 and nlp-31, plays a role in resistance to fungal infection (PubMed:18394898, PubMed:27927200). {ECO:0000250|UniProtKB:Q9V3Z1, ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:27927200, ECO:0000269|PubMed:27927209, ECO:0000269|PubMed:34407394}.
|
Caenorhabditis elegans
|
G5EEE1
|
FUTE_CAEEL
|
MSQIGGATCTWRYLGRFVTLGIYASVALFVWYTLVPTRSKHKDSIAINNNNADPATALIPVHTKNVVIYAATKFFGHPITTERFLATCPDVQNYCRITQEESEFDNADAVLFHNADYRGSTDKFKKMKSQRKPGVPYVLWSLESPTNDMFRPDSHMINWTMTYRTDSDVWAPYGTIVKLKNPVEVDLNAIWEGKTKTATWLASNCITQNHRFDLIKKIIDNGFEIDIWGNCGKQVSQCAGVDNQESPCVLELIKPYKFYISMENSNCKDYVTEKFWKALNDRMTIPIVLARKYYKDLGVPDSAYIAVDDYATLDEFLAHVKKVNKEKDLFLSYHQWRKEWKVIIGSGFSGWCTLCNKLQDKDYILKNPKSYKDVAWWHSFEMCNNQIASKYL
|
2.4.1.-
|
COFACTOR: Note=Unlike other alpha-(1,3)-fucosyltransferases, appears not to require a divalent metal cation as cofactor. {ECO:0000269|PubMed:17369288};
|
fucosylation [GO:0036065]; protein glycosylation [GO:0006486]
|
Golgi cisterna membrane [GO:0032580]
|
alpha-(1->3)-fucosyltransferase activity [GO:0046920]; fucosyltransferase activity [GO:0008417]
|
PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
| null | null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284, ECO:0000269|PubMed:26002521, ECO:0000269|PubMed:26538210}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. Very low activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288};
|
FUNCTION: Involved in the fucosylation of N-glycans (PubMed:15364955, PubMed:17369288, PubMed:23754284, PubMed:26002521, PubMed:26538210). Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the distal GlcNAc residue in N-glycans (PubMed:23754284). Catalyzes the transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288). Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288). {ECO:0000269|PubMed:15364955, ECO:0000269|PubMed:17369288, ECO:0000269|PubMed:23754284, ECO:0000269|PubMed:26002521, ECO:0000269|PubMed:26538210}.
|
Caenorhabditis elegans
|
G5EEE9
|
GCY23_CAEEL
|
MRRELFIFLLLLGECANVKVKVGHIGAVGSMRNAEKILQLSKEQLTQEGVLGNDFDIEILNQMGCGESYEGVAVGADMYHVQGVRAFIGPYCNAELDAVAKMATFWNIPVVGYMASSNSFADKTIFKTLARVSLRTTNSLAEAAAALIKHYGWNKVAIATNTGAVAFERVQSFEEVFHQRGINVVRKIMLEEYTNAKAIMNSGLLQELENSARVVVCAFSSTRDMNKEFMQAVTLSGMNNANYAWILPWLQLETKDMAPWLGENGEYQQNVKDHFANSFIIDDVNGFDNTLVTPFKERLEASGYSTDDLEMKNIYGYIHLYDALRLYALAVRATMNETGNENSYLNGKEVWNHMRRITFPGLVSNAGVTSGTVMMDDIAERAPVYAAFYVPPNSDTVRKVCELEPVMLTNCDGTKTGNGCYELQVTDLSTGFWPSIDGSLPADEPACGFRNEKCDYTTLIIGGCIVLLIILLIICFFILSRVCENRALANTPWRIYRDDFRTIQENEMKSMLSIGSSKTKMSNMSMFVKHHAVVGTNTHASFHLYPQRRPIVFNRQDLQLLNQMKQAVHDNLNPFLGMSFNEKEEMVVLWKFCSRGTIQDMIYNQEVSLDSKFHGAFIRDITLGLEYLHSSIIGYHGSLTPWSCLIDRNWMIKLTDYGIANPLERWEKLGLISTETLKEGDDKSGSAQKTSLLYQPPEMLKNKESNRTRRMDQSWVKQSQARRQMGDIYAFGMVMHEILFRALPFPNGTNVSEVMDYIRDGTKTFRPTVHDRTQIHPDLVALLLDCWNENPEVRPSIRRVRLNTENYLKVKGSLVDQMMRMMEQYANNLEKLVAERTGMLEEANVRADKLLGQLLPKYVANELKMGRSVPAKTFDMATVMFSDIVGFTTICSSSTPLEVVSMLNSIYSKFDDAINKHGSYKVETIGDAYMIVSGIPEENGNEHIRNICNTALELMLLLKTYEIPHRRNVKLRIRLGIHTGTVAAGVVGLTAPRYCLFGDTVNVASRMESTSEPEKIQMSQEARDFCVRYYSEFQITLRGTVEAKGKGPVTSYWLLGKQSESQMQQQNFSQLGI
|
4.6.1.2
| null |
cGMP biosynthetic process [GO:0006182]; detection of temperature stimulus [GO:0016048]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; thermosensory behavior [GO:0040040]; thermotaxis [GO:0043052]
|
cilium [GO:0005929]; neuron projection terminus [GO:0044306]; plasma membrane [GO:0005886]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]
|
PF01094;PF00211;PF07714;
|
3.40.50.2300;3.30.70.1230;1.10.510.10;
|
Adenylyl cyclase class-4/guanylyl cyclase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:16415369}. Note=Localizes exclusively to the sensory ending, known as cilium, in AFD neurons. {ECO:0000269|PubMed:16415369}.
|
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187};
| null | null | null | null |
FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates thermotaxis responses in AFD sensory neurons. May regulate AFD neuronal activity such as calcium responses to temperature gradients (PubMed:16415369). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:16415369}.
|
Caenorhabditis elegans
|
G5EEG1
|
NFYA1_CAEEL
|
MNGASRGDVQRPTPVQAPAKRPIPPTVFRFEKASKIGTSLDTTPKELPIRRPVPLPGPRFVKDVNPSPPATSSPNVQTQCHQPPVVRSQTHQASVSQTTPTQTTPSQYTPASVSTARAPQFHRSSHVTPSQQQRIEQAFGPAPVSQSQPQNGSYIQYNEPSTSVASTTTSFYSPNESEPVFTHAISFKPNEPENGQKAREQLELLDSGKINEINQSKVPTTIELPPNCKLFQYSWVLDGIPRTLLVPMPMDATEEDVKAMLPKTLEMDSNLFNNARPRDELPVLSFPNGTVPNVEMIGPKVQQPMLVNPKQFNRIMRRREMRQQLEASGRLPLARQKYLHESRHLHALKRKRGLDGRFDNTKTAESSSMVSSTTSPRKLKRRNRLPGEETSDSSSIVLPSPVEIQPKGGIVNSSMPSTSTGYINNGMDHQTDYIEHQQPMSTYDQYHDHVQYIAPDGNVNYHNNHDNGVDLTGSDGQSFTNL
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of nematode male tail tip morphogenesis [GO:0110039]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888]
|
CCAAT-binding factor complex [GO:0016602]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]
|
PF02045;
|
6.10.250.2430;
|
NFYA/HAP2 subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17574230}.
| null | null | null | null | null |
FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types (PubMed:17574230). In association with the components in the nfya-1-NF-Y complex, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues (PubMed:23933492). May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role (Probable). With the components in this complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head (PubMed:17574230). May regulate egl-5 expression in association with the mes-2-mes-3-mes-6 complex (PubMed:17574230). {ECO:0000269|PubMed:17574230, ECO:0000269|PubMed:23933492, ECO:0000305|PubMed:25873636}.
|
Caenorhabditis elegans
|
G5EEG7
|
SMU1_CAEEL
|
MSSIEIESSDVIRLIEQFLKESNLHRTLAILQEETNVSLNTVDSIDGFCNEITSGNWDNVLKTVQSLKLPAKKLIDLYEHVIIELVELRELATARLVARQTDPMILLKQIDPDRFARLESLINRPYFDGQEVYGDVSKEKRRSVIAQTLSSEVHVVAPSRLLSLLGQSLKWQLHQGLLPPGTAIDLFRGKAAQKEQIEERYPTMMARSIKFSTKSYPESAVFSPDANYLVSGSKDGFIEVWNYMNGKLRKDLKYQAQDNLMMMDAAVRCISFSRDSEMLATGSIDGKIKVWKVETGDCLRRFDRAHTKGVCAVRFSKDNSHILSGGNDHVVRVHGMKSGKCLKEMRGHSSYITDVRYSDEGNHIISCSTDGSIRVWHGKSGECLSTFRVGSEDYPILNVIPIPKSDPPQMIVCNRSNTLYVVNISGQVVRTMTSGKREKGDFINCILSPKGEWAYAIAEDGVMYCFMVLSGTLETTLPVTERLPIGLAHHPHQNLIASYAEDGLLKLWTD
| null | null |
embryo development ending in birth or egg hatching [GO:0009792]; locomotion [GO:0040011]; mechanosensory behavior [GO:0007638]; mRNA splicing, via spliceosome [GO:0000398]; muscle organ morphogenesis [GO:0048644]; nematode larval development [GO:0002119]; neuron development [GO:0048666]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]
|
nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; U2-type precatalytic spliceosome [GO:0071005]
|
identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF17814;PF00400;
|
2.130.10.10;
|
WD repeat SMU1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11438655, ECO:0000269|PubMed:15254247}.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (By similarity). Selectively regulates alternative splicing of unc-52 exon 17 (PubMed:11438655, PubMed:15254247). Thus, smu-1 mutants selectively suppress the effects of unc-52 nonsense mutations in exon 17 by promoting the accumulation of unc-52 isoforms that lack exon 17 and enhance the effects of unc-52 mutations that affect the exon 16 splice donor site (PubMed:11438655, PubMed:15254247). In contrast, smu-1 mutants do not suppress unc-52 nonsense mutations in exon 18 (PubMed:11438655). {ECO:0000250|UniProtKB:Q2TAY7, ECO:0000269|PubMed:11438655, ECO:0000269|PubMed:15254247}.
|
Caenorhabditis elegans
|
G5EEG9
|
HLH2_CAEEL
|
MADPNSQLTSATTVATAAIAQPQVMLPNAYDYPYNIDPTTIQMPDYWSGYHLNPYPPMQTTDIDYSSAFLPTHPPTETPASVAAPTSATSDIKPIHATSSTSTTAPSTAPAPTSTTDVLELKPTTAPATNSAETSAIVAPQPLTNLTAPIDAMSSMYTWPQTYPGYLPPSEDNKASEAVNPYISIPPTYTFGADPSVADFSSYQQQLAGQPNGLGGDTNLVDYNHQFPPAGMSPHFDPNGYPGMTGMPPGSSASSVRNDKSASRATSRRRVQGPPSSGIPTRHSSSSRLSDNESMSDDKDTDRRSQNNARERVRVRDINSAFKELGRMCTQHNQNTERNQTKLGILHNAVSVITQLEEQVRQRNMNPKVMAGMKRKPDDDKMKMLDDNAPSAQFGHPRF
| null | null |
basement membrane disassembly [GO:0034769]; body morphogenesis [GO:0010171]; cell fate specification [GO:0001708]; embryo development ending in birth or egg hatching [GO:0009792]; germ-line stem cell population maintenance [GO:0030718]; gonad development [GO:0008406]; gonad morphogenesis [GO:0035262]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; neuroblast fate specification [GO:0014018]; neuron development [GO:0048666]; neuron fate specification [GO:0048665]; positive regulation of distal tip cell migration [GO:1903356]; positive regulation of gene expression [GO:0010628]; positive regulation of programmed cell death [GO:0043068]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of ATP metabolic process [GO:1903578]; regulation of establishment of cell polarity [GO:2000114]; regulation of generation of precursor metabolites and energy [GO:0043467]; regulation of transcription by RNA polymerase II [GO:0006357]; reproduction [GO:0000003]; response to food [GO:0032094]; vulval development [GO:0040025]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; 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 DNA binding [GO:0043565]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076762}.
| null | null | null | null | null |
FUNCTION: Transcription factor which binds the E box motif 5'-CA[TC][AG]TG-3' (PubMed:11076762, PubMed:14701877, PubMed:19632181). Plays a key role in the anchor cell/ventral uterine precursor cell (AC/VU) decision; required for VU fate (PubMed:14701877, PubMed:31402303). Regulates expression of lin-12/Notch receptor and putative ligand lag-2 in the presumptive AC and presumptive VU cells (PubMed:31402303). Modulates expression of lag-2 in the gonadal distal tip cells (DTCs) (PubMed:14701877, PubMed:19376107). Involved in formation of the polarised cell membrane of the AC and thus facilitates invasion across the gonadal basement membrane, acting via transcriptional modulation of multiple genes (PubMed:21784067). Involved in specification of the hermaphrodite DTC and the male linker cell, perhaps acting in concert with the homeobox protein, ceh-22 (PubMed:19376107). Plays a role in regulation of migration of DTCs and the modulation of expression of alpha integrin ina-1 and ADAMTS protease gon-1 (PubMed:17588558, PubMed:25982859). Required for DTC maintenance, and for function of the DTC as a niche for germline stem cells (PubMed:19376107). Plays a role in cell-autonomously establishing a neuronal left-right asymmetry (PubMed:21041366). Required for specification of cell fate, acting in concert with lin-32, in the development of the male-specific genital sensilla (simple sense organs) known as rays (PubMed:11076762). Negatively modulates lifespan, perhaps acting by regulating expression of arginine kinases, which in turn results in altered metabolism and homeostasis of reactive oxygen species (ROS) (PubMed:32203922). {ECO:0000269|PubMed:11076762, ECO:0000269|PubMed:14701877, ECO:0000269|PubMed:17588558, ECO:0000269|PubMed:19376107, ECO:0000269|PubMed:19632181, ECO:0000269|PubMed:21041366, ECO:0000269|PubMed:21784067, ECO:0000269|PubMed:25982859, ECO:0000269|PubMed:31402303, ECO:0000269|PubMed:32203922}.
|
Caenorhabditis elegans
|
G5EEH5
|
MXL1_CAEEL
|
MSDMSDLEDDQTGHCGSGEHSGPFDPKRHAREQHNALERRRRDNIKDMYTSLREVVPDANGERVQASRAVILKKAIESIEKGQSDSATLSVDVAEQESKNAKLREEIARLKAKKDPSSSQSIIQ
| null | null |
determination of adult lifespan [GO:0008340]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]
|
PF00010;
|
4.10.280.10;
|
MAX family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which binds to the E box motif 5'-CACGTG-3', when in a heterodimeric complex with mdl-1 (PubMed:9764821). Involved in the control of lifespan in response to dietary restriction, the decline in protein homeostasis associated with normal aging and may overlap with the insulin-like signaling pathway (PubMed:24699255). Involved in promoting infection by the microsporidian pathogen N.parisii (PubMed:27402359). {ECO:0000269|PubMed:24699255, ECO:0000269|PubMed:27402359, ECO:0000269|PubMed:9764821}.
|
Caenorhabditis elegans
|
G5EEH9
|
NUP98_CAEEL
|
MFGQNKSFGSSSFGGGSSGSGLFGQNNQNNQNKGLFGQPANNSGTTGLFGAAQNKPAGSIFGAASNTSSIFGSPQQPQNNQSSLFGGGQNNANRSIFGSTSSAAPASSSLFGNNANNTGTSSIFGSNNNAPSGGGLFGASTVSGTTVKFEPPISSDTMMRNGTTQTISTKHMCISAMSKYDGKSIEELRVEDYIANRKAPGTGTTSTGGGLFGASNTTNQAGSSGLFGSSNAQQKTSLFGGASTSSPFGGNTSTANTGSSLFGNNNANTSAASGSLFGAKPAGSSLFGSTATTGASTFGQTTGSSLFGNQQPQTNTGGSLFGNTQNQNQSGSLFGNTGTTGTGLFGQAQQQPQQQSSGFSFGGAPAATNAFGQPAAANTGGSLFGNTSTANTGSSLFGAKPATSTGFTFGATQPTTTNAFGSTNTGGGLFGNNAAKPGGLFGNTTNTGTGGGLFGSQPQASSGGLFGSNTQATQPLNTGFGNLAQPQIVMQQQVAPVPVIGVTADVLQMQANMKSLKSQLTNAPYGDSPLLKYNANPEIDGKSSPASTQRQLRFLAAKKGALSSSSDAQDSSFIIPPISKVMSDLSPAVTRSADVTKDLNYTSKEAPPSLARGLRNSTFNPNMSLTNRSVHESSALDKTIDSALDASMNGTSNRLGVRGSVRRSNLKQLDMSLLADSSRVGRESRVADPDALPRISESERRQDVVTSTPAVDPVQAVIQRHNDRNRDPPSLNLDTTCDEHTGLEPVSAATSSAASVVSTPSEETVNVNSAAGVKLTKPDYFSLPTINEMKNMIKNGRVVLEDGLTVGRSSYGSVYWPGRVELKDVALDEIVVFRHREVTVYPNEEEKAPEGQELNRPAEVTLERVWYTDKKTKKEVRDVVKLSEIGWREHLERQTIRMGAAFKDFRAETGSWVFRVDHFSKYGLADDDEPMDGSPPQQALQASSPLQVIDMNTSARDVNNQVQRKKVHKATDAHHQEIILERVPAPAALGDVVPIIRRVNRKGLGGGTLDDSREESCIGNMTTEFNESGHDSIIEEGQQPEKKPKLELLADLEYESSRFIRNLQELKVMPKANDPAHRFHGGGHSAKMIGYGKSKLIDIGIVKGRSSHVGWSETGCLVWSAQPRHNQVLFGTIDRTSDVNENTLISMLDVNVHVSETSRKGPSSQSNSVKSSLTSNFVTYSDSYSSMFAKYIDVAQAGGYDGHVSVWKLISALFPYERREGWSFERGEEIGEWLRTEAVKSVPDDRSADTSSNGVWNQLCLGDIDKAFQIAIDNNQPQLATMLQTSAVCPEATVHCFKAQLDNWKKCETLHLIPKETLKCYVLMSGLSHYEWDQDGKNHSINCLDGLNWIQALGLHVWYLRAWTGLEESYDAYQKDVNAGRAASNRGDLPGELIKLACESQHSVEVVLDCAAGENPNDYFLQWHVWSLLYSVGYRTMSKTSETRLHRNYSSQLEASSLSKYALFVLQHIDDDEERSTAVRSLLDRIARFTDNDMFDSISEQFDIPSEWIADAQFSIAKSVDDSTQLFELAVAAKNYLEICRLFVDDIAPTAVVAGDHDALKAACAMVRPFENQIPEWGATGMVYTDYCRLINLIENDAEEELLQDVLESLETRLHAPTISKNSLQKLSLQTIGRVLFEYRADKNTLPEWTKLLGHRQMFKIFRDRSSWGIERFTIEFD
|
3.4.21.-
| null |
cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; mitotic chromosome centromere condensation [GO:1990893]; mRNA transport [GO:0051028]; nuclear pore localization [GO:0051664]; nucleus organization [GO:0006997]; P granule organization [GO:0030719]; post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery [GO:0000973]; protein import into nucleus [GO:0006606]; protein localization to kinetochore [GO:0034501]; protein localization to nuclear envelope [GO:0090435]; protein transport [GO:0015031]; proteolysis [GO:0006508]; RNA export from nucleus [GO:0006405]; telomere tethering at nuclear periphery [GO:0034398]
|
cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore cytoplasmic filaments [GO:0044614]; P granule [GO:0043186]
|
nuclear localization sequence binding [GO:0008139]; RNA binding [GO:0003723]; serine-type peptidase activity [GO:0008236]; structural constituent of nuclear pore [GO:0017056]
|
PF04096;PF13634;PF12110;PF21240;
|
1.10.10.2360;1.25.40.690;3.30.1610.10;
|
Nucleoporin GLFG family
|
PTM: The Nup98 and Nup96 chains are autoproteolytically processed from a single precursor protein. {ECO:0000269|PubMed:20335358}.
|
SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup98]: Cytoplasmic granule {ECO:0000269|PubMed:20335358}. Nucleus membrane {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:28122936}; Peripheral membrane protein {ECO:0000269|PubMed:20335358}; Nucleoplasmic side {ECO:0000269|PubMed:20335358}. Note=P granule localization dependent on nucleoporins npp-7, npp-8 and npp-9 which are involved in P granule integrity. {ECO:0000269|PubMed:20335358}.; SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:20335358}. Nucleus envelope {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360}. Chromosome {ECO:0000269|PubMed:16950114}. Note=Requires mel-28 for chromatin association during early steps of nuclear pore complex assembly. {ECO:0000269|PubMed:16950114}.
| null | null | null | null | null |
FUNCTION: Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC) (PubMed:20335358, PubMed:28122936). Required for the nuclear import of hcp-4 during mitotic prophase, this step is essential for centrosome assembly and resolution (PubMed:28122936). Regulates nucleoporin npp-5 localization to the nuclear membrane during interphase and to kinetochores during metaphase (PubMed:22238360). Has a role in P granule integrity; may promote the 'liquid phase' of P granules by increasing the number of interacting RNA-protein complexes (PubMed:20335358). Binds nos-2 mRNA, probably indirectly, and promotes its accumulation in P granules (PubMed:20335358). {ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360, ECO:0000269|PubMed:28122936}.
|
Caenorhabditis elegans
|
G5EEI4
|
ASP1_CAEEL
|
MQTFVLLALVAACSAAVIQVPTHKTESLRAKLIKEGKYTAFLASQHAARAQQLNTGFQPFVDYFDDFYLGNITLGTPPQPATVVLDTGSSNLWVIDAACKTQACNGYPDSGYTKQKFDTTKSTTFVKETRKFSIQYGSGSCNGYLGKDVLNFGGLTVQSQEFGVSTHLADVFGYQPVDGILGLGWPALAVDQVVPPMQNLIAQKQLDAPLFTVWLDRNLQIAQGTPGGLITYGAIDTVNCAKQVTYVPLSAKTYWQFPLDAFAVGTYSETKKDQVISDTGTSWLGAPNTIVSAIVKQTKAVFDWSTELYTVDCSTMKTQPDLIFTIGGAQFPVKSVEYVLDLQLGGGKCALAVFSMGSGGFGPSWILGDTFIRQYCNVYDIGNGQIGFATAVHKGL
|
3.4.23.-
| null |
programmed cell death [GO:0012501]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; external side of apical plasma membrane [GO:0098591]; extracellular region [GO:0005576]; lysosome [GO:0005764]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF07966;PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10854422}. Lysosome {ECO:0000305|PubMed:10854422}. Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Aspartic protease, which is part of the necrosis cell death pathway (PubMed:12410314, PubMed:26795495). Promotes B.thuringiensis Cry6Aa stability by preventing its proteolysis by host gut proteases. Required for Cry6Aa-induced necrotic death of intestinal cells (PubMed:26795495). Cry6Aa uptake into the host intestinal cells triggers an increase in intracellular Ca(2+) levels leading to lysosome rupture and to the subsequent release of asp-1 which leads to necrosis (PubMed:26795495). {ECO:0000269|PubMed:12410314, ECO:0000269|PubMed:26795495}.
|
Caenorhabditis elegans
|
G5EEK3
|
NOCA1_CAEEL
|
MSNERVSTGSLGERLMLRTRSTRGSVRETLSKAIRSTLGRASSMERKDMPDRPKYGTALTAMTSTTPPSPKDRSSDSGDGDSPRPRKFSSKECARIYFSNTSSEHSSRSNSSTPRRVRHTTASSGYGSLSHLPPISYRKSSDPLNSLMSQSMYVQSPGMHIDEPKCTSLSQRRLYYEDSSETYIPSSPSLTTLKDFMMTNDDETFDDFDFDNDDVKSVISSASTSRIFSVDNRMSKYQKNQSLRQFLNSPVRLRKRGDTSRRDAVEAGFEPRDTVPRCHSTQSLRDVQRVRSYNNSQFQASDLSLNPNGSIRAACDSTSGSVAPTAVVNPARNHVISHRQQHHTSYEKDLIPHHNIDVDRRRSLQALNGSSALYQLNNGGSPNGVRSQFSPSDLSIHTPVHHVGSRVRVSSVNQICDSNSAPQFSIDQRRSVHNIGNPVRNSFVDGIKTTSTPKNQIAVAPLAHKSRHLSESRDEMRGGAERRGSGGQMNLPAYTNYLIRHSGEERLVDGPVTNASDARIAYLEKRIRELELTQKEQSSHSTPSQSRHSSSKSSHFNGSSNLSTSEQLRLQEMSDELANKDRKVTSLESKLLKAYQRIERLNEEYDGKIKNLMYDSERARDDLTRCVDKIQQLENELDETRAAVQNGDHANEQEYHELRDKIWKQERELQESRTLLTRLREKEAEFERMRSEKGYLELKNENLNKKLEAKKRAVEELERSVSTLRLEQTICQQSCSSGSTPLADEMEIMSDIRPSLARPYTKAHSTLGSHNMSPLSHSKSSGLTKSFSNFALNSSKQRDDITANMSRSIREQNRHITMCRAMVVCLKDTVDRMARGENPDVARLLGVKLNVMSESEMEDDEDHEADASQPFSMMSAESALSKQCGKLADLDKDLDTIRCQLADWHGQTNAEGDGDRDVCRVQ
| null | null |
cytoplasmic microtubule organization [GO:0031122]; germ cell development [GO:0007281]; nematode larval development [GO:0002119]
|
adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; hemidesmosome [GO:0030056]; microtubule [GO:0005874]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26371552}. Apical cell membrane {ECO:0000269|PubMed:26371552}. Cell junction, hemidesmosome {ECO:0000269|PubMed:26586219}. Cell junction, adherens junction {ECO:0000269|PubMed:26586219}. Note=Isoform h: Co-localizes with gamma-tubulin to the apical cell membrane. {ECO:0000269|PubMed:26371552}.
| null | null | null | null | null |
FUNCTION: Plays a role in the assembly of microtubule arrays in the germline acting redundantly with ptrn-1 to control circumferential microtubule assembly along the body which is necessary for larval development, viability, and morphology and integrity of the epidermis (PubMed:26371552). Required for microtubule stability and anchorage by binding to microtubule minus ends (PubMed:26371552). Recruited to hemidesomosomes in early embryonic elongation to direct the nucleation and growth of non-centrosomal microtubules (PubMed:26586219). {ECO:0000269|PubMed:26371552, ECO:0000269|PubMed:26586219}.; FUNCTION: [Isoform b]: Required for normal nuclear migration in the embryonic epidermis. {ECO:0000269|PubMed:26371552}.; FUNCTION: [Isoform h]: Directs the assembly of non-centrosomal microtubule arrays that determine the position of nuclei within intracellular compartments in the epidermis and this is independent of ptrn-1 activity. {ECO:0000269|PubMed:26371552}.
|
Caenorhabditis elegans
|
G5EEK9
|
VPP2_CAEEL
|
MGSLSRSEEMRFCQLIVEKDAAFNIVAEIGKQPYVQFKDLNPNVNSFQRTFVKDIRRYDEMERKLRFLESQIVKDEIVIPGRVDTGDYTILPTSELNTLEGTLTELEKDVKSMNDSDSQLKANFMDLKEWDAVLDKTDEFFQGGVDDQAQEELENLDEEGAVPRVEKGPVNYLVGIIRRERLNGFERVLWRACHHTAYIRSSDIEEELEDPGTGEKVHKSVFIIFLKGDRMRSIVEKVCDGFKAKLFKNCPKTFKERQSARNDVRARIQDLQTVLGQTREHRFRVLQAAANNHHQWLKQVRMIKTVFHMLNLFTFDGIGRFFVGECWIPLKHVEDVRKAIEVGAERSGSSVKPVLNILETSVTPPTYNETNKFTAVFQGIVDSYGIATYRELNPAPYTIITFPFLFSCMFGDLGHGCIMLMAGLWFVLREKNLQARNIKDEIFNMFFGGRYIILLMGLFSIHAGIIYNDMFAKSFNIFGSGWKNPYNASEIEGWINRTEHGKEMLVELAPEDAYDHAGGPYSFGVDPIWNIAENKLNFLNSMKMKLSVILGISQMTFGVILSFFNHTYNKSKIDIFTVFIPQMLFMGCIFMYLCLQIILKWLFFWTKEATVFGQIYPGSHCAPSLLIGLINMFMMKDRNAGFVVDGGKVNGEYREVETCYLSQWYPGQSVIEMILVVIAVICVPVMLFGKPIHHVMQQKKKAKELHGNATVRANVVSDSSEIVLNGGSKKEGAAHEEHGHGGHEDESFGDIMVHQAIHTIEYVLGCVSHTASYLRLWALSLAHAQLSEVLWHMVFVTGGLGISGTAGFIAVYVVFFIFFVLTISILVLMEGLSAFLHTLRLHWVEFQSKFYLGLGYPFVPYSFKTALQEAEAA
| null | null |
collagen and cuticulin-based cuticle development [GO:0040002]; exosomal secretion [GO:1990182]; multicellular organismal-level water homeostasis [GO:0050891]; nematode larval development [GO:0002119]; regulation of secretion [GO:0051046]; vacuolar acidification [GO:0007035]
|
apical plasma membrane [GO:0016324]; cell body membrane [GO:0044298]; cytoplasmic vesicle [GO:0031410]; exocytic vesicle [GO:0070382]; multivesicular body [GO:0005771]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220]
|
ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF01496;
| null |
V-ATPase 116 kDa subunit family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:16785323}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:16785323}; Multi-pass membrane protein {ECO:0000255}. Note=In embryos, localizes to dot-like compartments or in cup-shaped structures (PubMed:11441002). Localizes to multivesicular body membranes in the epidermis (PubMed:16785323). Colocalizes with vha-8 to stacked sheets of the apical cell membrane of syncytial hypodermal cells (PubMed:16785323). In the epidermis, localizes to dispersed spots during intermolts which becomes aligned and colocalizes with actin bundles during the molts (PubMed:17179093). {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:17179093}.
| null | null | null | null | null |
FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in the assembly of the V-ATPase complex (PubMed:17179093). The V-ATPase is required for the function of the excretory canal (PubMed:16785323, PubMed:17179093). Independently of the V1 complex, the V0 complex of the V-ATPase is required for multivesicular body membrane fusion with the apical membrane of the epidermal cells during exosome release and thus regulates the release of cuticle components such as Hedgehog-related peptide wrt-2 but not collagen (PubMed:16785323). Also, in the epidermis, regulates the trafficking of che-14 and rdy-2 (PubMed:17179093). Regulates the secretion of granular material found in the amphid channel and in controlling osmoregulation in the amphid pocket (PubMed:17179093). {ECO:0000250|UniProtKB:G5EGP4, ECO:0000250|UniProtKB:Q29466, ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:17179093}.
|
Caenorhabditis elegans
|
G5EEL0
|
LIDB1_CAEEL
|
MYGHHPDYGYGNYGHPPPFAGPESSNSHYGMPPSQGTNSQNNMMMRSQATEPQPIGNTVSPLEFRIHDMNRRLYIFSSTGVSENDQQQWWDAFSHEFFDDDCKLWFVIGSEPVAFASRERYIINRQFIPKFFRSIFDSGMRELQYVLRGPSRECTLANGSQAYENENVLQITRYDQSSQFEVNTEGKLYVEFAPFDEVMNYRIKAWTLELKRSNEFVYNQNTADYRVEAQNPEQENKPRMGFFKSTFNLMTMLKILDPMQSIMSSAKSAPAITPREVMKRTLFQHHQVRQQNMRQQQLNQQMMIPAPEPEKPKPARKRQRKPAANPRGSKKATAAAAAAAAAATNGVPPTVPTASPANNQQFPPNPMTSQFQQMSYPDVMVVGEPSMMGSEFGENDERTISRVENSQYDPNAMQMQSLGQGPNSSMNINGRNMMNQHHPGMQPPPGQQHMPPHSMGSQMPTSMHNPMHMPPGSMQGHGGMPPMPSTMANQMPPPNLPPHTMSNQMPNSRMPPMQGQMPPSGMPGQMSNPNMMGSGMPPMSMSSQMPGSMSNPMPNQMPGGMQMNQMPPPNYSQYTGGPPPQWPPPNSAMITG
| null | null |
locomotion [GO:0040011]; mechanosensory behavior [GO:0007638]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vulval development [GO:0040026]; protein localization to nucleus [GO:0034504]; synapse assembly [GO:0007416]; vulval development [GO:0040025]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; LIM domain binding [GO:0030274]
|
PF17916;PF01803;
|
2.10.110.10;
|
LDB family
| null | null | null | null | null | null | null |
FUNCTION: Binds to the LIM domain of LIM domain-containing transcription factors (PubMed:10993673). Required for the blmp-1-mediated transcriptional activation or repression of several hypodermal genes, such as bed-3 (PubMed:32417234). Regulates sam-10 nuclear localization in PLM neurons (PubMed:21115607). Has a role in synaptic differentiation of PLM mechanosensory neurons (PubMed:21115607). Involved in gonadogenesis (PubMed:12736204). {ECO:0000269|PubMed:10993673, ECO:0000269|PubMed:12736204, ECO:0000269|PubMed:21115607, ECO:0000269|PubMed:32417234}.
|
Caenorhabditis elegans
|
G5EEL5
|
DBL1_CAEEL
|
MNDSVRTTTTISSTKSLVHSFQLSAILHLFLLISFTPMSAAADQHASHATRRGLLRKLGLEHVPVQTGPSIDVPQHMWDIYDDDNDVDWVRHYYPKEIIEDNEGFLLSYNLSLAARNAHNEEVTKATLKLRLRRNNKARRSGNISIYFFEDDINNDRFQIESRSVDNLTEWIDFDVTAAFLRRTNRISFFIDLPEDVEIEETQSSSLSSLPYARAQSAPLIVFSDLSEPSSVRRKRSAQTGNSERKNRKKGRKHHNTEAESNLCRRTDFYVDFDDLNWQDWIMAPKGYDAYQCQGSCPNPMPAQLNATNHAIIQSLLHSLRPDEVPPPCCVPTETSPLSILYMDVDKVIVIREYADMRVESCGCR
| null | null |
BMP signaling pathway [GO:0030509]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of cell size [GO:0045793]; positive regulation of DNA endoreduplication [GO:0032877]; positive regulation of gene expression [GO:0010628]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of organ growth [GO:0046622]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of cell morphogenesis [GO:0022604]; regulation of gene expression [GO:0010468]; regulation of lipid metabolic process [GO:0019216]; regulation of mesodermal cell fate specification [GO:0042661]
|
extracellular space [GO:0005615]
|
BMP receptor binding [GO:0070700]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Ligand for the serine/threonine-protein kinase receptor type-1 sma-6 which activates a TGF-beta-like signaling pathway (PubMed:24004951). Multifunctional protein that is involved in body size, male ectodermal patterning, innate immunity, lipid metabolism and neural plasticity (PubMed:10021351, PubMed:12176330, PubMed:23019581, PubMed:29162682, PubMed:9847238). Dose-dependent regulator of body size, probably influencing the sizes of some or all cells rather than their number (PubMed:10021351, PubMed:22189608, PubMed:9847238). Plays a role in patterning of male-specific genital sensilla (simple sense organs), known as rays, and mating-associated structures, spicules (PubMed:10021351, PubMed:9847238). Plays a protective role in response to infection by the Gram-negative bacterium S.marcescens, by activating expression of genes involved in innate immunity (PubMed:12176330). Regulator of lipid homeostasis, acting non cell-autonomously in the hypodermis; partly dependent on the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:29162682). Required for aversive olfactory learning of pathogenic bacteria in adults (PubMed:23019581). Involved in gland cell morphology, possibly via activation of a Smad-independent TGF-beta signaling pathway (PubMed:24690231). Required to oppose the autoregulation of expression of Runt-related transcription factor rnt-1. {ECO:0000269|PubMed:10021351, ECO:0000269|PubMed:12176330, ECO:0000269|PubMed:18158917, ECO:0000269|PubMed:22189608, ECO:0000269|PubMed:23019581, ECO:0000269|PubMed:24004951, ECO:0000269|PubMed:24690231, ECO:0000269|PubMed:29162682, ECO:0000269|PubMed:9847238}.
|
Caenorhabditis elegans
|
G5EEM0
|
NH114_CAEEL
|
MTPQSSPSSSRDHVCLVCQDFASGYHYGVPSCVGCKTFFRRTIMKKQKYICQFEGNCPVDKTIRCACRYCRFEKCLSVGMDRNALQQNRDPIGYTKRTRRPKKELKTTSDCSSDEGASTPPSVSPLQLSPPPISPLLFQAAPLKPRRCILQTLAEREKCANDLRLSEYLPIRSLHEALCSKALLNDTAFLEKWGQPSERHQIFDLRFVNHDDYHYWHERDWFLLTEYAKTFDVFEALDYQDKAELVRHAAITVPVLVQVWNSPDYGPDTIVFPDGAYFDRTPEPTRPAGLNRKKYQMLDLVLKPFRDLQLDATEFAAFKAVTFLNPDADISLPARKLVNNERVRITKQLYGYMAMKDDVDTAIERFARLVLMGTSMSKMACESKEAVWIADFFENIGFSAFARQLFFGDTTSVVAHKL
| null | null |
cell differentiation [GO:0030154]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; S-adenosylmethionine cycle [GO:0033353]
|
nucleus [GO:0005634]
|
nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU004334, ECO:0000269|PubMed:18629017, ECO:0000269|PubMed:23499532}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor which may have a role in detoxifying dietary metabolites arising from bacterial tryptophan metabolism (PubMed:23499532). Required for fertility and involved in proper postembryonic germline development, especially germline stem cell (GSC) proliferation (PubMed:23499532). Required for activation of the methionine/S-adenosylmethionine (Met/SAM) cycle in response to low levels of SAM (PubMed:33016879). {ECO:0000269|PubMed:23499532, ECO:0000269|PubMed:33016879}.
|
Caenorhabditis elegans
|
G5EEM5
|
ZYG9_CAEEL
|
MSNWDYLDEVDILPKLPPNFDELRESKKWQERKEALEALLKVLTDNERLSTKASYAELIGHLQMVLAKDANINCQALAAKCIGKFATGLRAKFSSFAGPLLPVIFEKMKEKKPMLREPLVDCSNEVGRTMQSLETGQEDILAALAKPNPQIKQQTALFVARQLDLVVPAKQPKGFIKAVVPVFGKLTGDADQDVREASLQGLGAVQRIIGDKNVKNLLGDASSDEGKMKKIGEYAEKSTASFAEEQAKNAPPVAPTSSTPSASAASGDPSGGTATAVVSSGAPVAEADPWDFLDAFDVLSKMPDGFDTNIESKKWQERKEALEGLLQLITANPKLDPKANYGALVERLQKVLEKDANINVAALAANCITGIANGLRTKFQPFAVSVTPIIFEKFKEKKPTLRDPLVACIDAVVATTNLEAVGEIVLAALGKPNPSIKTQTDLFLQRCFMKLNSQTMPKKTLKTLIPSLIKHSGDSDSEVREASYAAMGAMMRAIGEKPSLQLLADIASDNLKMSKIKEFHQKALDEAGPAEIAEMVKSIHKADAPPAAAPPKKTAPPKKQPEDEEVVEEEDEPLKPPPGDKKKKVPVKENEENEPPVVAPKAELLLSDNEDKKQRIKEEKQLKLVKWNFQAPTDEHISQLQTLLGNQAKVSLMSQLFHKDFKQHLAALDSLVRLADTSPRSLLSNSDLLLKWCTLRFFETNPAALIKVLELCKVIVELIRDTETPMSQEEVSAFVPYLLLKTGEAKDNMRTSVRDIVNVLSDVVGPLKMTPMLLDALKSKNARQRSECLLVIEYYITNAGISPLKSLSVEKTVAPFVGDKDVNVRNAAINVLVACFKFEGDQMWKAAGRMADKDKSLVEERIKRTGVKPGSGVVTSPPTGGPKILVPQQQGSVVRRPASRSRTREPEPEEVQSDTFTIRQDTMPPKTSSRYALRDDVFSSAMGRLDGTQVITPPQPVNGWSNNTFQMKRTNSSSSISSIDTSDQIQRSINNISSSLADVAQDAMFQVTYVLNQPEQRHLVDRRADLVFRASAAQLDLVIEEFNAGRDVSGTMDACTQMLFILMGGVETEHGLEPLNASPDTVKAIISSVLRCIIQIGNTESGYGMARSLNRLAMRLIYRVELSNLLCGLILAMTESLQMNTGITELVSKLSSKWCDELEKRRAQLRASDIVDSFNAFYVCALTELKMDISDSHILIVDNYLERVILQQGDVVLDAARRLSRPHMHLTSMINKILQMMRERKIDPIMPGTLEARMPQEDEAVVVRSGVQVSIDNILRDTSMAVKHIEQLNILIASSDRSWNEYMEYLKNNPMGELIKELVGECSRKKRIDFNLSHVVKSSMAVFKAMAATGPVQEEGRITPTDINRMDTMIVGTPLSRGDATITRARGNMIRPKRTTLSRDQMANIRHTLDRVKNH
| null | null |
cell division [GO:0051301]; centrosome duplication [GO:0051298]; embryo development ending in birth or egg hatching [GO:0009792]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; meiotic spindle organization [GO:0000212]; microtubule polymerization [GO:0046785]; microtubule-based process [GO:0007017]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]; spindle organization [GO:0007051]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; microtubule plus-end [GO:0035371]; mitotic spindle astral microtubule [GO:0061673]; mitotic spindle microtubule [GO:1990498]; spindle pole [GO:0000922]
|
microtubule binding [GO:0008017]; microtubule plus end polymerase [GO:0061863]; microtubule plus-end binding [GO:0051010]
|
PF21041;
|
1.25.10.10;
|
TOG/XMAP215 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10085292, ECO:0000269|PubMed:12011109, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:9606208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10085292, ECO:0000269|PubMed:12011109, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:16971515, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:9606208}. Cytoplasm {ECO:0000269|PubMed:10085292, ECO:0000269|PubMed:12011109, ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:9606208}. Note=Cycles between cytoplasm and centrosome during mitosis in a cell cycle- dependent manner. Centrosomal recruitment requires tbg-1.
| null | null | null | null | null |
FUNCTION: Plays a major role in organizing microtubules and spindle poles during mitosis and meiosis in one-cell stage embryos (PubMed:16971515). Required for default nucleus positioning in oocytes (PubMed:16971515). {ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:15866166, ECO:0000269|PubMed:16054029, ECO:0000269|PubMed:16971515, ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:2249759, ECO:0000269|PubMed:3949074, ECO:0000269|PubMed:6684994, ECO:0000269|PubMed:9606208}.
|
Caenorhabditis elegans
|
G5EEM6
|
TAB1_CAEEL
|
MGDDGFLDQYPANTDAGIGTVHSCRYSKQKNPVQNNDFLSCSMCIHNGPIKLYGIFSGFNGGDSTAKFVMNRLVYEIFGENPITPTLLPYQVVEEFKRKFENVAERYLLMNTDDLNNRLLKLEEQSETGNNAVSEINQKIRQGTTAIVVMIINQDLYVLNCGNSLAIAMNSENVVQLNSNLHNNDNPLEIVRIKGLGINPETVLNPTRAIGDLQRTHLFEETEAFKNAKGPPVISTPDVQYTKIDPSWRHLVLISDGVVQNLKEVEVENIPTEVSVRLIEDHTVTSTAQALVDSFARKHRDAYTMSDDKNFCISNHREEMTVIYVKLEEDYQAALYEQFDSAISTMESTNATLYEPCSTPYVDATNFNSGKNYEKMKKLLLTRPSK
| null | null |
endodermal cell fate specification [GO:0001714]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of stress-activated MAPK cascade [GO:0032873]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
mitogen-activated protein kinase binding [GO:0051019]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein kinase activator activity [GO:0030295]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00481;
|
3.60.40.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Involved in the Wnt signaling pathway by regulating mom-4 kinase activity. {ECO:0000269|PubMed:10391246, ECO:0000269|PubMed:11323434}.
|
Caenorhabditis elegans
|
G5EEM9
|
PLA1_CAEEL
|
MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTEDESEVSTPTAVGLPIGTSTPDGDETPTQPDPNGKYTMAQTKDADLSRPSGLPSNGNPGSSTTVPPASKSGPVAPPRPSGTPVAPQRNRRRKVTELKCSEVRWFFQEPKGTLWNPFNGRDSIMLEIKYRKEKGIELDEAMQEIYDESLTHYKMEMKDEPEIENGNIGMEQEKPMVVVMNGQYKVNKDNSKIDPIYWKDDSKEIRRGSWFSPDYQPLEMPLSDQIEKNHLQCFRNQMIPEGTTVFSKSETSNKPVLAELHVDGYDIRWSSVIDISLHQKGNAILRYLWAKSTPLRRGYEKEADWNDAAAEISHLILVVHGIGQKGYENLIAQNANQVRDGVVSAMEKVYPEEKSRPMFLPVEWRSALKLDNGLTDNITIPKMSSMRASLNSTAMDVMYYQSPLFRTEIVRGVVSQLNRTYKLFKANNPQFNGHVSVFGHSLGSVICYDVLTQYSPLMLFDKYVTKSIDEYLKRDDTNASEEARKALEAMKLAREQLRDNLEGGIHKLLVTKEEQLEFKVKYLFAVGSPLGVFLTMRGGESTDLLSKATNVERVFNIFHPYDPVAYRLEPFFAPEYRHIRPIKLFSNTDLRARASYENLPLDVYKHYLKKLKNLNKAKKNKDDKTADARSGGDDENEDEDECDSDEDARSGCSSPRSMTPPPFETAAANAAAAAKETKAVKKGWFSFGTSSNPKKTQSTASLGSVNATSTENIEFAKEAAEELPLAEKILGSGVRVPHRIDFQLQPALTEKSYWSVLKSHFAYWTNADLALFLANVLYCKPLKPEEAKPTWA
|
3.1.1.111; 3.1.1.4
| null |
phosphatidylcholine catabolic process [GO:0034638]; phosphatidylinositol catabolic process [GO:0031161]; phosphatidylinositol metabolic process [GO:0046488]; regulation of asymmetric cell division [GO:0009786]; regulation of protein localization [GO:0032880]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; phosphatase complex [GO:1903293]
|
calcium-independent phospholipase A2 activity [GO:0047499]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylserine binding [GO:0001786]; phospholipase A1 activity [GO:0008970]; phospholipase activity [GO:0004620]
|
PF02862;
| null |
PA-PLA1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 2-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+) + hexadecanoate; Xref=Rhea:RHEA:66708, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72835, ChEBI:CHEBI:167448; Evidence={ECO:0000305|PubMed:20668164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66709; Evidence={ECO:0000305|PubMed:20668164}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+); Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214; EC=3.1.1.111; Evidence={ECO:0000269|PubMed:20668164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213; Evidence={ECO:0000305|PubMed:20668164}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+) + hexadecanoate; Xref=Rhea:RHEA:43968, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75029, ChEBI:CHEBI:77342; Evidence={ECO:0000269|PubMed:20668164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43969; Evidence={ECO:0000305|PubMed:20668164}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:20668164}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000305|PubMed:20668164}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:23007400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:23007400}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:23007400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:23007400};
| null | null | null | null |
FUNCTION: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids, being phosphatidylinositol (PI) its major substrate. PI is a versatile lipid that not only serves as a structural component of cellular membranes, but also plays important roles in signal transduction through distinct phosphorylated derivatives of the inositol head group (PubMed:20668164). Catalyzes the hydrolysis of phosphatidylcholine at sn-2 position in vitro (PubMed:23007400). Regulates asymmetric division, an important property of stem cells in C.elegans, by controlling the subcellular localizations of beta-catenin (PubMed:18497747, PubMed:20668164). {ECO:0000269|PubMed:18497747, ECO:0000269|PubMed:20668164, ECO:0000269|PubMed:23007400}.
|
Caenorhabditis elegans
|
G5EEN4
|
GCK3_CAEEL
|
MSSSNLAGNTNTTTTSSAASAAAAHSAANASTITSEYSTTQTTTGTFNTDTLSSIGSTSTLHGSQPSQPPPPPPPQVSSPIAAAAAASAALVAQLNPADRWPTEPSAYKLDESIGVGATATVFTAYCLPRNEKVAIKCINLEKCQTSVDELSHEIQAMSQCNHPNVVSYYTSFIAQEELWVVMRLLNCGSMLDILKRKVKAIGKEQAQFGVLDEVSIATVLREVLKGLEYFHLNGQIHRDIKAGNILLADDGTIQIADFGVSGWLASSGGDLSRQKVRHTFVGTPCWMAPEVMEQVQGYDFKADIWSLGILAIELATGTAPYHKYPPMKVLMLTLQNDPPTLETNAERKDQYKAYGKSFKTLIRDCLQKDPAKRPTASELLKYSFFKKGKDKKYLVHTLIENLASVPVVAHHSSKKVASGKLRKDAHGNWEFEYDSPQESDDDSDLEDEEREKKKKKASASASGAGAAGAAGGATGGAASGAPSAQEGGGATTPCPETLNMVLRVRNQQRELNDIKFDYTKSADTVEGIAHELVTAELIDCHDLVIVAANLQKLIDFAESKSDRRSITFALNSGVHANEIPDERTLTGFAQISLLD
|
2.7.11.1
| null |
cell differentiation [GO:0030154]; epithelial tube morphogenesis [GO:0060562]; hyperosmotic response [GO:0006972]; meiotic cell cycle [GO:0051321]; multicellular organismal-level water homeostasis [GO:0050891]; phosphorylation [GO:0016310]; positive regulation of gene expression [GO:0010628]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF12202;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Phosphorylated at Thr-280 and Ser-419 probably by wnk-1; phosphorylation results in weak activation (PubMed:18049475). Predominantly autophosphorylated at Thr-32 and Ser-190 and weakly autophosphorylated at Thr-13 and Ser-405 in vitro (PubMed:20595048). {ECO:0000269|PubMed:18049475, ECO:0000269|PubMed:20595048}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20595048}. Nucleus {ECO:0000269|PubMed:20595048}. Note=Localizes in the nucleus in intestinal cells. {ECO:0000269|PubMed:20595048}.
|
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:18049475, ECO:0000269|PubMed:20595048}; 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:18049475, ECO:0000269|PubMed:20595048};
| null | null | null | null |
FUNCTION: Plays a role in osmotic stress responses by regulating ion homeostasis and by controlling cell volume via the phosphorylation-mediated inhibition of the chloride channel clh-3 (PubMed:15684092, PubMed:17596296). In addition, increases gpdh-1 translation upon osmotic stress, likely downstream of wnk-1 (PubMed:23076791). Involved in several developmental processes including the tubular formation of the excretory canals, the formation of the intestine and the progression through larval stages (PubMed:20595048). In addition, required for germ line development by controlling meiosis and chromosomal segregation during spermatogenesis. By controlling clh-3 activity, may regulate the development of the excretory canals and fertility (PubMed:18049475). {ECO:0000269|PubMed:15684092, ECO:0000269|PubMed:17596296, ECO:0000269|PubMed:18049475, ECO:0000269|PubMed:20595048, ECO:0000269|PubMed:23076791}.
|
Caenorhabditis elegans
|
G5EEQ5
|
REF1_CAEEL
|
MVLISTPPPAYAHNRKTSQEKKRRDEINAKIKELQLLIQNESDNEKMTQGDVLNRAVEVVSRMETESPGPSSNPNRKGFFDGFRSIESLTYSFIKSLGVNSDVCQDFVQRAKQFFDRERSSLLSTVSGKSKRRSESEILHSSMSYRSQSSSPSTSESGITIDRKEVKKNREQDRRDRQGEAFDALKNFIIENKLMTSHQVEKMQRLNTLDIIIAYIQNKKHNFVSRSDQEQSLYAHAIAEGKKTAKNIAFQFFKSDRHLVVRCADLEKFFEFSLSPKPLFGFPSMPIPIPPPSFPIFPFRPFPFFPMPMAPMATSPKSQQSPSYSLDSPPPSSDTSSSSIETPSTPNENSNSNPKASRKSKLFRPWE
| null | null |
anterior/posterior pattern specification [GO:0009952]; epidermal cell fate specification [GO:0009957]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail tip morphogenesis [GO:0045138]; neuron development [GO:0048666]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16376329}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor (PubMed:11311160, PubMed:15935776, PubMed:16376329). Binds 5'-TGCCACGTGTCCA-3' in vitro, probably via the E-box motif 5'-CA[TC][AG]TG-3' (PubMed:15935776). Acts in embryonic development in a Notch-dependent manner, perhaps as a direct target of transcriptional regulator lag-1 in the Notch signaling pathway (PubMed:15935776, PubMed:16376329). Also acts in embryonic development in a Notch-independent manner (PubMed:15935776). Plays a role in both Notch-dependent and -independent pathways in the execution of neuronal lineage decisions in the embryo (PubMed:16376329). Also involved in regulating cell fate leading to formation of neuronal structures known as postdeirids (PubMed:11311160). Involved in the pattern of cell fusion with a large syncytium known as hyp-7, during larval development, in hermaphrodites (PubMed:11311160). Plays a role in regulating the activity of homeobox protein mab-5 in Pn.p cells (PubMed:11311160). {ECO:0000269|PubMed:11311160, ECO:0000269|PubMed:15935776, ECO:0000269|PubMed:16376329}.
|
Caenorhabditis elegans
|
G5EET5
|
CBXH1_CAEEL
|
MSRQNPVRSTRGNSLRAREAQQAQDAPLFQESSSNVFVVEKVLNKRLTRGGSEYYIKWQGFPESECSWEPIENLQCDRMIQEYEKEAAKRTTRKRRYSPQPSTSSSAELQPSTSDEWAGKTLKTIIGITKAPGELHFLCKFSDDSVHLIPLREANVRFPSQVIKFYETRLVLQGVSPTIPGGMS
| null | null |
chromatin organization [GO:0006325]; germ cell development [GO:0007281]; gonad development [GO:0008406]; negative regulation of gene expression [GO:0010629]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vulval development [GO:0040027]; nematode larval development [GO:0002119]; positive regulation of growth rate [GO:0040010]; regulation of cell differentiation [GO:0045595]; regulation of gene expression [GO:0010468]; reproduction [GO:0000003]
|
heterochromatin [GO:0000792]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; methylated histone binding [GO:0035064]
|
PF00385;PF01393;
|
2.40.50.40;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:26476455}. Note=Partially co-localizes with histone H3 tails methylated at 'Lys-9' (H3K9me3) and 'Lys-23'(H3K23me2) in chromatin (PubMed:26476455). Localizes to distinct nuclear foci, not overlapping significantly with hpl-2, in embryonic cells (PubMed:16905130, PubMed:26476455). {ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:26476455}.
| null | null | null | null | null |
FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes (By similarity). Involved in epigenetic repression (By similarity). Probably does not act as global transcriptional repressor (PubMed:23028351). Plays a role in linking epigenetic regulation with the innate immune response (PubMed:22083954). Acting in concert with chromobox protein homolog hpl-2 and histone H1 protein his-24, involved in reproduction, somatic gonad development, male tail development and vulval cell fate decisions; perhaps as a result of modulating expression of Hox genes mab-5 and egl-5 (PubMed:16905130, PubMed:23028351). Role in growth and somatic gonad development is antagonized by histone-lysine N-methyltransferase set-2/SET1 (PubMed:17967446). Required for larval development, acting redundantly with hpl-2 (PubMed:16905130, PubMed:26476455). Plays a role in the formation of the vulva and in fertility, acting together with a CoREST-like complex, and hpl-2 (PubMed:16905130, PubMed:26476455). {ECO:0000250|UniProtKB:Q13185, ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:17967446, ECO:0000269|PubMed:22083954, ECO:0000269|PubMed:23028351, ECO:0000269|PubMed:26476455}.
|
Caenorhabditis elegans
|
G5EET6
|
EFA6_CAEEL
|
MAKVASSGAEEALATIDGAPRRNVKKSEAFVMSGDVLISLNRNVSSTYAKLLGDQLPPGTTVASSIHPHQLSRATASAGVSFPSMNRNGAAAQKLSRLPVPVSTSQIERRGSLARKTSEESSPTAIRMLKTAPIERMESTDVEESEEETVMMTTDEKENQKKPNENDDEVMVVDEEQFIVVSNDMKSPNEEIVAKSLRSAMFTMPTDNHHHSYNSSPQISTLSPHLRSNGDGPSRSPVYDDVDDDLNGSLDAKDMSNNSHQQSFRSPENYSEKDTPSKHSVVTIDGSGVSNHYDQDGMFSHVYYSTQDTTPKHGSPSLRKQIFESRTTPNTAASNSSASASPSLHATSESRGATGGVSLRSAESSNLNQTAVPSTSTNSVGGEREAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRVELRGESSARERLLRVFSARYLECNPAIFDSLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNIAHTGCTFKREMLKTLFQSIKDNAISLQNSAKNSTANGSVASTSRRQPQQIYEVDPDSVVEYYSGFLMRKYVRETDGGKTPFGRRSWRMVYARLRGLVLYFDTDEHPKATSRYASLENAVSLHHALAEPAPDYKKKSFVFRVRIAHGGEILFQTSNQKELQEWCEKINFVAAAFSSPTLPLPVTSKPETAPMPRLPRIPCLAPITKQLSTHEARVAELNEMIEIVSQSVSPNQPQQLITDRWVLLSFEKRRYSTYINVLRRSLEARKASSATTMNIMMTPTRRQQQNQKPVVSEDRLSYTDAVNGAAAH
| null | null |
microtubule depolymerization [GO:0007019]; mitotic nuclear membrane disassembly [GO:0007077]; negative regulation of axon extension involved in regeneration [GO:0048692]; negative regulation of axon regeneration [GO:0048681]; negative regulation of mitotic spindle elongation [GO:1902845]; regulation of ARF protein signal transduction [GO:0032012]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of mitotic centrosome separation [GO:0046602]; response to axon injury [GO:0048678]
|
cell cortex [GO:0005938]; microtubule minus-end [GO:0036449]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; phospholipid binding [GO:0005543]
|
PF15410;PF01369;
|
1.10.1000.11;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:17676955, ECO:0000269|PubMed:21076413, ECO:0000269|PubMed:26339988}. Cell membrane {ECO:0000269|PubMed:26339988}. Note=Present throughout the embryonic cortex during the first embryonic mitosis, but at reduced levels in the posterior cortex (PubMed:21076413). Localizes to the plasma membrane of the soma and processes of neurons. Localizes to the cellular cortex in the steady (uninjured) state. Following injury, transiently relocalizes to the sites marked by the microtubule minus end binding protein ptrn-1 together with tac-1 (PubMed:26339988). {ECO:0000269|PubMed:21076413, ECO:0000269|PubMed:26339988}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide exchange factor for arf-6 (By similarity). Involved in response to injury in mechanosensory neurons. Inhibits axon regrowth via microtubule dynamics, possibly by inducing axonal microtubule catastrophes (PubMed:21943602, PubMed:26339988). Limits microtubule growth near the cellular cortex of early embryonic cells (PubMed:21076413). {ECO:0000250|UniProtKB:Q9NYI0, ECO:0000269|PubMed:21076413, ECO:0000269|PubMed:21943602, ECO:0000269|PubMed:26339988}.
|
Caenorhabditis elegans
|
G5EEU2
|
SET25_CAEEL
|
MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPNNERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGWTCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFWIYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACENGTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGFGVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRFINHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF
|
2.1.1.-; 2.1.1.366
| null |
methylation [GO:0032259]; negative regulation of gene expression, epigenetic [GO:0045814]
|
heterochromatin [GO:0000792]; nuclear lamina [GO:0005652]
|
double-stranded DNA binding [GO:0003690]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone methyltransferase activity [GO:0042054]; metal ion binding [GO:0046872]
|
PF00856;
|
2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22939621}. Chromosome {ECO:0000269|PubMed:22939621}. Nucleus lamina {ECO:0000269|PubMed:22939621}. Note=Colocalizes with its own product and hpl-1 in foci in the peripheral region of the nucleus, in a manner dependent on H3K9me3. {ECO:0000269|PubMed:22939621}.
|
CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:22939621}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000269|PubMed:22939621};
| null | null | null | null |
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using mono- and dimethylated H3 'Lys-9' as substrate (PubMed:22939621, PubMed:28428426). Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina (PubMed:22939621). Required for small-RNA-induced H3K9 methylation (PubMed:26365259). Together with met-2, protects and stabilizes repeat-rich genomic regions by suppressing transcription-induced replication stress through methylation of H3K9 (PubMed:27668659). Suppresses transcription from various repetitive genomic elements through methylation of H3K9; exposure to moderately raised temperature reduces methylation by set-25 leading to de-repression of transcription of repetitive elements lasting at least 3 subsequent generations, despite culture at lower temperatures (PubMed:28428426). May play a role in transgenerational transmission of environmental information (PubMed:28428426). {ECO:0000269|PubMed:22939621, ECO:0000269|PubMed:26365259, ECO:0000269|PubMed:27668659}.
|
Caenorhabditis elegans
|
G5EEU3
|
AEX1_CAEEL
|
MREEALESICAALSISFTEDPDHLESIIDRFSEIFKVKDHLNQLRKKCEKFQTFTLEIRPVGSSNCTENVYAYIIESETCRQLELKPTGTTKLEIGSDKNVSLKFGLSQKKDSTTSKKGLSRSASLLKKLKFSDKKNLDELKISIFPLDIAVRKNINLGSGKSTLLEMKLIRNDHRNMIQCLEFDDFLEMTRSFHEWQAQISESELYDGSLGDPTFSMFYSIAFFFEIPSFVLKLTEMTCFLVWDDEMKKLDERALADVSLKMTACESEVDLQHPLLSPALSYLNDCTCNTIRCILVPFSTEPFFPPVSPSRLKSINVALKLIADICVLDVWDEFENLANPSNFLSSELKKLLESSAERYGESLKKQEFNELCRTILNLWMSLSNESQPYYIFFHQFDINYIGAAMLKLDKYLAESIQISLKCQLDLLNLRIPTELENFTKTTMRLFVTLRNLLNMVEAFHLPECQLFHFEEWFTDISVFWTYSWREVTLQMVERTITLDEDGDSVKYGARRPLPAGLYSFLCIQKGISDDLARLEFTFPHHLVVCAASVVNIMCQNINAYARKLFSEAMRNHEEKASRLVRATNGIEQAMCFVEEGYRRFAQFQRLEEYVDVDDLSAVRSTSIRLLKSTRDTCEIQVSTLLSHFVNLKTDIVLKIAKNLCADGKESNSGLKSYMRELASSERIESILECCYGLVDDVRCLLLPNCFKLSTQHFATSLEQQIRKNIRQKQPAEYYSNIYVGFLNILIFKRLKQMYLKFQIALKYIYEFLEIEDRKDIELLSNLHLNSFSTKDLILSYYDSLCEKIDRTRFGNAPHVDVHISYVKMVDEDTISIQIKLIKMSPIEWIDVISDRVDYFVRLELFPKILFPSNKFESPTTNPMPQSTRPQWKQLFEIRVPLECFFLRGACLAISVFDHERFIDRLVGRGFISLHSVPQASEEKPTQRLQVPLLPNDFSDQNNVFYQLLKTRACRDSIAKEFIETRTRRHQRIRALQHYIRINRNRVGHMLLG
| null | null |
defecation [GO:0030421]; egg-laying behavior [GO:0018991]; exocytosis [GO:0006887]; lipid transport involved in lipid storage [GO:0010877]; locomotion [GO:0040011]; male mating behavior [GO:0060179]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of defecation [GO:2000294]; positive regulation of intestinal lipid absorption [GO:1904731]; positive regulation of triglyceride transport [GO:1905885]; protein localization to synapse [GO:0035418]; regulation of muscle contraction [GO:0006937]
|
exocytic vesicle [GO:0070382]; secretory vesicle [GO:0099503]
| null |
PF00168;
|
2.60.40.150;
|
Unc-13 family
| null | null | null | null | null | null | null |
FUNCTION: Involved in retrograde signaling from post-synaptic cells to pre-synaptic neurons, probably by regulating vesicle exocytosis in post-synaptic cells (PubMed:11804572, PubMed:19028454, PubMed:2323555). Acts in muscles, to regulate the localization of synaptic vesicle fusion protein unc-13 likely during vesicle exocytosis and thus regulate retrograde signaling at the neuromuscular junction (NMJ) (PubMed:11804572). Regulates anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP) (PubMed:11804572, PubMed:19028454, PubMed:2323555). Probably by regulating DMP, plays a homeostatic role in the uptake of triglycerides (PubMed:25849533). Regulates locomotion (PubMed:11804572). {ECO:0000269|PubMed:11804572, ECO:0000269|PubMed:19028454, ECO:0000269|PubMed:2323555, ECO:0000269|PubMed:25849533}.
|
Caenorhabditis elegans
|
G5EEV2
|
TRR1_CAEEL
|
MDPAMASPGYRSVQSDRSNHLTELETRIQNLADNSQRDDVKLKMLQEIWSTIENHFTLSSHEKVVERLILSFLQVFCNTSPQFIAENNTQQLRKLMLEIILRLSNVEAMKHHSKEIIKQMMRLITVENEENANLAIKIVTDQGRSTGKMQYCGEVSQIMVSFKTMVIDLTASGRAGDMFNIKEHKAPPSTSSDEQVITEYLKTCYYQQTVLLNGTEGKPPLKYNMIPSAHQSTKVLLEVPYLVIFFYQHFKTAIQTEALDFMRLGLDFLNVRVPDEDKLKTNQIITDDFVSAQSRFLSFVNIMAKIPAFMDLIMQNGPLLVSGTMQMLERCPADLISVRREVLMALKYFTSGEMKSKFFPMLPRLIAEEVVLGTGFTAIEHLRVFMYQMLADLLHHMRNSIDYEMITHVIFVFCRTLHDPNNSSQVQIMSARLLNSLAESLCKMDSHDTFQTRDLLIEILESHVAKLKTLAVYHMPILFQQYGTEIDYEYKSYERDAEKPGMNIPKDTIRGVPKRRIRRLSIDSVEELEFLASEPSTSEDADESGGDPNKLPPPTKEGKKTSPEAILTAMSTMTPPPLAIVEARNLVKYIMHTCKFVTGQLRIARPSQDMYHCSKERDLFERLLRYGVMCMDVFVLPTTRNQPQMHSSMRTKDEKDALESLANVFTTIDHAIFREIFEKYMDFLIERIYNRNYPLQLMVNTFLVRNEVPFFASTMLSFLMSRMKLLEVSNDKTMLYVKLFKIIFSAIGANGSGLHGDKMLTSYLPEILKQSTVLALTAREPLNYFLLLRALFRSIGGGAQDILYGKFLQLLPNLLQFLNKLTNLQSCQHRIQMRELFVELCLTVPVRLSSLLPYLPLLMDPLVCAMNGSPNIVTQGLRTLELCVDNLQPEYLLENMLPVRGALMQGLWRVVSKAPDTSSMTAAFRILGKFGGANRKLLNQPQILQVATLGDTVQSYINMEFSRMGLDGNHSIHLPLSELMRVVADQMRYPADMILNPSPAMIPSTHMKKWCMELSKAVLLAGLGSSGSPITPSANLPKIIKKLLEDFDPNNRTTEVYTCPRESDRELFVNALLAMAYGIWNKDGFRHVYSKFFIKVLRQFALIGVLEYIGGNGWMRHAEEEGVLPLCLDSSVMVDALIICLSETSSSFIIAGVMSLRHINETLSLTLPDIDQMSKVPMCKYLMEKVFKLCHGPAWYARSGGINAIGYMIESFPRKFVMDFVIDVVDSIMEVILGTVEEISSGSADSAYDCLKKMMRVYFIKEEGQEEENLTLATIFVSAISKHYFHSNERVREFAIGLMDHCMVHSRLAPSLDKFYYRFKEFFEPELMRVLTTVPTMSLADAGGSLDGVQNYMFNCPDGFDFEKDMDMYKRYLSHLLDIAQTDTFTLNQRNAFKKCETCPSHFLPPFPITTHIDSMRASALQCLVIAYDRMKKQYIDKGIELGDEHKMIEILALRSSKITVDQVYESDESWRRLMTVLLRAVTDRETPEIAEKLHPSLLKVSPISTIIIATFGASYIRNISGAGDDSDSDRHISYNDIMKFKCLVELNPKILVTKMAVNLANQMVKYKMSDKISRILSVPSSFTEEELDDFEAEKMKGIRELDMIGHTVKMLAGCPVTTFTEQIIVDISRFAAHFEYAYSQDVLVNWIDDVTVILNKSPKDVWKFFLSRESILDPARRSFIRRIIVYQSSGPLRQEFMDTPEYFEKLIDLDDEENKDEDERKIWDRDMFAFSIVDRISKSCPEWLISPNSPIPRIKKLFSETEFNERYVVRALTEVKKFQEEIIVKRMTEHKYKVPKLILNTFLRYLRLNIYDYDLFIVIASCFNGNFVTDLSFLREYLETEVIPKVPLQWRRELFLRIMQKFDTDPQTAGTSMQHVKALQYLVIPTLHWAFERYDTDEIVGTAPIDDSDSSMDVDPAGSSDNLVARLTSVIDSHRNYLSDGMVIVFYQLCTLFVQNASEHIHNNNCKKQGGRLRILMLFAWPCLTMYNHQDPTMRYTGFFFLANIIERFTINRKIVLQVFHQLMTTYQQDTRDQIRKAIDILTPALRTRMEDGHLQILSHVKKILIEECHNLQHVQHVFQMVVRNYRVYYHVRLELLTPLLNGVQRALVMPNSVLEKFSWQTRRHAVEICEMVIKWELFRTLKTDHIISDEEALEVDKQLDKLRTASSTDRFDFEEAHNKRDMPDAQRTIIKEHADVIVNMLVRFCMTFHQNSGSSSTSQSGNHGVELTKKCQLLLRAALRPSMWGEFVSFRLTMIEKFLSIPNDNALRNDISSTAYANTIQNAQHTLDMLCNIIPVMPKTSLMTMMRQLQRPLIQCLNNGAQNFKMTRLVTQIVSRLLEKTNVSVNGLDELEQLNQYISRFLHEHFGSLLNCRNLSGPVLGVLGAFSLLRTICGHEPAYLDHLMPSFVKVMERAAKEHLAYVANSQDGNMVKNFFPDVAELLCACMELVRPRVDHISMEIKRSIVGGIIAELIIKSNHDKIIQTSVKLLGAMISTQDMEFTILTVLPLLVRIQSIIVTKFKNCKDLIADYLVVVITVFENSEYRNSEAGSRLWEGFFWGLKSSDPQTREKFSIVWEKTWPHMATVDIAHRMKYIMQNQDWSKFKHAFWLKFALWGMLRTIAKRPTDPNNKRKKVILLNCATPWRTIEYAAKLKDQPMEVETEMKREEPEPMEVDEKDSQDDSKDAGEPKEKEKLTLELLLAGQQELLDEASNYDFADALDTVSQITFALNENQVTSKMWVVLFKSFWSSLSQSEIEDFTALVVPFMSSGVHNNYQTGVQDSVLAVWLEAVGDAVHLPSRLIEFISSKHECWHTGIRLLENHIWTIPKQLNNTLLREMKVAPGLAGDIETLESLGTLYNEISEFDQFAAIWERRAVFPDTMRAMSAMQLGDMELAQSYLEKSMSSTYETLAPTINPNNTSNSEKHVSPIIDKEYDHWMEMYITNCSELLQWQNVADVCNGKDMQHVRGLINAASHIPDWNVVEECKSQIAGCIPPSFHLDYTLFNLMSTVMRMNENSSPTHMKERCKIAIQECTEAHISRWRALPSVVSYGHVKILQAMNLVREIEESTDIRIALLEAPSNKVDQALMGDMKSLMKVFRNRTPTTSDDMGFVSTWYDWRNQIHGMMLQRFEYWDKVGLNVAATGNQSIVPIHSMAQAQLAVAKHAKNLGFHNLTKDLLNKLAGLTAIPMMDAQDKVCTYGKTLRDMANSAADERVKNELLCEALEVLEDVRIDDLQKDQVAALLYHRANIHSVLDQAENADYTFSAASQLVDLQNSVTTTGIKLMKNWGHHLYKRFFSTTVCKETGNNFGRQALACYFIAARVDNDIKARKPIAKILWLSKHLNACGSHEVMNRVIKKQLHSLNLFNWLYWLPQLVTDVRYKPNSNFVLILCKMAAAHPLQVFYHIREAVSVDDIDSVLEEDYTDEQMSMDVSDEDCFADDPPFDRILKICLKYRPTDIRVFHRVLKELDEMNETWVERHLRHAICLKDQMFKDFSEQMDATFNEMQYSEDVTMMTLRWRKQLEEDLVYFQQNYNLDFLEIRNKRKMIVTKGCMGVEKSQIMFEKELSQVFTEPAGMQDEFDFVTNMTNMMVSQLDIHAVDAPRPQGYIRIVLDWIRAIRRRFDRLPRRIPLESSSPYLARFSHRTGCIEMPYDLLNVLRAKNHTLMASNQTGQYISMLSRFEPNFEIVIKGGQVIRKIYIRGQTGKSAAFYLKKSVQDEPTNRVPQMFKHLDHVLQTDRESARRHLHAPTVLQMRVGQKTTLYEVASVQPYAMPPDCTRNYPASQIDIVHPYDVLTATFNGSYYPDDMVLHFFERFAQSSSSIGQPLPTPTNQDGTVAPPRLTEAHHIKNIIYEDFARDMIPFRLLYDYLTARYPDPVMYYAMKKQLLHSLAVLSTIEYHCNLTPMGPDQMMMTMNTGVLSNPSYRFEIRGGRSLHDIQHFGHEVPFRLTPNLSILVGVAQDGDLLWSMAAASKCLMKKEPEVIMRPLVWDEFANNTDCDKSRLQVFACHASNSYINGVASKLRNTNSADAKLRKDDCVSLISRAKDSDNLARMPPTYHAWF
| null | null |
cell differentiation [GO:0030154]; DNA repair [GO:0006281]; negative regulation of vulval development [GO:0040027]; positive regulation of growth rate [GO:0040010]; regulation of DNA-templated transcription [GO:0006355]; reproduction [GO:0000003]; spermatogenesis [GO:0007283]
|
condensed chromosome [GO:0000793]; histone acetyltransferase complex [GO:0000123]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; SAGA complex [GO:0000124]
| null |
PF02259;PF20175;PF20206;
| null |
PI3/PI4-kinase family, TRA1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15068795}. Chromosome {ECO:0000269|PubMed:15068795}. Note=Localized to condensed chromosomes during pachytene and diakinesis stages of meiosis I in germ cells. {ECO:0000269|PubMed:15068795}.
| null | null | null | null | null |
FUNCTION: Influences germ cell fate in hermaphrodites (PubMed:24098152). Acts downstream of tra-2 and tra-3 and through the Tip60 histone acetyltransferase complex to regulate germ cell fate decisions (By similarity). Required for spermatogenesis and embryonic development (By similarity). Acts with tra-2 to promote expression of fog-3 and control male tail development (By similarity). Involved in the negative regulation of vulval development (PubMed:15068795). {ECO:0000250|UniProtKB:A8WTE8, ECO:0000269|PubMed:15068795, ECO:0000269|PubMed:24098152}.
|
Caenorhabditis elegans
|
G5EEV9
|
SID2_CAEEL
|
MPRFVYFCFALIALLPISWTMDGILITDVEIHVDVCQISCKASNTASLLINDAPFTPMCNSAGDQIFFTYNGTAAISDLKNVTFILEVTTDTKNCTFTANYTGYFTPDPKSKPFQLGFASATLNRDMGKVTKTIMEDSGEMVEQDFSNSSAVPTPASTTPLPQSTVAHLTIAYVHLQYEETKTVVNKNGGAVAVAVIEGIALIAILAFLGYRTMVNHKLQNSTRTNGLYGYDNNNSSRITVPDAMRMSDIPPPRDPMYASPPTPLSQPTPARNTVMTTQELVVPTANSSAAQPSTTSNGQFNDPFATLESW
| null | null |
endocytosis [GO:0006897]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; RNA transport [GO:0050658]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}; Single-pass type I membrane protein {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}. Cytoplasm {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}. Note=Localizes to the apical membrane of intestinal cells and also to punctate cytoplasmic structures. {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558}.
| null | null | null | null | null |
FUNCTION: Plays a role in RNA-mediated gene silencing by mediating endocytic uptake of double-stranded RNA (dsRNA) ingested from the environment into intestinal cells from the intestinal lumen. Selective for dsRNAs of at least 50 bp. Required for avoidance behavior induced by small RNAs derived from pathogenic bacteria such as P.aeruginosa (PubMed:32908307). {ECO:0000269|PubMed:17381285, ECO:0000269|PubMed:17563372, ECO:0000269|PubMed:22902558, ECO:0000269|PubMed:32908307}.
|
Caenorhabditis elegans
|
G5EEW6
|
SIG7_CAEEL
|
MAVLIETTLGDLIIDLFVKERPRCSLNFLKLCKKKYYNLNQFHSIERNYVAQTGDPTGTGKGGESVYSDMYGEQGRYFEREDLPKMRHTRMGIVSFVNNGDNMLGSQFFITLGENLDYLDDQHTIFGQVTEGLETLEKLNEQLADTNNRPFKDIRISHTIVLDDPFDEDARISFPPRSPSPTYEMLVKTDQIALDEKEDEDEGKTAEEIAEELQQREMAEQAQILEMVGDLKDADEVPPENVLFVCKLNPVTTDEDLEIIFSRFGKINNCEIVRDRRSGDSLQYAFIEFDNAKSCEQAFFKMDNVLIDDRRIHVDFSQSVSQNYKYKPKSQQQEAPKRRQSPQRRPEVKRSHQRSPSPRRRRSPSPKKDKKRDYRREPARRRRSSDNHRDRDRSYRDNNRDRRDNHRDSDRDRRRHDRSPDRRRDRR
|
5.2.1.8
| null |
nematode larval development [GO:0002119]; positive regulation of gastrulation [GO:2000543]; positive regulation of oocyte development [GO:0060282]; positive regulation of vulval development [GO:0040026]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; RNA binding [GO:0003723]; RNA polymerase II complex binding [GO:0000993]
|
PF00160;PF00076;
|
3.30.70.330;2.40.100.10;
|
Cyclophilin-type PPIase family, PPIL4 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:27541139}. Chromosome {ECO:0000269|PubMed:27541139}. Note=Co-localizes with transcriptionally active chromatin in all autosomes of mitotic and meiotic nuclei in germ cells. In transcriptionally inactive diakinetic oocytes, diffusely localized in the nucleoplasm. {ECO:0000269|PubMed:27541139}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000250|UniProtKB:Q08752};
| null | null | null | null |
FUNCTION: Probable PPIase that accelerates the folding of proteins (By similarity). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in RNA polymerase II (RNA pol II)-mediated transcription elongation, and in primary transcript splicing, including co-transcriptional trans-splicing, in association with the catalytic subunit of the RNA pol II complex ama-1 (PubMed:27541139). Also plays a role in the regulation of elongation-dependent phosphorylation of ama-1 to control transcription (PubMed:27541139). Involved in the transcription of several genes during embryogenesis and in particular, of genes related to developmental processes such as gastrulation, and also regulates transcription in germ cells from embryogenesis to adulthood (PubMed:27541139). {ECO:0000250|UniProtKB:Q08752, ECO:0000269|PubMed:27541139}.
|
Caenorhabditis elegans
|
G5EF15
|
POS1_CAEEL
|
MADNDFLSGEAIMVFKKEILDSHSDFTRSLSHQSASPEAYDQENVFSQDFQPFMKQDKETQNSASQPTSEQSLANRDPCTVPDDLREEMMRQRRKEDAFKTALCDAYKRSQACSYGDQCRFAHGVHELRLPMNPRGRNHPKYKTVLCDKFSMTGNCKYGTRCQFIHKIVDGNAAKLASGAHANTSSKSPARNAAAHNHSLFVPQGSTDRSMDLNQSLPIRQSDLVRAFARATRLDVSGYNSTAQLAQYFESQFQRIQQLSSHHH
| null | null |
cell fate specification [GO:0001708]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic pattern specification [GO:0009880]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of translation [GO:0006417]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; P granule [GO:0043186]
|
metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; poly(U) RNA binding [GO:0008266]; single-stranded RNA binding [GO:0003727]; transcription corepressor activity [GO:0003714]
|
PF00642;
|
6.10.250.3220;4.10.1000.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9834181}. Note=Localized to P granules in the germline blastomeres P1, P2, P3 and P4. {ECO:0000269|PubMed:9834181}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that coordinates cell fate specification and differentiation during early embryogenesis (PubMed:23034181, PubMed:9834181). Binds to a consensus pos-1 recognition element (PRE) consisting of the sequence 5'-UA(U 2-3)RGD(N 1-3)G-3', where R is any purine, D is A, G, or U, and N is any base (PubMed:18952820, PubMed:23034181). The PRE motif is found within the 3' untranslated region of many maternal transcripts required for early development (PubMed:18952820). Binds to the 3' untranslated region (UTR) of Notch receptor homolog glp-1, thereby repressing glp-1 translation in the posterior blastomeres in the embryo (PubMed:12702662, PubMed:23034181). Binding to glp-1 3' UTR excludes cell fate regulator gld-1 binding to an overlapping binding site in the glp-1 3' UTR (PubMed:23034181). Binds to the neg-1 3'UTR thereby opposing neg-1 expression and cytoplasmic polyadenylation of the neg-1 mRNA poly(A) tail promoted by gld-2 and gld-3 (PubMed:26096734). By inhibiting the cytoplasmic lengthening of neg-1 mRNA, restricts the accumulation of neg-1 protein and promotes endo-mesoderm development in anterior blastomeres (PubMed:26096734). Essential for germline specification (PubMed:9834181). {ECO:0000269|PubMed:12702662, ECO:0000269|PubMed:18952820, ECO:0000269|PubMed:23034181, ECO:0000269|PubMed:26096734, ECO:0000269|PubMed:9834181}.
|
Caenorhabditis elegans
|
G5EF33
|
MIG13_CAEEL
|
MTKLLIALILFSICWKPYSAEPIASFFDGLDSRNECKARLDRRLTGFSGLLYSHSKYGQEPYNTSRNCVLMLVAPIGYSIRVRALQFDVASTENARTCEKDTLHVFDHETTLDPESYAPARIDDITSPGPIIGQFCGHFENRILNTSSHNALTLWWHSNPNGSNSKGFKLHWGSFRVSKTGNCVTGEFSCGNGECIPIESACDRFADCSNGEDLIHSRQMAANCQNIELDPLTTVSGVFVLLFSATIILSLCGFIMFVCCLCKCLKSTIPIKGASSHTTTTTATDYKPDPPQFYPPSPPKMPPPSAASSYTPRLHHHFEGPLVPSETSAFHSSNRMQNHYSVNSDINGDYTYVRNDVHRNLL
| null | null |
positive regulation of cell migration [GO:0030335]
|
axon [GO:0030424]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]
| null |
PF00431;PF00057;
|
4.10.400.10;2.60.120.290;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10412978, ECO:0000269|PubMed:23784779, ECO:0000269|PubMed:27780040}; Single-pass type I membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:10412978}. Cell projection, axon {ECO:0000269|PubMed:10412978, ECO:0000269|PubMed:26762178}. Cell projection, dendrite {ECO:0000269|PubMed:26762178}. Note=Localizes to the leading edge of migrating Q-neuroblasts. {ECO:0000269|PubMed:27780040}.
| null | null | null | null | null |
FUNCTION: Probable receptor that acts as an upstream signaling protein to promote the guidance, migration and positioning of the right Q neuroblast (QR) and its descendants along the anteroposterior body axis, and also the anterior migration of BDU interneurons during larval development (PubMed:10412978, PubMed:15750187, PubMed:22293500, PubMed:23784779, PubMed:26022293, PubMed:27780040, PubMed:8898225). Associates with and recruits the downstream components tyrosine kinase abl-1 and the tyrosine kinase adapter protein sem-5 to the leading edge of migrating Q neuroblasts and their descendants to activate signaling through the two parallel wve-1 and wsp-1 pathways, respectively, and direct migration along the anteroposterior body axis (PubMed:27780040). Involved in cytoskeleton dynamics regulating the organization of the actin cytoskeleton at the leading edge of migrating cells to ensure correct Q cell polarity and promote migration (PubMed:23784779, PubMed:27780040). Role in cytoskeleton organization may be by activation of the wve-1 and wsp-1 pathways which recruit the Arp2/3 complex to the leading edge of migrating cells (PubMed:27780040). Plays a role in regulating the asymmetric distribution of the actin cytoskeleton-binding protein cor-1 in Q neuroblasts which is required for the anterior migration of QR neuroblasts (PubMed:23784779). {ECO:0000269|PubMed:10412978, ECO:0000269|PubMed:15750187, ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:23784779, ECO:0000269|PubMed:26022293, ECO:0000269|PubMed:27780040, ECO:0000269|PubMed:8898225}.
|
Caenorhabditis elegans
|
G5EF48
|
FLD1_CAEEL
|
MRQLAELLTDLLGPVPTMFLWVIVSFAFFRALQFIVRWYLFGKWTWPNFNFFDIRNRIRRRRRGGQEAENTENPPENEAEAGEQVEQEPEPDSRDLSAIPPNKKWRISNECVSLFHSVISGLWAAYALLYYKQLVQDLVNYRCDVAINLVLMSAGYLFHDLVDLLVNEQSARIIELLFHHVVVLSAFAVTMFFNRFLGVVVFGLLMELNSIFLHSRSLLNLYGVDKKSPSFRIIALLNMVTLFAFRLCVSAYLVYFVVVSIPDLEWYVSIINGLVIASLASTNTVLTYRLLAADGLLGSRRTRRTPAATAETQVGDVESGPLRTQVEDEDHHTIGVQTIHGTTEDATQTV
| null | null |
membrane assembly [GO:0071709]; phospholipid homeostasis [GO:0055091]; plasma membrane organization [GO:0007009]; regulation of membrane lipid distribution [GO:0097035]
|
plasma membrane [GO:0005886]
| null |
PF03798;
| null | null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30509349}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Regulates the composition and fluidity of the plasma membrane (PubMed:30509349). Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity (PubMed:30509349). Does not appear to have any effect on LCPUFA synthesis (PubMed:30509349). {ECO:0000269|PubMed:30509349}.
|
Caenorhabditis elegans
|
G5EF53
|
SWSN4_CAEEL
|
MSGRPAFEQFTAQPPQPAGEVVAQQAGDGAQGQELTISKLENAITSMEEQGLQNDHRHAKAVLLKQKLQSGLPDAVPGQENGGNQQITPAQLNQLRAQVSAYRLLARNEQVPANLIADAVMLRPKVTTLLPEPYEYPGEAENGEKLPYDLMKIFNLHQIRCNRPTTISVPSGIDPVGMLKQRENMIQNRIGLRMKLLNNLPADIPDHMKLKAEIELRALRLVNLQTQVRSEVMACLKRDTTLETALNPYAYRRTKRQSLREARVTEKLEKQQKMEQERKRRQKHTDLMQAIIQHGKEFKEYHRNNLLKMAKSRKAVMTYHQNNERERKKDEIRNEKLRMQKLMQEDEEGYRALLDEKKDQRLVYLLQQTDEYVDSLCSLVRQHQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTGKALTGDQAPKTEEIEFWLETHPEYEIVPRDQLSDDEEEEEEEAPVEPEEEKDDQYAGMDEETKAKMILEKARNEEDEYDQKTKKQMADYYATAHKIKEKVVKQHTTMGGGDPNLLLKPYQIKGLEWMVSLYNNNLNGILADEMGLGKTIQTISLVTYLMEVKQNNGPYLVIVPLSTLSNWQNEFAKWAPSVTTIIYKGTKDARRRVEGQIRKGAFNVLMTTYEYVIKEKALLGKIRWKYMIIDEGHRLKNHNCKLTLMLNGFFHAQHRLLLTGTPLQNKLPELWALLNFLLPSIFSSCGTFEQWFNAPFATTGEKVELNQEETMLIIRRLHKVLRPFLLRRLKKEVESQLPDKTEYVIKCDQSALQKVIYRHMQKGLLLDAKMSSGARSLMNTVVHLRKLCNHPFLFPNIEDSCRAYWKVNEVNGTDLMRVAGKLELLDRILPKLKATGHRILMFFQMTSMMNIFEDFLNFRRYTYLRLDGSTKPDERGDLLTQFNAPNSDLFLFMLSTRAGGLGLNLQTADTVIIFDSDWNPHQDMQAQDRAHRIGQKKEVRVLRLITANSVEEKILAAARYKLNVDEKVIQAGKFDQRSTGAERKQMLEQIIQADGEEEEEEEVPDDETVNQMVARSEEEFNIFQSMDIDRRREEANQLHRKPRLLEEHEIPDDILKLSFDYEEMERAREEGREVVDQTPNQRRRRREVDYSSDLLSDEQFMKQVEEVEDENNQAVAERKKQRKRKMAGLDENDDSMDDVVLQHKKKKTDPELAEKINEMLDVILEYKNEDGELIADVFQTLPTRKELPDYYQVISKPMDFDRINKKIETGRYTVMEELNDDMNLLVNNAQTYNEEGSEIYVSSETIGKLWKEQYDKFMNPPKPVEEPVKKKEPSTPSTSSSRPSTSGTPSVSDLQRTQQATAQQMLMLMTHMQSLPPAQAQQFQQALMTQTGGNQALMLQYMQSAMLAQRAQASTKVTPKKDEKKETSSSVKTEEAKKDDEPSTSSASAPPPKKKKESEDSEDPMEEDEEEEIIGQKKEPASSRRKSRPTRRFSNEDEEEEDDE
|
3.6.4.-
| null |
chromatin remodeling [GO:0006338]; gonad development [GO:0008406]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]
|
nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]
|
ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; hydrolase activity [GO:0016787]
|
PF07533;PF00439;PF00271;PF07529;PF08880;PF00176;
|
1.20.5.170;3.40.5.120;1.20.920.10;3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11030341, ECO:0000269|PubMed:27207389}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology) (By similarity). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain (PubMed:34473995). Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad (PubMed:24402584). Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23 (PubMed:27207389). Required during mitosis for asymmetric cell division of T blast cells (PubMed:11030341). {ECO:0000250|UniProtKB:P51532, ECO:0000269|PubMed:11030341, ECO:0000269|PubMed:24402584, ECO:0000269|PubMed:27207389, ECO:0000269|PubMed:34473995}.
|
Caenorhabditis elegans
|
G5EF60
|
STIM1_CAEEL
|
MGRVSWIIALYLTINVVIVVNGDRVTRNVEVTAEEEKIRDKLGYEAIRDIHRDMDDDHSGSIDRNESTGFMKEDMQMRGSERTRRENKFHGDDDAITVDDLWEAWFESIERTWTNERLVEWLINDVNLPSIVEAVKAKKIDGKILPRFASPNSDFLNKELGIKSSVYRQKLRLNSLDVVLFGYKDNNNRTKDILLAFLALLLTSLIFLYVRQKQKAQQKVNELSNKLTELKCMETEFEDVQKMLNDERSKRSISDGVVNHTEMENLRVQLEEAERRLEANSNGSQAPLALQPLLRRTCENEMAFLEKQRQDCFKEMKEAIEMVDRLQKKQGSVLSSLKLATGAASTSDQVDSKIFALKSRMEKIHTLTRETQERWLQIESLCGFPLLYLNETEHINRSIASSHFYNKSHEGSSSSGSISNAHSNPNAVNSNFVKKVSPPIPPSQQTANLRFVPTEQSDSIHSEDTSPIVEDVAISRSLTQDLAEADMQSIVSGSTNGSGSVAALKKRKGIFPKLFRRNTSKSSSLGGTSN
| null | null |
intracellular calcium ion homeostasis [GO:0006874]; ovulation [GO:0030728]; positive regulation of engulfment of apoptotic cell [GO:1901076]; positive regulation of smooth muscle contraction [GO:0045987]; reproduction [GO:0000003]; store-operated calcium entry [GO:0002115]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; intracellular organelle [GO:0043229]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
calcium channel activity [GO:0005262]; calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]
|
PF07647;PF16533;
|
1.10.238.180;1.10.287.3550;1.10.150.50;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}; Single-pass type I membrane protein {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}. Note=Localizes to intracellular puncta in the anterior intestine and reticular structure in the posterior intestine. {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}.
| null | null | null | null | null |
FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as a Ca(2+) sensor which upon Ca(2+) depletion, activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, orai-1. Essential for Ca (2+) and IP3-dependent contractile activity of gonad sheath cells and spermatheca. Essential for fertility. Does not play a role in posterior body wall muscle contraction (pBoc) rhythmicity, intestinal cell oscillatory Ca(2+) signaling or intestinal ER Ca(2+) hemostasis. {ECO:0000269|PubMed:16966474, ECO:0000269|PubMed:17218360}.
|
Caenorhabditis elegans
|
G5EF76
|
LIN22_CAEEL
|
MTSFLCSDTEIESDGGISRCKKIKNKPLMEKKRRARINKSLSQLKQILIQDEHKNSIQHSKWEKADILEMAVEYLQQLRSAQPCSLSPSTSSISTPPTPKEEIRNIKVPLNPIASFLNPMMQQYVAYQQLAQLSMYTQLFNNPAGVPLRADAGVTAQSPELAEKLKIEDRSRV
| null | null |
anterior/posterior pattern specification [GO:0009952]; epidermal cell fate specification [GO:0009957]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron differentiation [GO:0045665]; nematode male tail tip morphogenesis [GO:0045138]; Notch signaling pathway [GO:0007219]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; N-box binding [GO:0071820]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor (PubMed:29108019, PubMed:9247331). During development, required for cell fate specification, probably by promoting or repressing expression of genes involved in specific cell fate (PubMed:29108019, PubMed:9247331). Involved in specifying lineages derived from the epidermal stem cells of the lateral ectoderm, known as seam cells (PubMed:29108019, PubMed:9247331). Modulates symmetric divisions of seam cells, perhaps in concert with the Wnt signaling pathway (PubMed:29108019). May repress expression of homeobox genes mab-5, egl-5 and lin-39 (PubMed:9247331). {ECO:0000269|PubMed:29108019, ECO:0000269|PubMed:9247331}.
|
Caenorhabditis elegans
|
G5EF96
|
UNC40_CAEEL
|
MILRHFGFILIILTVYLSSTHATTRKHHRRSIDNDARNLGFQFVMEPRRNVTVMESSSHLLECSYVLAHERLVHDVRIEWKRDGVLLSERTSSRIKVMSNGSLWIESVSSAEEGTYQCAVHVTTKSDQTSDTWTFLSRKATLRLADLAKFELQAIDRTLAKGQPTAFHCLINSKPTPTAVWLHNDEPIVNGGEYHILPVSNTLEISSTQSRHEGTYRCTVEGAGKRRSSQTARLTVTTETVSNELVFITTPRLQVVEQGDEFLLECLVASLIRPQVRWLKDSRQIIVDGVRIRRVGVSSILVSRASIEDTGLYTCRASNNDDSIDRAVSVEVRAPPRITTRPTTKVAVETADVELECGTAAARPEARVNWYKNGEAIIGSEYFVIEPNRLRILGVVRADQAIYQCIAENDVGSEQASAQLLVDAPDSSSVAASSGVPMTSSAPLGLRSTSSGSRFINVEWDPPVQRNGNIMRYHIFYKDNLIDRERMINSSSTSATLTSLQPSTMYLIRVTAENEAGMGKFSDSLKVTTNKEQAVPGKVASLTTTATGPETIDIRWSPPSGGQPALRYKIFYSHDPLEKNEKETLITTSTTHYTLHGMDKYTGYQIRIEAEGSNGSGLSSDTVKVRTQSDEPSAPPVNIQAEADSSTSVRVSWDEPEEESVNGEITGYRLKYKTKARGAKGNTLVIDATAREYTMGNLEPNTQYLIRMAVVNHNGTGPFSDWVSIDTPGQDKEERTLGAPREIRPHAGIDYILVSWLPPADEQNLVRGYQIGWGLSVPDTETIRVTASTTQYKIARLHSERDYVISLRAFNNLGSGFPIYETVRTLSRETPSHFNEDSDSDDSDVGSSESTPVGVRAEAISATSIRVMWTESDETAFNTQYTVRYSTAVDGNQHRYVNSTETWATVEGLRPATEYEFAVRAVASNGQLSTWSMATRNRTLAAPPSSAPRDLTVLPAESGDPHSSSLHWQPPKYSNGEIEEYLVFYTDRASLADKDWTINYVAGDKLSHQVSNLLPKANYFFKIQARNEKGHGPFSSVVGYTPSGGAILSGKDRHNARGHGSAASGDTVSLVDQLQSLLHSNPLYLILLAAFALILILTLILIIMCCWKRSSGGGRKNGYQSGKKTSAGAGSGGGIGGLGGPPNDLWINGTGSHMRAGASDYMVDGLATAHLTAADIESPTPRYHHLQGQGTLTRSYHQSSQSLEGRQRTPQVVYTGTGRHQPIQRIDFESPYGSSSAIGSASTPPLPMQAPPSGPPTVIDGYRTLRGTPPNSSAANALRSFTQLAGATPPPPHSAASSSSRPTIIAAGGRQVPVGRATAQPRVNVANIYSPFASCSASSDAGESDKKSGECMEMRETTPIKSNTAGSSNGEKMNTNMNPSHSAEDLNAHLENLDTMLDDLQQLQHNLHFETSMDK
| null | null |
axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; brain development [GO:0007420]; cell projection morphogenesis [GO:0048858]; cell-cell adhesion [GO:0098609]; chemorepulsion of axon [GO:0061643]; dendrite morphogenesis [GO:0048813]; determination of left/right asymmetry in nervous system [GO:0035545]; distal tip cell migration [GO:0097628]; dorsal/ventral axon guidance [GO:0033563]; gonad morphogenesis [GO:0035262]; motor neuron axon guidance [GO:0008045]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of sensory neuron axon guidance [GO:1905490]; nematode male tail tip morphogenesis [GO:0045138]; netrin-activated signaling pathway [GO:0038007]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of locomotion [GO:0040017]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of synapse assembly [GO:0051965]; regulation of cell migration [GO:0030334]; regulation of dorsal/ventral axon guidance [GO:1905815]; regulation of mesodermal cell fate specification [GO:0042661]; regulation of motor neuron axon guidance [GO:1905812]; sensory neuron axon guidance [GO:0097374]
|
axonal growth cone [GO:0044295]; cell projection membrane [GO:0031253]; cell surface [GO:0009986]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
cell-cell adhesion mediator activity [GO:0098632]; netrin receptor activity [GO:0005042]; protein domain specific binding [GO:0019904]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, DCC family
| null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for netrin unc-6 required for asymmetric axon formation, axon guidance and cell migrations (PubMed:11454756, PubMed:16520734, PubMed:22426253, PubMed:8861903, PubMed:9473333). Required during axon formation, in response to unc-6, to initiate, maintain and orient asymmetric neuronal growth, and may signal via phosphoinositide 3-kinase (PI3K) (PubMed:16520734). Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:11454756, PubMed:22426253, PubMed:8861903, PubMed:9473333). Axon migration is mediated by the secreted unc-6, which promotes attraction of neurons and axons through binding to the unc-40 receptor, while repulsion requires both unc-5 and unc-40 receptors (PubMed:11454756, PubMed:22426253, PubMed:8861903, PubMed:9473333). Involved in dendritic morphogenesis; may act by localizing unc-6 at the tips of growing dendrites for interaction with unc-5 on the apposing branch to induce mutual repulsion (PubMed:22426253). Involved in the ventral-dorsal and anterior-posterior migration of gonadal distal tip cells (DTCs) along the body (PubMed:11454756). Involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail (PubMed:24004945). Positively modulates a TGF-beta-like signaling pathway, independent of its role in unc-6 mediated axon guidance, in association with RGM drag-1 (PubMed:24004951). Mediates attraction of muscle plasma membrane extensions, known as muscle arms, towards the secreted madd-4 guidance cue, enhanced by interaction with the coreceptor eva-1 (PubMed:25122090). {ECO:0000269|PubMed:11454756, ECO:0000269|PubMed:16520734, ECO:0000269|PubMed:22426253, ECO:0000269|PubMed:24004945, ECO:0000269|PubMed:24004951, ECO:0000269|PubMed:25122090, ECO:0000269|PubMed:8861903, ECO:0000269|PubMed:9473333}.
|
Caenorhabditis elegans
|
G5EFA2
|
BIR1_CAEEL
|
MAPGTKKKSDMAKFTFYKDRLMTFKNFEYDRDPDAKCTSQAVAQAGFYCTGPQSGKCAFCNKELDFDPEDDPWYEHTKRDEPCEFVRIGKLDDSELTINDTVRLSQTAMIMTKLFEHEMMINNLSNHSSSDALFDQLKKVPNTASTTKSNSRRGK
| null | null |
chromosome condensation [GO:0030261]; chromosome segregation [GO:0007059]; egg-laying behavior [GO:0018991]; inductive cell migration [GO:0040039]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic sister chromatid separation [GO:1901970]; regulation of multicellular organism growth [GO:0040014]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromosome passenger complex [GO:0032133]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; spindle midzone [GO:0051233]
|
metal ion binding [GO:0046872]
|
PF00653;
| null |
IAP family
| null |
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:10983970}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10983970}. Midbody {ECO:0000269|PubMed:10983970}. Note=In mitosis and meiosis, localizes to chromosomes during prometaphase and metaphase, localizes to both chromosomes and the spindle midzone during anaphase and disappears from chromosomes during telophase but remains at the spindle midzone. Persists at the cytokinetic remnant during cytokinesis. Also localizes to the chromosome of polar bodies during oogenesis. {ECO:0000269|PubMed:10983970}.
| null | null | null | null | null |
FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis (PubMed:10209096, PubMed:10983970, PubMed:12707312). The CPC complex has essential functions at the centromere in ensuring correct chromosome condensation, alignment and segregation (PubMed:10983970, PubMed:12707312). In the complex, required to direct the Aurora B/air-2 kinase to chromosomes (PubMed:10983970, PubMed:12707312). Also functions in spindle midzone formation and in the formation of polar bodies during oogenesis (PubMed:10209096, PubMed:10983970). Required for the localization of the kinetochore component hcp-1 to chromosomes (PubMed:10983970). Involved in the positive regulation of transcription (PubMed:12682297). Involved in the transcriptional regulation of collagen genes (PubMed:17116281). {ECO:0000269|PubMed:10209096, ECO:0000269|PubMed:10983970, ECO:0000269|PubMed:12682297, ECO:0000269|PubMed:12707312, ECO:0000269|PubMed:17116281}.
|
Caenorhabditis elegans
|
G5EFC3
|
KCNAG_CAEEL
|
MLDACSFNRFDSNRSSARRFSRRGSDYFGDKGISMDERIVLNVGGVRHETYQATLKKIPATRLSRLTPSLANFDPLLNEYFFDRHPAVFAMILNYYRTGKLHYPTDVCGPLFEEELQYWGLDASDTEPCCWMQLLHAKDTQETLAVLDRMDADHEDDPQLREQDTMKKFGWEEDYFQGKRTRWMKLKPQMWSLFDEPYSSQAAKLIAGISVLFIFISIFSFCLKTHQSFRLPVLIGQNITMPGGVVQPSIERVSTEPLPIFGQIEMLCNIWFTLELIIRFVFCPSKIRFFKSPLNMIDLVATLSFYADAMMVRVVEDEPKDVVEFLSMIRIFRLFKLTQHHQGLQILIHTFRASAKELILLVFFLILGIVIFAALVYYAEKMEANPNNQFQSIPLGLWWAICTMTTVGYGDMTPHTSFGRLVGSLCAVMGVLTIALPVPVIVSNFAMFYSHNQARDKLPKRRRRVLPVEQIRLQARRHAAVLEPSASQGGLGGGQAIRRRNMPILIDQNCCDEENHNHKHREKSENSDEGTNSSSTTGVDTVVKLGPSETAITTTIIS
| null | null |
monoatomic ion transmembrane transport [GO:0034220]; potassium ion transmembrane transport [GO:0071805]; protein homooligomerization [GO:0051260]
|
axon terminus [GO:0043679]; dendrite membrane [GO:0032590]; neuronal cell body membrane [GO:0032809]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076]
|
delayed rectifier potassium channel activity [GO:0005251]; voltage-gated monoatomic ion channel activity [GO:0005244]
|
PF02214;PF00520;
|
1.10.287.70;1.20.120.350;
|
Potassium channel family, C (Shaw) (TC 1.A.1.2) subfamily, Shaw sub-subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08510}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08510}.
| null | null | null | null | null |
FUNCTION: Voltage-dependent potassium channel involved in the excitation of muscles operating egg-laying and defecation. {ECO:0000269|PubMed:9247271, ECO:0000269|PubMed:9247272}.
|
Caenorhabditis elegans
|
G5EFD2
|
KSRA_CAEEL
|
MMQTQVASRAGYSNLPQFGAGIAQDIKTQAINNLKECLKLTTINRFLTSSYEEDAKSVERKIFSAVYQMTKIGLIDREKREINAIWFTFVGLSAQNIRHLEICSITDFNALFSITNQELRSLADRGRLDVETKRKLLQSTVILQNHWNAYHSRTSSGSTDEPSGQSTPAIVTPSPKFNVPSLSVTSAKMIQSSSMGFATTPKSPKTSSRLVHAIPHKWHRSTKFRFSGDAVCHFCQRPLGFGFLNAWEKCRSCKWKVHTQCKGRVGDSCGLTPDHLRFLFDKLIQENNGGMWKDPQSVPGSRSMNEPAFQFPDTAIDSSSSTNSSAPSTPALPAGISGNVSSLTAPYRSERKFLFPDTENYSVHNRLPILVISEGDHPTTTEIQQETENHNKSAAASMSGNIESEGTIVANHEDSTGSQEVDSEAAPSQEAVDKFNKRADGGFTWERHAWNMSTIRGPNAQASWNEVTIQFETIEFDKQAPIIGRGRFGKVLRGFHYGDVAVKVYTMEHISDASKKAEEFKLEVSAYKNTRHDNIALFLGYFMSDGQYGMVMSLSKGSQSLYTLLHVVREKLDLATTRKIAQQICQAVSYLHTKKILHKDLRSKNILLESKNKVVITDFGILSMKRLAHPKQKSGYLTSKFWTNYIAPELAMAMRTEYDEYECDDFPFSENSDVYAFGCVWFEMLTGALPYAGELPHQILFAKTQGIRPVLPNVKCTQELKELLVSCWNTAPQDRPTLTDINLKLTALPKKPRVNRSPSFPVMMKSYESTF
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
|
cell fate specification [GO:0001708]; defense response to Gram-positive bacterium [GO:0050830]; meiotic cell cycle [GO:0051321]; myoblast migration [GO:0051451]; nematode larval development [GO:0002119]; phosphorylation [GO:0016310]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of vulval development [GO:0040026]; Ras protein signal transduction [GO:0007265]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mitogen-activated protein kinase kinase binding [GO:0031434]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF07714;
|
3.30.60.20;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family
| null | null |
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:0000305}; 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:0000305};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which positively regulates Ras-mediated signaling probably acting at the level of let-60/ras or/and lin-45/raf. Involved in sex myoblast migration (PubMed:11882296, PubMed:8521513). Plays a role in responses to M.nematophilum-mediated bacterial infection by promoting tail swelling and preventing constipation (PubMed:15268855). Functions redundantly with ksr-2 in the Ras-mediated regulation of larval survival, the development of excretory canal and in mpk-1 phosphorylation in somatic cells (PubMed:11882296, PubMed:8521513). In addition, involved in determining vulval precursor cell fate during vulval induction independently of its kinase activity (PubMed:10409742, PubMed:11882296, PubMed:8521513, PubMed:8521514). Plays a role in egg-laying (PubMed:23900546). {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11882296, ECO:0000269|PubMed:15268855, ECO:0000269|PubMed:23900546, ECO:0000269|PubMed:8521513, ECO:0000269|PubMed:8521514}.
|
Caenorhabditis elegans
|
G5EFD4
|
HMT1_CAEEL
|
MGFSPFLDECRAEGLWPIGPSCNKIISFGVYTFFIVVNFIVLCIPNSNSANNNYRRMTDDDASSTSKLTISKILSICTIFAVICQSIFYFCFTFYFHPYTHLLLAFCVSKLFFWILSLCSFSKWRNQPSTPISLAFAFSAALLIHCIPLTDWKKYFEPTSKNRGDLTFYIIELALVTVVFFFTIVTGLFNFSGCSSRESAWNNLSKKVVTVAPYIWPTKSISLQLRVVFCLFLLIIGRLINVSLPILSKWIVDELATPDTFQYSLLFLATFLKFLQGNGAMGGFLNTVRTYLWIPIQQYTTRELEVELFKHLHSLSLRWHLSRKTGQVLRVMDRGTSSVNNILNYILFNVVPTIADIVIAVIFFFSAFNAYFGLIVFGTMALYLTVTISITEWRTQYIREANEKDNATSAIATDSLINYETVKYYGNEEFEVNRFKNAIESYQVTEWKTQASLAFLNCLQNAIIGIGMIGGSVFVVYMIVHEKTLTVGDYVLFTTYLLQLYTPLNFFGTIYRVIQKAFVDMENMFDLMNDEVEVKDLPHALPYTDPRGTISVKNLTFEYNTGLPVIKNISFEIGNGQTVALVGSSGSGKSTLIRLLFRLFESTEGSIEFDGIDVRNYTMHSLRQQIGIVPQDTVLFNDTIMYNIRFGRPDASDEEVIEAAKAAMIHEKITSLPEGYATMVGERGLKLSGGEKQRVAIARTILKKPQFIFLDEATSALDTPTERAIQKCLEKLCKSRTGVVVAHRLSTVVNADLILVLDKGIILERGNHKELLAQQGTYASMWEAQIAEQRAKSIELGEELP
| null | null |
cadmium ion transmembrane transport [GO:0070574]; cellular detoxification of cadmium ion [GO:0098849]; detoxification of cadmium ion [GO:0071585]; detoxification of copper ion [GO:0010273]; heme transport [GO:0015886]; response to cadmium ion [GO:0046686]; transmembrane transport [GO:0055085]
|
early endosome [GO:0005769]; late endosome [GO:0005770]; membrane [GO:0016020]; recycling endosome [GO:0055037]; vacuolar membrane [GO:0005774]
|
ABC-type heme transporter activity [GO:0015439]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadmium ion transmembrane transporter activity [GO:0015086]; heme binding [GO:0020037]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
| null |
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15840570}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:31053883}. Late endosome {ECO:0000269|PubMed:31053883}. Recycling endosome {ECO:0000269|PubMed:31053883}.
| null | null | null | null | null |
FUNCTION: May play a pivotal role in the detoxification of heavy metals such as cadmium but do not depend exclusively on phytochelatins (PC) synthesis. {ECO:0000269|PubMed:15840570, ECO:0000269|PubMed:31053883}.
|
Caenorhabditis elegans
|
G5EFD5
|
UNC71_CAEEL
|
MICASKITMLGLLVMCTLGGVLGKVDIRQTTANKAFMETMRADGYEVVHPFQIRDKNERIGIDTRNYFLKAQEHYSHVTIVIRSNQLGRLKLVLERNNFIFLNQTAFHKLDADGERVIQNRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGTTFGIWPLDGGDRNSRRHPHILYKSEWSQEAKCGSSMAHAVGQRRMKKHVHKHRSHHHEHNKKRDVSKRTKYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLSRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASGHIYHIQKDASILFTAGSFANQEVSNAAIRSICTARSAVIVKGVEQFATHWNGELLAQSIGHLLGLEHDTTACSCEPSPECVMRQQPGRVGGGGGSPFSWQFSKCSVARMHGIWQDGNIQCLLNKPFQVSELRECGNGVVDGSEECDCGSRENCQDPCCDPLTCTLRPHAQCAAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGHLIDGTVCGTDGQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQNTKGAEYANCGQRQADGTYHPCQIEDTRCGTLHCHSGSITPIDSSLKAFTFHFTENSHQIQCKSIASAAVGLTSDGTNCASGRVCVAGSCVEMSSVSSATACPTNNLALLCSGHGHCTTTARCVCFNGWSGVACDIRSNSSTYQGSMGFGEEGSGGSSQKSSERKTIMIPHLNIGTTLETATLFAILLGFGVFLLLCLVCLMLCYRRRSVVEIPKPSDEKDEESPDRQIKFGNMPSYREEKRKRKSNKKIYGALNRITEADERDSTSLRSRDSAGGSQQLVDRRNGAPVVVGGIRDPYAGEHIYAESSSNHLTRQFRGINSDGSYPLRSFGSWRSSAPISPASSSGQLTDVSTATTPLRLNKIGKFLKTLQSDDESPSPFSDHQSFTTGIGIGARLEQMQFGGGGDEELSAVEADHDVGSNTESSRGCEEPMDPGSWDSPTLVNGASSSSTSNNYNFRQSPSLFSDPFKLEMTNSMHN
| null | null |
cell-cell adhesion [GO:0098609]; membrane protein ectodomain proteolysis [GO:0006509]; plasma membrane fusion [GO:0045026]; proteolysis [GO:0006508]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF08516;PF00200;PF07974;PF01421;
|
3.40.390.10;4.10.70.10;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12783787, ECO:0000305|PubMed:8970152}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Involved in the migration of sex myoblasts (progenitors of egg-laying muscles), Q neuroblasts and BDU interneurons during development (PubMed:12783787, PubMed:22293500, PubMed:9073451). Involved in axon branching and guidance of neurons including GABAergic type D motor neurons (PubMed:12783787). Promotes sex myoblast migration and positioning independently of gonad attraction cues (PubMed:12783787, PubMed:9073451). May act downstream of mig-13 in order to promote the guidance, migration and positioning of Q neuroblasts and their descendants along the anteroposterior body axis (PubMed:22293500). Required for coordinated movements (PubMed:12783787). {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:9073451}.
|
Caenorhabditis elegans
|
G5EFD9
|
ADA10_CAEEL
|
MSSPIRNRLQLVVTLIFCLFFENVNGLNNFIDNFETLNYRATHVANQVTRRKRSIDSAASHYQEPIGFRFNAYNRTFHVQLHPIDDSLFHEDHMSDVDGGYADIKPSHFLYEGYLKDDPNSHVHGSVFDGVFEGHIQTGEGRRYSIDKAAKYFERDDRPTQYHSIIYRDDEINHRKWRVKRDAENLSEQMQGCGFSSRVRREMTDVQNSGESTDFFTNYMTMGGRSKRANTLRDHDGLYFVRTCSLYMQADHKLYEHIRMKEGNNDPIRTREEIVSLFYNHIKAVNEIYEGTNFNGIKGLHFVIQRTSIYTPDSCDRGRAKTDSDNPFCEENVDVSNFLNLNSQRNHSAFCLAYALTFRDFVGGTLGLAWVASPQFNTAGGICQVHQRYNEGSRGWVYRSLNTGIVTLVNYGNRVPARVSQLTLAHEIGHNFGSPHDFPAECQPGLPDGNFIMFASATSGDKPNNGKFSPCSVKNISAVLAVVLKSMPVDPTRNASPVGIGKRNCFQERTSAFCGNQIYEPGEECDCGFSQADCDQMGDKCCVPHEARGNGGPGPCKRKPGAQCSPSQGYCCNPDTCSLHGKNEEKICRQESECSNLQTCDGRNAQCPVSPPKHDGIPCQDSTKVCSSGQCNGSVCAMFGLEDCFLTEGKADELCFLACIKDGKCTSSVHLPEFSANRTNFLQNMRKDKPGLILHPGSPCNNYKGYCDIFRKCRSVDANGPLARLKNLLFNKRTIETLTQWAQDNWWVVGVGGLVFLVIMALFVKCCAVHTPSTNPNKPPALNIYQTLTRPGTLIRQHRQRHRAAAGSVPPGPGAQPRSGAASAPSRTTPSARPSAPPLVAPQVAVAVPPGVVGPPIPLIATHPGSSSSTPAVIVLEPPPPYTAADPGSAMGGPRRGHRKNKRQTSSDAAGSSGNGGKKKGK
|
3.4.24.81
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P78325}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78325};
|
cell fate specification [GO:0001708]; embryo development ending in birth or egg hatching [GO:0009792]; membrane protein ectodomain proteolysis [GO:0006509]; nematode male tail tip morphogenesis [GO:0045138]; Notch signaling pathway [GO:0007219]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of axon guidance [GO:1902667]; regulation of mesodermal cell fate specification [GO:0042661]; vulval development [GO:0040025]
|
basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle membrane [GO:0030659]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF21299;PF13574;
|
3.40.390.10;4.10.70.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes to the basolateral cell membrane in embryos. {ECO:0000269|PubMed:28068334}.
|
CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000250|UniProtKB:O14672};
| null | null | null | null |
FUNCTION: Metalloprotease (By similarity). Acts together with protease adm-4 and in a cell autonomous manner to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision and vulva precursor cell specification (PubMed:16197940, PubMed:9409830, PubMed:9428412). By modulating glp-1/Notch signaling, plays a role in germline development (PubMed:16197940). Probably by modulating BMP-like Sma/Mab signaling via the shedding of unc-40 ectodomain, involved in the regulation of body size and mesoderm development (PubMed:28068334). Probably by shedding ephrin efn-4, regulates axon guidance of SDQL neuron during development (PubMed:26903502). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:9409830, ECO:0000269|PubMed:9428412}.
|
Caenorhabditis elegans
|
G5EFE7
|
FUT8_CAEEL
|
MLKCIAAVGTVVWMTMFLFLYSQLSNNQSGGDSIRAWRQTKEAIDKLQEQNEDLKSILEKERQERNDQHKKIMEQSHQLPPNPENPSLPKPEPVKEIISKPSILGPVQQEVQKRMLDDRIREMFYLLHSQTIENSTKILLETQMISLMGLSAQLEKLEGSEEERFKQRTAITQRIFKSIEKLQNPKACSEAKTLVCNLDKECGFGCQLHHVTYCAITAFATQRMMVLKRDGSSWKYSSHGWTSVFKKLSKCSFDEAVGNTEAKPFAEPSPARVVSLGIVDSLITKPTFLPQAVPEQLLESLTSLHSHPPAFFVGTFISYLMRFNSATQEKLDKALKSIPLDKGPIVGLQIRRTDKVGTEAAFHALKEYMEWTEIWFKVEEKRQGKPLERRIFIASDDPTVVPEAKNDYPNYEVYGSTEIAKTAQLNNRYTDASLMGVITDIYILSKVNYLVCTFSSQVCRMGYELRQPSGADDGSKFHSLDDIYYFGGQQAHEVIVIEDHIAQNNKEIDLKVGDKVGIAGNHWNGYSKGTNRQTYKEGVFPSYKVVNDWRKFKFEALLD
|
2.4.1.68
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15604090}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15604090}; Note=May also use Ca(2+). The enzyme has substantial activity without divalent cations. {ECO:0000269|PubMed:15604090};
|
fucosylation [GO:0036065]; N-glycan fucosylation [GO:0036071]; protein N-linked glycosylation [GO:0006487]
|
Golgi cisterna membrane [GO:0032580]
|
alpha-(1->6)-fucosyltransferase activity [GO:0046921]; fucosyltransferase activity [GO:0008417]; galactoside 6-L-fucosyltransferase activity [GO:0046702]; glycoprotein 6-alpha-L-fucosyltransferase activity [GO:0008424]; metal ion binding [GO:0046872]
|
PF19745;
|
3.40.50.11350;2.30.30.40;
|
Glycosyltransferase 23 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|PIRNR:PIRNR000472}; Single-pass type II membrane protein {ECO:0000305}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:12985, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13532, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60651, ChEBI:CHEBI:137207; EC=2.4.1.68; Evidence={ECO:0000255|PIRNR:PIRNR000472, ECO:0000269|PubMed:15604090};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|PIRNR:PIRNR000472}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7.5. {ECO:0000269|PubMed:15604090};
| null |
FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans (PubMed:15604090). The addition is prevented if the GlcNAc residue is already fucosylated (PubMed:15604090). Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds (PubMed:20062796). {ECO:0000255|PIRNR:PIRNR000472, ECO:0000269|PubMed:15604090, ECO:0000269|PubMed:20062796}.
|
Caenorhabditis elegans
|
G5EFF1
|
ASD2_CAEEL
|
MDCDNGVVSEISDDKELLNLETVIPPPPNDSGHEFIGPSSGPPQVTITPSGVQSGSANGVSTSQQQQYSAEYLSQLLKDKKQLAAFPNVFHHLERLADEEINKVRVVLFQCEFSKESAPLPDAEGDSTVHTEKVFVPAKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGRGSMRDKKKEELNRGKPNWEHLSEELHVLIQCEDTENRAKVKLMRAVEEVRKLLVPAPEGEDDLKRKQLMELAIINGTYRSGTDQSALAAAQLAAVKHQQQPFAAALQAAALQRGVLPMMANGLSRSPTMAVCGAPIVMSPSGRASSAGATATSQAALIMQQQSQLHAANAGNAALQQQAALLQQQQAAEYQQLLLSQAGLYDFSAMQQQYAAVGQNAAVAAAQAQAQAQYGALAAAAAANSAGNQQYADYAGVDLTSQQSAHGGYYVRRWA
| null | null |
mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing [GO:0008380]
|
nucleus [GO:0005634]; P granule [GO:0043186]; ribonucleoprotein complex [GO:1990904]
|
mRNA binding [GO:0003729]; pre-mRNA intronic binding [GO:0097157]; single-stranded RNA binding [GO:0003727]
|
PF00013;PF16544;
|
1.20.5.4010;3.30.1370.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23071450}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that binds to the 5'-NACUAAY-N(1,20)-UAAY-3' consensus sequence in pre-mRNA introns to promote alternative splicing (PubMed:18230701, PubMed:20573244, PubMed:23071450). Required for mutually exclusive alternative splicing where it modulates the switch between mutually exclusive exons during pre-mRNA maturation (PubMed:18230701, PubMed:23071450). Involved in muscle-specific gene expression regulating the alternative splicing of genes such as let-2 and unc-60 to ensure that their respective isoforms are expressed in muscle (PubMed:18230701, PubMed:23071450). Promotes the removal of intron 10 from let-2 pre-mRNA to allow for the exclusive expression of the muscle-specific let-2 isoform (as opposed to the non-muscle-specific isoform expressed in embryos) in body wall muscles during late larval and adult stages of development (PubMed:18230701). Binds cooperatively with RNA-binding protein sup-12 to intron 1A of the unc-60 pre-mRNA to promote alternative splicing and expression of the muscle specific isoform of unc-60 (PubMed:23071450). {ECO:0000269|PubMed:18230701, ECO:0000269|PubMed:20573244, ECO:0000269|PubMed:23071450}.
|
Caenorhabditis elegans
|
G5EFF4
|
SEM4_CAEEL
|
MNELLAEMAAVSSRRKQSKPRRMSGEGDAMMSPIDLSTKSFDENNCEKGAGGALPLEDRSNILPHFSVPFANPQQFLSLCAQLGNSSSRNVSSTASTTSSCPIQSCSQSFSSPAALTWHVLDAHEDEQEIFSCDVCTTTFSNGQDIREHKCQKTLASRSTSVPPSTIPSSVCFLSTPTTPCLQFSINESIGTSEIREEDEEEDMDVEDGEHVANQLFGHLLQKSDDKSKMASLFNHAFPPFAAFPNMPPPFLMRQPFDPRADVFAAGRHDNDDDWEALMEISTSDEAEKIRALVGDKAVPTTDPNQCILCRRVLSCKSALQMHYRTHTGERPFKCKICQRAFTTKGNLKTHMGVHRSKHSFRGLPISLPPQLAAMHQHQHQIAPPQRIHIHNPPTSAASAAAAVAQIQASQQCPICQQRFLNAGELAVHITEHRNSLTQPPRVMPTPTTTRVQTFPFVPFFTTPPSLNATDMSTQFNLANILSAQLKNDSSPNTDTSSVEEKITRDDPPKMASLSPSNSSDSSSSVRQDILESSEFEEKLKKLEEPPILEQQVSTTPNPKNENPLLAMQKMWAETEPPPPRQMPVLSKHQCGVCFKHFSSSSALQIHMRTHTGDKPFKCDMCGRAFTTRGNLKVHMGTHSWQQSPSRRGRRIFDVASSVTEKPMLQSPILPTSGAPGASPLAMLGPNGLSGLEMMMMLWRTVCSVCQKVCQSPNELEQHLKEHLNNGSSAAPTPLASAATPPPS
| null | null |
mesodermal cell differentiation [GO:0048333]; muscle cell differentiation [GO:0042692]; myoblast fate specification [GO:0048626]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast differentiation [GO:0014016]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to oxidative stress [GO:0006979]; transdifferentiation [GO:0060290]; vulval cell fate determination [GO:0072326]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00096;PF12874;
|
3.30.160.60;
|
Sal C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor, involved in positive and negative modulation of transcription (PubMed:12835398, PubMed:28614700). Binds to multiple DNA sequence motifs in the regulatory elements of target genes, including homeobox selector egl-5 and LIM homeobox mec-3 (PubMed:12835398). Involved in cell-fate regulation in multiple lineages, including neuronal, mesodermal and vulval (PubMed:10926783, PubMed:12835398, PubMed:28614700, PubMed:8756352). Required to regulate the fate of PLM touch receptor neurons, acting via negative modulation of transcription of egl-5 and mec-3 (PubMed:12835398). May modulate gene expression by interacting with different transcription factors during neuronal and mesodermal cell development (PubMed:8756352). Promotes the proliferative sex myoblast (SM) fate, in a cell autonomous manner, acting via the SoxC transcription factor sem-2 (PubMed:28614700). Involved in vulval cell-fate determination, acting by regulating expression of homeobox protein lin-39, and may link lin-39 to incoming signaling pathways (PubMed:10926783). Plays a role in detoxification of reactive oxygen species (ROS), by regulating expression of transcription factor skn-1 and the phase II detoxification genes (PubMed:32718932). {ECO:0000269|PubMed:10926783, ECO:0000269|PubMed:12835398, ECO:0000269|PubMed:28614700, ECO:0000269|PubMed:32718932, ECO:0000269|PubMed:8756352}.
|
Caenorhabditis elegans
|
G5EFF5
|
DAF12_CAEEL
|
MGTNGGVIAEQSMEIETNENPDKVEEPVVRRKRVTRRRHRRIHSKNNCLTPPNSDDDPQMSTPDDPVIHSPPSIGAAPGMNGYHGSGVKLEESSGACGSPDDGLLDSSEESRRRQKTCRVCGDHATGYNFNVITCESCKAFFRRNALRPKEFKCPYSEDCEINSVSRRFCQKCRLRKCFTVGMKKEWILNEEQLRRRKNSRLNNTGTCNKRSQPGNQQSPQGPNQQPHLSPHHPGVAIYPPQPQRPLTINPMDNQMMHHMQANRPNAMPQLISPPGAQPYPLTSPVGSSASDSPPNRSLTMMHNGEKSPDGYDPNIMAHRAPPPSFNNRPKMDSGQVVLSTEEYKQLLSRIPGAQVPGLMNEEEPINKRAAYNCNGHPMPAETTPPYSAPMSDMSLSRHNSTSSGTEKNHMTHSTVSAIPGNSAQNHFDIASFGMGIVTATGGGDAAEEMYKRMNMFYENCIQSALDSPENQEPKPQEAMIPKEEYMTPTHGFQYQSDPYQVPPAERNINYQLNAAELKALDAVREAFYGMDDPMEQGRQMQSFLKANKTPADIMNIMDVTMRRFVKVAKGVPAFREVSQEGKFSLLKGGMIEMLTVRGVTRYDASTNSFKTPTIKGQNVSVNVDDMFAKLNANAQAQKAKCLEFFGFFDEEIKKNELAVYLVMLAVLFSVRSDPPMNENDVRIVTERHNHFMSLLNRYLESLFGEQARRIFERIPKALGLLNEIARNAGMLFMGTVRSGEAEELPGEFFKIK
| null | null |
cell differentiation [GO:0030154]; chemotaxis [GO:0006935]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; male mating behavior [GO:0060179]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of dauer larval development [GO:0061066]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of dauer larval development [GO:0061065]; regulation of development, heterochronic [GO:0040034]; regulation of nematode pharyngeal pumping [GO:0043051]
|
nucleus [GO:0005634]
|
(25S)-Delta(4)-dafachronate binding [GO:1902051]; (25S)-Delta(7)-dafachronate binding [GO:1902052]; DNA-binding transcription factor activity [GO:0003700]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270]
|
PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10859169, ECO:0000269|PubMed:15611047, ECO:0000269|PubMed:23990780}. Note=Diffuse expression during mitosis (PubMed:10859169). Increased nuclear accumulation upon infection by E.coli (PubMed:23990780). {ECO:0000269|PubMed:10859169, ECO:0000269|PubMed:23990780}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor which binds directly to response elements in target gene promoters (PubMed:10859169, PubMed:15314028, PubMed:15383841, PubMed:15489294, PubMed:15611047, PubMed:16626392, PubMed:19828440, PubMed:21814518, PubMed:9477318). Activity is modulated by binding of steroid hormone ligands that include dafachronic acids (PubMed:16529801). Regulates expression of genes involved in postembryonic development and the dauer diapause, in response to environmental cues (PubMed:10859169, PubMed:15383841, PubMed:15489294, PubMed:16626392, PubMed:19828440, PubMed:21814518, PubMed:9477318). Inhibits the expression of let-7 family members when bound to corepressor din-1s which is an isoform of din-1 (PubMed:19828440). Plays a role in controlling the timing of seam cell development during the larval stages (PubMed:21471153). Has a role in the immune response to bacterial infection, via regulation of let-7 miRNAs (PubMed:23990780). Controls expression of genes that promote the aerobic catabolism of fatty acids for reproductive growth (PubMed:25774872). May be involved in thermotolerance (PubMed:24957743). {ECO:0000269|PubMed:10859169, ECO:0000269|PubMed:15314028, ECO:0000269|PubMed:15383841, ECO:0000269|PubMed:15489294, ECO:0000269|PubMed:15611047, ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:16626392, ECO:0000269|PubMed:19828440, ECO:0000269|PubMed:21471153, ECO:0000269|PubMed:21814518, ECO:0000269|PubMed:23990780, ECO:0000269|PubMed:24957743, ECO:0000269|PubMed:25774872, ECO:0000269|PubMed:9477318}.
|
Caenorhabditis elegans
|
G5EFH8
|
CBS1_CAEEL
|
MIQNEVSATHGSTKKGITYNTILEAAQRPTPLVPLKKLKVEHQLQSDIYVKLEYLNIAGSLEDRTADKAFQFAEEIGVVRGDEVFVTAGGSAAISYATVAAVKGIKLTIYAPKGEFDLVDTVLHTLGVKTVELPFGTFAEARVQTDEAAQQKGVFSLNKFTTNAAFVANLQKTALEIEKAVNNKSIGKVGAVVIPLNTGAAAAGIAAYYKGIGEHGVRVVGVTCKKDTIPEMGLDLKNDLLQEYNVEKREVEEDEAYSFTRHLIGTEGIMAGPSSGAAVLEAIKLAKELPAGSTIVVVLMDGIRNYLRHFLDDDWITANKKDVVTRKDGPQPNSIYDPKVLVYDPTKLAGEWTQDPETKSWSHSEVEFNKFNPERPLVLDTVLDAIGKTPLVKLQHIPKAHGVKCNVYVKCEYMNAGGSTKDRIAKRMVEIAEKTGKPGKLVPGVTLIEPTSGNTGIGLSLASAVRGYKCIITMPKKMSKEKSIAMASLGSTIIRTPNEAGFDSPHSHIGVALRLKSEIQDAVVLDQYCNPGNPLAHYEETAEEIIYDMGDKHIDLVVLTAGTGGTVTGISRKIHERIPTAKVVGVDPHGSILAGPAETDIDFYEVEGIGYDFLPGTLDTSAIDYWAKSHDKESFLMARELIRSEGILCGGSSGCAVHYALEECKSLNLPAEANVVVLLPDGIRNYITKFLDDDWMNERHFLDA
|
4.2.1.22
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P35520};
|
cysteine biosynthetic process from serine [GO:0006535]; sulfur compound biosynthetic process [GO:0044272]
|
cytoplasm [GO:0005737]
|
cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146]; pyridoxal phosphate binding [GO:0030170]
|
PF00291;
|
3.40.50.1100;
|
Cysteine synthase/cystathionine beta-synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22240119}.
|
CATALYTIC ACTIVITY: Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine; Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22; Evidence={ECO:0000269|PubMed:22240119};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.57 mM for serine as substrate (at 16 degrees Celsius) {ECO:0000269|PubMed:22240119}; KM=4.29 mM for homocysteine as substrate (at 16 degrees Celsius) {ECO:0000269|PubMed:22240119}; Vmax=1.5 mmol/h/mg enzyme with serine as substrate (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:22240119}; Vmax=0.3 mmol/h/mg enzyme with cysteine as substrate (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:22240119};
|
PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2. {ECO:0000250|UniProtKB:P35520}.
| null | null |
FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine (PubMed:22240119). Plays a role in maintaining homocysteine homeostasis (PubMed:22240119). Involved in cold-induced somatic longevity mediated by prostaglandin E2 (PGE2) signals from adult germ cells, perhaps acting via a role in the production of hydrogen sulfide (H2S) (PubMed:31485561). Required for normal development (PubMed:22240119). {ECO:0000269|PubMed:22240119, ECO:0000269|PubMed:31485561}.
|
Caenorhabditis elegans
|
G5EFI7
|
MYRF1_CAEEL
|
MSSSDLLKGEFDGLNSEHFNMMQYLTQDTDEDDGSMVSPTSSADSMHQNLGVQQQQQQMLQAQQRQNQNGIFQPRRFPESPAMTDPCGNVSSSSSSSHHSDPMFSPNEFNGYAGANDNGNQTMNNIQSQQLSQQQHQQTRGGNLMMPQQSSIHAQMQNMNAPQFWSQPGTAAVNQPTNTLAQLNLFNIIRGGADSGMPSPVLEMPRKRSRLDTPCETPRIAPSFAGIDGFPDENYSQQQAIRFSKFQEEQWSPLYDINAQPLQQLQVHVVADKGFNYNSNDNCFVNQKKNHFQISVNVEASDTMPPKYVNFNNRLVPIRDFKLSFCGVKAEMPSSEITIRQSRADRKPHTHTPVLFEIQERRMTKVCVPRLHFSETTLNNQRKQKNRPNPEQKFFLLVVRLFASIDESEHGVLIQSYASEKVIVRATNPGSFEPQDTDIGWQRNGGALYTQGAVSVGTEHQVESAKLTVAGDIYMSGRIINPSDIRLKEAITERETAEAIENLLKLRVVDYRYKPEVADIWGLDEQQRHRTGLIAQELQAVLPDAVRDIGDYLTIDEGRVFYETVMATQQLCRMTGDLDSKIDEKVAEISRRLNEYAVRKKLASSMASNLNGDNKSLSYSRCSLTSTATNATSQPKRSRKHRAIKQAQSCGSRLSQGTVVTLVSIMAACLLAMSALYVLDWHNRNYGYHQHFETNTPSTKGELANLVISPANFMPSFQPDAPILLEKCFNPSCKTYCCTDTPPVVEDSRAIATHGLDNGDEVYPESPSNRTNGIARAPNLEHMAFETGVEIRIPALNVTLDQRYCVERSCNKRKGIFNVFVPVSRYMPDVALEIEIKAPISKVVSNCGAFPSTEFNHKVCPLSRTQQSESPVPTSTRLFDNIFELSMGSFIQSAYRFRVGYSTETCFSEDSNGSYEEYNLIFYRMCTLSSS
|
3.4.-.-
| null |
cell differentiation [GO:0030154]; ecdysis, collagen and cuticulin-based cuticle [GO:0042395]; molting cycle, collagen and cuticulin-based cuticle [GO:0018996]; nematode larval development [GO:0002119]; positive regulation of DNA-templated transcription [GO:0045893]; protein autoprocessing [GO:0016540]; regulation of neuron remodeling [GO:1904799]; regulation of synapse assembly [GO:0051963]
|
apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity [GO:0003700]; peptidase activity [GO:0008233]; sequence-specific DNA binding [GO:0043565]
|
PF13888;PF13887;PF05224;PF13884;
|
1.10.10.10;
|
MRF family
|
PTM: Myelin regulatory factor: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity. {ECO:0000305|PubMed:28441531}.
|
SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:33950834}. Apical cell membrane {ECO:0000269|PubMed:33950834}; Single-pass membrane protein {ECO:0000255}. Note=In early L1 larvae, localizes to the cell membrane of the pharynx, epidermis, and neurons, but is not enriched in the nucleus or cytoplasm of these cell types (PubMed:33950834). Later in the L1 larval stage, accumulates in the nucleus of the pharynx, epidermis, and neurons (PubMed:33950834). {ECO:0000269|PubMed:33950834}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 1, N-terminal]: Endoplasmic reticulum membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:28441531}. Cytoplasm {ECO:0000269|PubMed:28441531}. Apical cell membrane {ECO:0000269|PubMed:33950834}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage (PubMed:28441531). In early L1 larvae, localizes to the cell membrane of the pharynx, epidermis, and neurons, but is not enriched in the nucleus or cytoplasm of these cell types (PubMed:33950834). Cell membrane localization is promoted by pan-1 (PubMed:33950834). Later in the L1 larval stage, accumulates in the nucleus of the pharynx, epidermis, and neurons (PubMed:33950834). {ECO:0000269|PubMed:28441531, ECO:0000269|PubMed:33950834}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 1, C-terminal]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: [Myelin regulatory factor homolog 1]: Constitutes a precursor of the transcription factor (PubMed:28441531). Mediates the autocatalytic cleavage that releases the Myelin regulatory factor homolog 1, N-terminal component that specifically activates transcription of genes involved in synaptic rewiring during nervous system maturation (PubMed:28441531). {ECO:0000269|PubMed:28441531}.; FUNCTION: [Myelin regulatory factor homolog 1, C-terminal]: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. {ECO:0000250|UniProtKB:Q9Y2G1}.; FUNCTION: [Myelin regulatory factor homolog 1, N-terminal]: Transcription factor that specifically activates expression of genes involved in synaptic rewiring during nervous system maturation (PubMed:28441531). Specifically required for dorsal D (DD) GABAergic motor neurons synaptic rewiring (PubMed:28441531, PubMed:33950834). Acts in complex with myrf-2 paralog (PubMed:28441531). {ECO:0000269|PubMed:28441531, ECO:0000269|PubMed:33950834}.
|
Caenorhabditis elegans
|
G5EFI8
|
PLCE1_CAEEL
|
MNWDTLKGVLKTRRLTKRTIPAYIHPTSRSDSTSSTQSATAGFILNEEPITLFRLELERLQYILHFPEEVAFQLSSTEYQLFYSIQPMDYVRYVSCDLTSVPVSENPSPVRNLVKRLSEVSSWITHVIVSQPTHDDRKVALTAILRIVETCWNIGNFNAAVEVLMGLKSEKLRPFWLSLRQEEKSQFDSLCETLLPANQALPSQAYINAVQRALRMPQSRVIPFFGIFLRDLYAIVNDLPNIVVIGQEGETQKLEFMSDPNGEDHFSSRIGVGGLLNADKINLVAIVLDNLELFHRHSRTMIKLLEEQAVPPIQIPQNEREQKEKEAKTYEPVQVVRGSSHGVALIPLDTLTFDLDVIQRLQHGTTVIHYEPDSGRSNLCLLRLDPSCGQINWHKISYSVNKDPKEKDVLAKVSVSNLQPLDSGRGAPSPMPSGRTPGTGGVGVEEGELKLSVVKGVELVDSYDIDIEAIYRRHSMEEMSVPVSCWKVSHGQLLSDNEFIYFLAPQQIAQFWTNGLQSVVKSLQGQQRYPDRRMLWIKNVYLSLYEITGESNCGPRPFEALQAFGLSQTNTNATRPNDSSLSSEPGGAKSRLKNLKNAMQKKLRGASREGSRSQSPQPHSPLVRPPSIKSQISSQSGPPGPNSPGYLLKPRGEPANSDAGDIDSIYTPRSRTPTSSSYGGRSVGGRSCKSWRSRGGETPNSGSISSSGQMSIQVSGLSGPSGKEFQEKPLTLVEFAELFRLFNTRMRKDLRDVFNDVLSTATTPQHCPKRERDRHSPRMQSRLASVSNSYNADFLSNDFLTRNTAVTSHHISEKQNKIYNALALASVNSMGGLMDTSRSSMLTPQMLRAFVNTHQMEQIDEQTAIKLIQDHEPDGICRQKNQMSFEGFTRFLCDPVNFAFVPETIEPDEEDLRYPLSHYYINSSHNTYLTGHQLKGPSSSEMYRQVLLTGCRCVELDCWDGDDGLPLIYHGHTLVSKIGFRQVVEIIKKSAFITSDLPVILSIENHCSLQQQAKMAQMFKTVLGDLLVSNFLFEADFSDSPRLPCPLQMKNKILIKNKKMIVDPPTPLPMIERGAVQRGETQLNLHRKQSKNSYESSTVDEVEDDDLDEFLDDEENEEDDQEEVQVRSEKEDSPKTSKRAEKSARNIKQQDSLCSDHSVEQAKPSTSKTTSKTNDRKTEDEVLYAQLAQNAIRNQQPRKNNTGVQIAPELSDIVIYMQATKFKGFPPVDGIQSPRIMEEGPASASLSFSSRARTPSNLLNTPAPPRRQRSSTQLSQELAAEFLGSVRANATATCYQVTSLNENAAKKLMKRHPAKCVSYTRDHLIRTYPSAKHYDSSNFNPINCWAHGMQMVALNFQTPDVIMAVNQAMFEQSGNCGYQLKPRCLWDESHLLYNKFLPLSKDIAGHSALLLNLTIISGQHVYPNTHYASLYVEIEVIGIHNDCVREKSKVVQRNSVNPIWNHTTQLRIACVDLAFLRIAVCDSGQNGRVVAHRVVPVKCIRPGFRHLPLRTPTNLPIDNAMIFLRTRFEQEEHIYLHDDDSNTYCNLEHTLAYRTDLTPNLSPTPILKKQIFVLRITGAFADETAITVHSESGSTVKTVMQQALLNAGKNADQVEEYVLIEESLPAPSGEDPIEQRVLPLNEPIMDAVACWNGSMRRFVLRKKGSDPSSRAWITSIIKSGTSGSSTSVSPSPLTKDGHVKSASSNQLHGRSLDTDAFGEHLEVTEGKWLNPRARSMGDTFLVCVHNVSEDQPYAILRAGIHSTAADIIRQVFVKARRSNVDDSEFVLVEETCDDPKLNQGQSMLQALSLARKRSNDLTPKYPNNRTTSRVLGQNENVWKAQSRWKSMGRFVLENRKDTVHATLEKEFHEMAKIIREGIPKKDETYYMIYYSGLPGEDI
|
3.1.4.11
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9497345};
|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate catabolic process [GO:1902634]; activation of immune response [GO:0002253]; defense response to Gram-positive bacterium [GO:0050830]; G protein-coupled receptor signaling pathway [GO:0007186]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of protein import into nucleus [GO:0042307]; Ras protein signal transduction [GO:0007265]; release of sequestered calcium ion into cytosol [GO:0051209]
| null |
GTPase inhibitor activity [GO:0005095]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; phosphatidylinositol phospholipase C activity [GO:0004435]; small GTPase binding [GO:0031267]
|
PF00168;PF09279;PF00388;PF00387;PF00788;PF00617;
|
2.60.40.150;1.10.238.10;3.20.20.190;1.10.840.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000255|RuleBase:RU361133, ECO:0000269|PubMed:9497345};
| null | null | null | null |
FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (PubMed:9497345). plc-1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity (By similarity). By activating IP3 receptor itr-1-mediated intracellular Ca(2+) release via the production of IP3, regulates ovulation by controlling contraction and/or dilation of the distal spermatheca valve during oocyte entry and the timing of the dilation of the spermatheca-uterine valve during oocyte exit (PubMed:15194811, PubMed:15355798, PubMed:18369461, PubMed:23671426). In a similar manner, plays an essential role in epidermal morphogenesis by regulating migration of epidermal cells during ventral closure and to a lesser extent by regulating epidermal cell dorsal intercalation (PubMed:18369461). Involved in the immune response to S.aureus bacterium by activating kinase dkf-1 via the production of DAG which in turn activates transcription factor hlh-30 (PubMed:27184844). In ASER neurons, required for adjusting the orientation behavior in salt gradients based on the memory of previous salt concentration encountered (PubMed:23887678). {ECO:0000250|UniProtKB:Q9P212, ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:15355798, ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:23671426, ECO:0000269|PubMed:23887678, ECO:0000269|PubMed:27184844, ECO:0000269|PubMed:9497345}.
|
Caenorhabditis elegans
|
G5EFJ4
|
CAPG1_CAEEL
|
MPPKKRIRGPKLPALREEKSTGTDVASDESFNESADFLNNEELNNDQNDAENTVLSEGVSTLRINENMTKEDRACISAALFIKKRVVESIRTVFQSRDDINDEIHTSSRKLIAAFKKADQNRKKKVDLMKVFLDEIDVRLSMIIEEVTVPEHRARVFKLIAVTITEIQAFKLPSDLLDFIINFINTWGHSDNVAARINTTCFISYIFETGKRYLTTEGEYSGFEVKIAAKMFLQLKRALLDKEQTARVPAIRGLGFLQEIPIPSNWPVDAMKHSPRELLLRSCRDTAWECRLVAVQSMVPLETDVRLLSDIVYYDKCLNVRVAALEQFSNLRPNKHVREKIEMLDLCLKDHEVNIRDAAKEVLKNWVRNLSTRWSESQKSKDSNDVVILNSNSESTTGEENKMKGYILAAQALTLLWLTGALETLEGHSNLRRLITHTLDVIRQMYVCQADPINTFAEVLISDLREKMKSSAVPIITKSTVGSILDDSELADTQDPSTNRAMIFFWRCLVDYISDRKRNDADKINAMSRFVSPLRTMVEHVEKILVRVKNLDVYPNISQRADYEDHTFVLQMSIVENIICVMRHAPTDQPGVDAYKQMLISMLMNVFYQKKVIDLIVQELAQFYKEDPNALFTLFNDRIEEMRSKYKSGQFPVIENSVPVGETKVRKDLEEETRKTGRRTISDKDGIAVIDLYELKVLNALLKTGILLGWSTTYQNRYNNKLREGISSKDLSTRVLCTECIGIGAIYDYDQAENTLREMMKSFNTQDEPVQCSLIAALTDIQIEHGDQVDALFSWNSKQPNFAVFLSDIVVNAHVSGECETMLRAVEAISRLFLNTKIDPNQQKWQRTMVTLMTRASYAITNRFSAKVRSTIIVMLKFFCSINKNNQLLLIKSFHNFFDMWANSTTPERLTENRHEMVTKLKRCAATFVALTRHSTLPLEEQKKCKPTHVDLVDDIFHEMAGAPDSTSVDYYICALNFVEYQSLSRSALTKIHGDLESYIFLHELDGDKHRYNELRKAHRKIAKILGLNEDEIEEVPSKTDLRKEAAPSKTNKRNANLISTDIAVDNDVNMEEDDKPGPSRPATVRKPRAPRATPASATKKKPLVEEDALEILKSPPRNTKKPPSRPTTATRPTAVAARTAPPRSARKLRSEK
| null | null |
cell division [GO:0051301]; dosage compensation by hypoactivation of X chromosome [GO:0042464]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic chromosome segregation [GO:0045132]; meiotic sister chromatid segregation [GO:0045144]; mitotic chromosome condensation [GO:0007076]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of gene expression [GO:0010629]
|
condensed chromosome [GO:0000793]; condensin complex [GO:0000796]; cytoplasm [GO:0005737]; dosage compensation complex [GO:0046536]; X chromosome [GO:0000805]
| null |
PF12719;
|
1.25.10.10;
|
CND3 (condensin subunit 3) family
| null |
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23684975}. Note=During meiosis and mitosis, localizes to condensed chromosomes in both sexes (PubMed:19119011). Localizes to the spindle midzone in between separating chromosomes during anaphase and to the midbody during cytokinesis (PubMed:23684975). During interphase, localizes specifically to X chromosomes in hermaphrodites after the onset of dosage compensation (PubMed:19119011). {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23684975}.
| null | null | null | null | null |
FUNCTION: Member of two distinct condensin I complexes, the condensin I complex and the condensin I-like dosage compensation complex (PubMed:19119011, PubMed:19781752). The condensin I complex is required for conversion of interphase chromatin into mitotic-like condensed chromosomes and for chromosome segregation in meiosis and mitosis (PubMed:19119011, PubMed:19781752). As a member of the condensin I complex, further controls crossover number and distribution in meiosis by restricting double strand break formation, probably by influencing higher-order chromosome structure (PubMed:19781752). Regulatory subunit of the condensin I-like dosage compensation complex that associates specifically with hermaphrodite X chromosomes to reduce their gene transcription during interphase, possibly through chromatin reorganization (PubMed:19119011). {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752}.
|
Caenorhabditis elegans
|
G5EFJ9
|
UN103_CAEEL
|
MKTAVFGRDSGEPGSPCGAPPSLTFTPPATLVPPTHHHSRSTNRGGVSGTGGGGSGGLQGAPGAGGPRASHSSRRTSRLHNNVSALGVLSLGADVLPEYKLQPTRIHHCTIVHYSPFKAVWDWIILLLVIYTAVFTPYVAAFLLRELQDTAKKSRFTEPLEIVDLIVDIMFIVDIIINFRTTYVNENDEACQVVSDPGKIATHYFKGWFIIDMVAAVPFDLLLVSTNSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLLLLMATFALIAHWLACIWYAIGSAELSHKEYTWLHQLSKQLAQPYTSTNGTIPTGGPTLKSRYVTSLYFTLSTITSIGFGNVSATTDSEKIFTIIMMILGSLMYASVFGNVSAIIQRLYSGTARYHTEMSRLREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNLVLKGFPDCLQADICLHLNRNLLSGCAAFAGSTPGCLRALSMRFRTTHSPPGDTLVHRGDILTGLYFIARGSVEILNDDNTVMGILGKDDIFGENPLLYDEVGKSSCNVRALTYCDLHKILRDDLLDVLDMYPEFAETFCKNLTITYNLRDDAQSLRKKFDRHKLLRMSSSMNKDRYTTPPDGDHGNAAVRRSAESVSRCDSNPIDRRQSAGSRSSSRCSPPHAALTATRSEATPLLRRSTNHHEEDDALFDDIRAFARGNTVTMSPTVAGNSVSPTTAIHNDGIHSQQLSDRSDDYEERRANMFGRRLESIESQMERMQNKFNSDMETLIKLVKEQSIIRNNGSSNEEPNARYRPNNYISSAIRLPNGGGGGVVDEMRVSRLSSHEPPTPTQETDTIL
| null | null |
mating behavior [GO:0007617]; membrane repolarization during action potential [GO:0086011]; potassium ion transmembrane transport [GO:0071805]; regulation of egg-laying behavior [GO:0046662]; regulation of membrane potential [GO:0042391]; regulation of muscle contraction [GO:0006937]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
inward rectifier potassium channel activity [GO:0005242]
|
PF00027;PF00520;
|
1.10.1200.260;1.10.287.70;2.60.120.10;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.1/KCNH2 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly (By similarity). Regulates the movements of the male's copulatory spicules before and during male mating behavior (PubMed:12684455). {ECO:0000250|UniProtKB:Q12809, ECO:0000269|PubMed:12684455}.
|
Caenorhabditis elegans
|
G5EFL0
|
GLD4_CAEEL
|
MNEDSRLSSSQQPSTSTPRSSIPSTMNSDEPNTCRRLSQSQEQPSTSRTCKSETPEFGYSDSLPFAPWRRKRYGLNIQGLHEEIVDMYHWIKPNEIESRLRTKVFEKVRDSVLRRWKQKTIKISMFGSLRTNLFLPTSDIDVLVECDDWVGTPGDWLAETARGLEADNIAESVMVYGGAFVPIVKMVDRDTRLSIDISFNTVQGVRAASYIAKVKEEFPLIEPLVLLLKQFLHYRNLNQTFTGGLSSYGLVLLLVNFFQLYALNMRSRTIYDRGVNLGHLLLRFLELYSLEFNFEEMGISPGQCCYIPKSASGARYGHKQAQPGNLALEDPLLTANDVGRSTYNFSSIANAFGQAFQILLVAVTLRERKGKNHVAMRAYKGSLLHLIMPFTSKELTYRNWLMSGVLSMPGQEAPASYDLNQLHNTLVSPMVDLSRYAWLRKAPAKAEKRDSRPLTIVNPADDRQTLAQQLKKQILEQTEAKKSLEKMPACDDNKKEEELVATRETDVELEAEDTESEGHHNGENDLILTGPPLPTSTQSVNTSATVSTAASISEREDTDSPGLSSSMGNQSSEEDEDNGINNRNNSAVPVQFKKPFNEVVAQPARESKRTQTTSEDKMQDQFHFNGYSYPPPSRYAAGTAAPSHKHRNAHPQRQRPSIRNLSQGSDGSDEYNVESWNNNIRQGRRASSNSPSPSRQQTNTRNCGPTNNIPYDSFRSQNKNSTLDGSNNSSEEPITMYADVVKKKSSITTSTNTSTADVNVTNGNPIPANGIIPQSMAVVNVGRGSYRNALTTSPMTPPSAHTSMQKQHHLRKDNECGFDNNSATSSTDLSHHQPQLVPPVNRLQR
|
2.7.7.19
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O17087}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O17087};
|
cytoplasmic polyadenylation [GO:0180011]; meiotic cell cycle [GO:0051321]; positive regulation of meiotic cell cycle [GO:0051446]; RNA 3'-end processing [GO:0031123]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; P granule [GO:0043186]; perinuclear region of cytoplasm [GO:0048471]; TRAMP complex [GO:0031499]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A) RNA polymerase activity [GO:1990817]
|
PF01909;PF03828;
|
1.10.1410.10;3.30.460.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19339688}. Cytoplasmic granule {ECO:0000269|PubMed:19339688}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19339688}. Note=Localizes to P granules. This association is less apparent during pachytene, becomes obvious in maturing oocytes and is most prominently visible in developing embryos. {ECO:0000269|PubMed:19339688}.
|
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:19339688};
| null | null | null | null |
FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. The enzymatic activity is enhanced by its interaction with gls-1. Required, together with gld-2, for early meiotic progression in male and female germ cells and for gld-1 protein accumulation in the hermaphrodite germline. In the germline, forms a complex with gls-1 which directly binds to gld-1 mRNA and prevents its degradation. {ECO:0000269|PubMed:19339688}.
|
Caenorhabditis elegans
|
G5EFM9
|
NEKL3_CAEEL
|
MDKISNIYNFDDPPPDKLSLELFIIEKKIGKGQFSEVFRAQCTWVDLHVALKKIQVFEMVDQKARQDCLKEIDLLKQLNHVNVIRYYASFIDNNQLNIVLELAEAGDMSRMIKHFKKGGRLIPEKTIWKYFVQLARALAHMHSKRIMHRDIKPANVFITGNGIVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIQESGYNFKSDLWSTGCLLYEMAALQSPFYGDKMNLYSLCKKIENCEYPPLPADIYSTQLRDLVSRCILPEASKRPETSEVLQVAEHMNNYFSPSGDQSTTPSTQF
|
2.7.11.34
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9HC98};
|
gonad development [GO:0008406]; molting cycle [GO:0042303]; multicellular organism growth [GO:0035264]; phosphorylation [GO:0016310]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25523392}. Note=In hyp7 syncytium, localizes in puncta and small tubules near the plasma membrane apical region. Does not co-localize with nekl-2. {ECO:0000269|PubMed:25523392}.
|
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=2.7.11.34; Evidence={ECO:0000250|UniProtKB:Q9HC98}; 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=2.7.11.34; Evidence={ECO:0000250|UniProtKB:Q9HC98};
| null | null | null | null |
FUNCTION: Probable serine/threonine-protein kinase required for the completion of molting. {ECO:0000269|PubMed:25523392}.
|
Caenorhabditis elegans
|
G5EFN6
|
FLP2_CAEEL
|
MQVSGILSALFLVLLAVIVSPFQFVQPKRILPIPTSRDQLLRGQLAYLKGTTVAQPAVNDNTLGIFEASAMAKRLRGEPIRFGKRSPREPIRFGKRFNPLPDYDFQ
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; locomotion [GO:0040011]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of protein secretion [GO:0050714]; signal transduction [GO:0007165]; sleep [GO:0030431]
| null | null | null | null | null | null | null | null | null | null | null | null |
FUNCTION: FMRFamide-like neuropeptides (PubMed:15809090, PubMed:24533288). Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity, and working in concert with neuropeptide pdf-1 (PubMed:27585848). Involved in neural modulation of systemic mitochondrial unfolded protein response (PubMed:27767096). {ECO:0000269|PubMed:15809090, ECO:0000269|PubMed:24533288, ECO:0000269|PubMed:27585848, ECO:0000269|PubMed:27767096}.; FUNCTION: [SPREPIRF-amide]: Acts as a ligand to FMRFamide peptide receptor frpr-18 in vitro. {ECO:0000269|PubMed:15809090, ECO:0000269|PubMed:24533288}.; FUNCTION: [LRGEPIRF-amide]: Acts as a ligand to FMRFamide peptide receptor frpr-18 in vitro. {ECO:0000269|PubMed:15809090, ECO:0000269|PubMed:24533288}.
|
Caenorhabditis elegans
|
G5EFP5
|
FUTC_CAEEL
|
MRVRPASVYRYLLLGVCALLGIYTVYSIIGYDDGSHVPIHRPQRHLYLTVSQDRIGSRFGKLAPKRILYWTTIFGATVPSTALSDCPGLTDRCVIDTNRHQLDSADAVVFHAADISKFPLPVSRKPDQIFVFNSMETPDNSGRFAVPDGFFNWTSTHLYSSDAIHKYGTFLIPTQIAESRGFKVQSYYVQPKRLVKTMKGIFGLISNCHTKSKRELALQELGKHINVTIGGKCASDDRLKSICPAGVECIDVFEQYPFYIAIENTVCNDYVTEKIWSRITVPSIPIVMRRRVYQNILPPKSFIAMDDYKNPSEMANHLRSLEANSTAYGEYFEWRQKGLWTSAPWNAPGYRNGLCRVCELLWKAKDNETEVYKSYDNIWKWFDNESQCETDEFVRSWLSG
|
2.4.1.65
|
COFACTOR: Note=Unlike other alpha-(1,3)-fucosyltransferases, appears not to require a divalent metal cation as cofactor. {ECO:0000269|PubMed:17369288};
|
fucosylation [GO:0036065]; protein glycosylation [GO:0006486]
|
Golgi cisterna membrane [GO:0032580]
|
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity [GO:0017060]
|
PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:17369288}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304; EC=2.4.1.65; Evidence={ECO:0000269|PubMed:17369288};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:17369288}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 23 degrees Celsius. Vey low activity at 37 degrees Celsius. {ECO:0000269|PubMed:17369288};
|
FUNCTION: Catalyzes the addition of fucose in alpha 1-3 linkage. Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2-Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (GnM3F6) acceptors. {ECO:0000269|PubMed:17369288}.
|
Caenorhabditis elegans
|
G5EFQ0
|
GCY18_CAEEL
|
MLKTLLFILIFFNIPIIAIEEIPDIKENGEKSSYTQFDNGAKLEVNKEHKRVIKIGHIGAVGVMPNDARILNISKENLIEEGLVGDDIEFEIVSRQACSESFEGVAVAAELYHVHQVRAFIGPYCAAELEAVTKMATFWNIPIISYSSVPNAVSDRSVYKTLARVSSKNTNSIAEATVALLLHYKWLKVAIATNTGSTAFERVSIFEEIMHREGVTIVKKVMFDENTDANEMMNSGQLGDLAANARIIICLFSSTKELSKEFMQATYTMRMNNAEYAYIIPWLQSGTKDLTPWIGADGEMLQRVKDHYANAIIVDDVNGFDDSVVSSFVEKIEKHGMQKSDIDVTNINGYLHLFDSLKLYALAIRKVLNETDNEAYVTNGQFIWNRMRRMKFEGVVSRSSSEENKDAGAIGTVLMDDVADRAPIFSAFYISPNRDKVMKMVNMESELISNCDGLKNKSGCFQLKINDIKSGFWPSEDGSMPLDEPICGYRGQRCSYLLEISVGSLIILLILISVVFFFLFRYCENKQLEKMPWRIFHDDLQFIDEEQVKSMMSVGSVTTKLSNIQTGQKQHAIIGVNTHTTYHRYKQRRPIKFIKEDMQLLTQMKQAVHDNLNPFLGAAFNEKEEMLVLWKFCSRGTIQDIIYNANVVLDEKFHGAFVRDITLGLEYLHASPIGYHGSLTPWCCLIDRNWMVKLSDYGIANPLERWEKQGAIEIAAAKDSDDKSQASQATSIIYMAPELLKNRETNKRRGMDQSWVKQSMLRRQAGDIYSFGMVMYEILFRSLPFRDNTNISELVDYLADGSKTVSPEIQNQMGLHPDLNALLRDCWSENPEIRPSIRRVRLNTEMVLKTKGSLVDQMMKMMEQYANNLEKLVAERTGMLEEANIRADQLLTQLLPAYVANELKMGRSVAPKLYSSATILFSDIVGFTTICSGSTPLEVVNMLNGLYTGFDECITRNKSYKVETIGDAYMVVSGIPEENEYNHSRNIANTALDMRQYLTGYQIPHRPTHRVRCRWGFHTGSVAAGVVGLTCPRYCLFGDTVNVSSRMESTGTPGMIQMSEEAHMHIRAHHPVFTTTERGEVQVKGKGTCRTFWLEDRVGDASTTNYIQNVEGV
|
4.6.1.2
| null |
cGMP biosynthetic process [GO:0006182]; detection of temperature stimulus [GO:0016048]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; thermosensory behavior [GO:0040040]; thermotaxis [GO:0043052]
|
cilium [GO:0005929]; microvillus membrane [GO:0031528]; neuron projection terminus [GO:0044306]; plasma membrane [GO:0005886]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; metal ion binding [GO:0046872]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]
|
PF01094;PF00211;PF07714;
|
3.40.50.2300;3.30.70.1230;1.10.510.10;
|
Adenylyl cyclase class-4/guanylyl cyclase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:16415369}. Note=Localizes exclusively to the sensory ending, known as cilium, in AFD neurons. {ECO:0000269|PubMed:16415369}.
|
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187};
| null | null | null | null |
FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates thermotaxis responses in AFD sensory neurons. May regulate AFD neuronal activity such as calcium responses to temperature gradients (PubMed:16415369). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:16415369}.
|
Caenorhabditis elegans
|
G5EFQ5
|
RUNX1_CAEEL
|
MTNVFHHVRNFIEQQPAPAKTLEKSSSPNILYTALPKHWRSNKSFQEPFYVVLLTPVPDNTEVSIWAGNDEKPCEEVRNEKAKVHRQVAKFNDLRFVGRSGRGRKFHLTIVIHSAPMMVATVKNVIKVTVDGPRDARIPKPQGSLKRQAEQQTIFPNDIIRTPGPPMPMTMIPPPWFPLPMTQTFPPSFFPLISPGPHPSISAALWKIHSESMKTPIKQKVEQENVSLNTSTCLSSPSIFITPTSDDRKLKRPSSPRSITKSSETSINLIQETPESVESKRRRNVSITSSNSSSPTIWRPF
| null | null |
asymmetric cell division [GO:0008356]; asymmetric stem cell division [GO:0098722]; chondrocyte differentiation [GO:0002062]; dopamine metabolic process [GO:0042417]; embryo development ending in birth or egg hatching [GO:0009792]; hemopoiesis [GO:0030097]; negative regulation of gene expression [GO:0010629]; negative regulation of stem cell differentiation [GO:2000737]; nematode male tail tip morphogenesis [GO:0045138]; neuron differentiation [GO:0030182]; ossification [GO:0001503]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979]
|
core-binding factor complex [GO:0016513]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; 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]; SMAD binding [GO:0046332]
|
PF00853;
|
2.60.40.720;
| null |
PTM: May be ubiquitinated in order to be targeted for proteasome-mediated degradation in intestinal cells. {ECO:0000269|PubMed:22308034}.; PTM: May be phosphorylated by members of the p38 MAP kinase pathway. {ECO:0000269|PubMed:22308034}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00399, ECO:0000269|PubMed:16226243, ECO:0000269|PubMed:16236764, ECO:0000269|PubMed:31740621}. Note=High level of nuclear localization in interphase seam cells before the symmetric larval stage L2 divisions, but subsequently rnt-1 disappears during mitosis, and largely remains absent when the nuclei reform in telophase. {ECO:0000269|PubMed:31740621}.
| null | null | null | null | null |
FUNCTION: Transcription factor (By similarity). Binds to regulatory DNA sequences in order to modulate transcription; negatively autoregulates its own expression, perhaps dependent upon CBF beta homolog bro-1 (PubMed:18158917). Promotes proliferation, and prevents differentiation, of seam cells, a stem cell-like lineage, acting in concert with bro-1 (PubMed:31740621). Required for controlling cell proliferation in the seam cells, perhaps by repressing expression of cyclin-dependent kinase inhibitor cki-1 (PubMed:16236764, PubMed:17933794). Inhibition of seam cell differentiation is regulated by rnt-1 and bro-1, perhaps acting upstream of pop-1, by antagonizing pop-1 repressor function (PubMed:31740621). Required for asymmetrical cell divisions in the lineage derived from a posterior embryonic seam cell, the T blast cell, and for asymmetric expression of zinc finger protein tlp-1 (PubMed:16226243). Regulates growth and male tail development (PubMed:15385167, PubMed:16226243, PubMed:16236764, PubMed:31083672). Involved in the oxidative stress response, perhaps downstream of the p38 MAP kinase pathway, and acting as part of a negative feedback loop via a transcriptional target gene, tyrosine-protein phosphatase vhp-1 (PubMed:22308034). Positively modulates dopaminergic signaling in a non-cell autonomous manner (PubMed:31083672). May be involved in TGF-beta signaling (PubMed:15385167). {ECO:0000250|UniProtKB:Q13950, ECO:0000269|PubMed:15385167, ECO:0000269|PubMed:16226243, ECO:0000269|PubMed:16236764, ECO:0000269|PubMed:17933794, ECO:0000269|PubMed:18158917, ECO:0000269|PubMed:22308034, ECO:0000269|PubMed:31083672, ECO:0000269|PubMed:31740621}.
|
Caenorhabditis elegans
|
G5EFR6
|
MCA1_CAEEL
|
MQKSQNVTAVTETNGVAAALGGHHTSPDTNAGKTKDAKEFGCSLGDLRGLMEARGAEAIVRLSTEHEGVEGLCKKLKTDSLVGLNGEQADLDRRRHVYGANTIPPAKSKGFVRLVLDACKDPTLVILVLSGFINLALSFYEPTSAAEDATQHLVNATTAAILANGTFMSTTEAPSEGHGTAWIEGVAILLCVIVVVLVTAVNDYSKERQFRSLQEKIETGQKFSVIRNGEAIDVPVSDLVVGDIARVKYGDLLPADGFLIQSNDLKIDESSLTGESDHIKKSIESDPVLLSGTYAMEGSGKMLITAVGVNSQTGIIMTLLGAGKAGIGDDDSTSTSSSSSSSSSSSGSSSNGSSDSSKSGDDDLTAKSVLQAKLSKLALQIIYCGTTIAIIALIVLVTRFCLDHYVFEKNEFSLVDIQMFVKFFIIAVTILVISIPEGLPLAIALALTYSVRKMMHDNNLVRHLDACETMGNATSICSDKTGTLTTNRMTVVQSYINGNHYTSQEAQPHGANLPGSTGPILMEAISVNCAYNSMIVEPTKAGEQIQQLGNKTECGLLGFVNRLGGDYAAIRKKFPEHDLTKVYTFNSSRKCMMTVVPYAENGQNIGYRVYCKGASEIVLGRCTYLIGSDGKPHQLTGDRLKEITSTIIHEMANSGLRTICVAYKTIIKKGTRDVEKTEIEFAEDSDIDWDDEDAMYQNFTGIAICGIQDPVRPEVPVAISKCKKAGITVRMVTGDNIMTARAIAMSCKILEPGEDFLALEGKEFNERIRDENGKVSQAKLDEIWPRLRVLARAQPADKYTLVKGIIDSKATPQREIVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVITAFVGAVTVSDSPLKAVHMLWINLIMDTLASLALATEQPTDELLERKPYGRKKSLISRTMVKNILCHALYQLIIIFVIFFYGDTIFGIKTGLYAPLFAPPSQHFTLVFNAFVMMTVFNEINARKVHGERNVFKGLASNRVFCVIWVTTFIAQIIIVQFGGAWFSTAPLTLQQWIVCLVLGFSTLIWGQIVATIPSKKLPKAWKVGKGEVQPANLHINGDYNVRARSRAVTLRRSGKSLWVRGMFIIGNHLRVLRAFGMEKSEKAAFGRTAPAMTAEAAERWRASYRKYRHQKHQEKKATAETAESVKSADWAKEQKEKKKTFKQIKQVARGKSLDKDSKKHHKKRKDQTNVDMEDIELN
|
7.2.2.10
| null |
calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; regulation of cytosolic calcium ion concentration [GO:0051480]
|
intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]
|
PF13246;PF00689;PF00690;PF00122;PF08282;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIB subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23634}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361146}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000255|RuleBase:RU361146};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane. {ECO:0000269|PubMed:9933625}.
|
Caenorhabditis elegans
|
G5EFS2
|
MSI1H_CAEEL
|
MTTTVSTGATAVATLRETSPPVDGHEEARLNADSDDGSHGSQDPGKMFIGGLSWQTTAENLRDYFGRFGEVNECMVMRDPATKRARGFGFITFVDPSSVDKVLNNREHELDGKKIDPKVAFPKRTQAKLVTKTKKVFIGGLSATSTLEDMKQYFETYGKVEDAMLMFDKATQRHRGFGFVTFDSDEVADKVCEIHFHEINGKMVECKKAQPKEVMLPVQLNKSRAAAARNLYGMPPETLLAYAQYLPRFGGNLMYPNFTNVFNNMPGGYSGLSTPGGSSNRPPHQFDTASLYSLNNGGQLLDSQAQMFMNQQSYHSHSKY
| null | null |
central nervous system development [GO:0007417]; nervous system process [GO:0050877]; regulation of translation [GO:0006417]
|
cytoplasm [GO:0005737]; perikaryon [GO:0043204]
|
mRNA binding [GO:0003729]
|
PF00076;
|
3.30.70.330;
|
Musashi family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11122376}. Perikaryon {ECO:0000269|PubMed:11122376}.
| null | null | null | null | null |
FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level (PubMed:24630719). Binds RNA containing the 5'-[GA]U(1-3)AGU-3' motif located in the 3' UTR of the target mRNA (By similarity). Binds to the mRNA of three Arp2/3 complex components arx-1, arx-2 and arx-3 and negatively regulates their translation during association learning (PubMed:24630719). Plays a role in time-dependent memory loss and the retention of conditioned behavior over time, probably through negative regulation of the Arp2/3 actin cytoskeleton branching complex and regulation of synapse size (PubMed:24630719, PubMed:36223338). Required for two aspects of male mating behavior: turning around the hermaphrodite head or tail and vulva location (PubMed:11122376). {ECO:0000250|UniProtKB:Q61474, ECO:0000269|PubMed:11122376, ECO:0000269|PubMed:24630719, ECO:0000269|PubMed:36223338}.
|
Caenorhabditis elegans
|
G5EFS4
|
DCPS_CAEEL
|
MKRIADEELVREERAEESTQKWLQDAKFQEILGADSSHKSLFVLLSHPDGSQGILLANKSPFSEEKSDIEKLLATAQLQEISRNDIFGSYNIEIDPKLNLLKSQLIYPINDRLIAKYRQEEKFVIRETPELYETVTRPYIEKYQLNLNWVYNCLEKRSEVDKIVFEDPDNENGFVLLQDIKWDGKTLENLYVLAICHRHGLKSVRDLTGDDLEMLYNMRDKSLEAINQKYGLKTDQIKCYFHYQPSFYHLHVHFINLKYDAPASTTMSAILLDDVINNLELNPEHYKKSTLTFTRKNGDKLMEMFREALKN
|
3.6.1.59
| null |
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; methylguanosine-cap decapping [GO:0110156]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; purine ribonucleotide metabolic process [GO:0009150]; response to heat [GO:0009408]; RNA catabolic process [GO:0006401]; sulfur compound metabolic process [GO:0006790]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]
|
5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; adenylylsulfatase activity [GO:0047627]; RNA 7-methylguanosine cap binding [GO:0000340]; sulfate adenylyltransferase (ADP) activity [GO:0004780]
|
PF05652;PF11969;
|
3.30.428.10;3.30.200.40;
|
HIT family
| null |
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616; EC=3.6.1.59; Evidence={ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = (N(2),N(2),N(7))-trimethyl-GMP + a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:65384, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17171, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74434, ChEBI:CHEBI:167616, ChEBI:CHEBI:167623; EC=3.6.1.59; Evidence={ECO:0000269|PubMed:15383679};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for m7GpppBODIPY {ECO:0000269|PubMed:12871939}; KM=8.52 uM for GpppBODIPY {ECO:0000269|PubMed:12871939}; KM=5.04 uM for ApppBODIPY {ECO:0000269|PubMed:12871939}; Note=kcat is 0.174 sec(-1) with m7GpppBODIPY as substrate. The catalytic efficiency with m7GpppBODIPY is at least 35- to 75-fold higher than with ApppBODIPY and GpppBODIPY as substrates, respectively.;
| null | null | null |
FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP. {ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:22985415}.
|
Caenorhabditis elegans
|
G5EFT4
|
AMP1_CAEEL
|
MAPPHPRDPSTAANYEQVTVSHYALKWKVDFEKKHIAGDVSITLDVKQDTERIVLDTRDLSVQSVALNLNGEPKKAGFTLEDNQALGQKLVITTESLKSGDRPVLEIKYESSNNAAALQFLTAEQTTDRVAPYLFSQCQAINARSIVPCMDTPSVKSTYEAEVCVPIGLTCLMSAIGQGSTPSECGKRTIFSFKQPVSIPSYLLAIVVGHLERKEISERCAVWAEPSQAEASFYEFAETEKILKVAEDVAGPYVWGRYDLVVLPATFPFGGMENPCLTFITPTLLAGDRSLVNVIAHEISHSWTGNLVTNFSWEHFWLNEGFTVFLERKIHGKMYGELERQFESESGYEEALVRTVNDVFGPDHEYTKLVQNLGNADPDDAFSSVPYEKGSALLFTIEQALGDNSRFEQFLRDYIQKYAYKTVSTEEWKEYLYDSFTDKKVILDNIDWNLWLHKAGLPPKPKYDSTPMQACKDLAAKWTTEGSEAPTDGEVFAKMSNSQKLAVLDAVRVNKTMFGDRMPALTATYKLDQAKNAELKFSWLMLGLETKWSPIVDASLAFALAVGRMKYCKPIYRSLFGWSATRDRAISQFKANIPNMHPITVKAIQSLLK
|
3.4.11.6
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P09960}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P09960};
|
leukotriene biosynthetic process [GO:0019370]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
aminopeptidase activity [GO:0004177]; epoxide hydrolase activity [GO:0004301]; leukotriene-A4 hydrolase activity [GO:0004463]; metalloaminopeptidase activity [GO:0070006]; zinc ion binding [GO:0008270]
|
PF09127;PF01433;PF17900;
|
3.30.2010.30;1.10.390.10;1.25.40.320;2.60.40.1730;
|
Peptidase M1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9774412}.
|
CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; Evidence={ECO:0000305|PubMed:9774412};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for L-Lys-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.43 mM for L-Arg-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.46 mM for L-Met-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=0.9 mM for L-Val-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=1.9 mM for L-Pro-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=2 mM for L-Leu-pNitroaniline {ECO:0000269|PubMed:9774412}; KM=5.53 mM for L-Ala-pNitroaniline {ECO:0000269|PubMed:9774412}; Note=No activity with L-Asp-pNA, L-Glu-pNA or D-Leu-pNA. {ECO:0000269|PubMed:9774412};
| null | null | null |
FUNCTION: Aminopeptidase which preferentially removes N-terminal Arg and Lys residues from peptides and proteins. {ECO:0000269|PubMed:9774412}.
|
Caenorhabditis elegans
|
G5EFT5
|
HSF1_CAEEL
|
MQPTGNQIQQNQQQQQQLIMRVPKQEVSVSGAARRYVQQAPPNRPPRQNHQNGAIGGKKSSVTIQEVPNNAYLETLNKSGNNKVDDDKLPVFLIKLWNIVEDPNLQSIVHWDDSGASFHISDPYLFGRNVLPHFFKHNNMNSMVRQLNMYGFRKMTPLSQGGLTRTESDQDHLEFSHPCFVQGRPELLSQIKRKQSARTVEDKQVNEQTQQNLEVVMAEMRAMREKAKNMEDKMNKLTKENRDMWTQMGSMRQQHARQQQYFKKLLHFLVSVMQPGLSKRVAKRGVLEIDFCAANGTAGPNSKRARMNSEEGPYKDVCDLLESLQRETQEPFSRRFTNNEGPLISEVTDEFGNSPVGRGSAQDLFGDTFGAQSSRYSDGGATSSREQSPHPIISQPQSNSAGAHGANEQKPDDMYMGSGPLTHENIHRGISALKRDYQGASPASGGPSTSSSAPSGAGAGARMAQKRAAPYKNATRQMAQPQQDYSGGFVNNYSGFMPSDPSMIPYQPSHQYLQPHQKLMAIEDQHHPTTSTSSTNADPHQNLYSPTLGLSPSFDRQLSQELQEYFTGTDTSLESFRDLVSNHNWDDFGNNVPLDDDEEGSEDPLRQLALENAPETSNYDGAEDLLFDNEQQYPENGFDVPDPNYLPLADEEIFPHSPALRTPSPSDPNLV
| null | null |
ascaroside biosynthetic process [GO:1904070]; cellular response to heat [GO:0034605]; dauer larval development [GO:0040024]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; determination of adult lifespan [GO:0008340]; innate immune response [GO:0045087]; negative regulation of gene expression [GO:0010629]; nematode larval development [GO:0002119]; positive regulation of dauer entry [GO:1905911]; positive regulation of fatty acid beta-oxidation [GO:0032000]; positive regulation of gene expression [GO:0010628]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription by RNA polymerase II [GO:0045944]; programmed cell death [GO:0012501]; programmed cell death involved in cell development [GO:0010623]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; response to heat [GO:0009408]; response to odorant [GO:1990834]; response to topologically incorrect protein [GO:0035966]; serotonin receptor signaling pathway [GO:0007210]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nuclear stress granule [GO:0097165]; nucleus [GO:0005634]; WASH complex [GO:0071203]
|
calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00447;
|
1.10.10.10;
|
HSF family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.; PTM: Sumoylated (PubMed:29036198). Sumoylation may inhibit transcriptional activity in response to heat shock (PubMed:29036198). {ECO:0000269|PubMed:29036198}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23107491}. Cytoplasm {ECO:0000269|PubMed:22265419}. Note=Localizes constitutively to the nucleus (PubMed:23107491, PubMed:29042483). Localization to the nucleus enhanced by heat shock (PubMed:22265419). Localization to nucleus inhibited by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419). In response to heat shock, forms nuclear stress granules (PubMed:23107491, PubMed:29036198). These structures are dependent upon either heat shock, or can be induced by treatment with sodium azide, which may act by inhibiting ATP production (PubMed:23107491). DNA binding may promote localization to stress granules (PubMed:23107491). Localization to stress granules partially overlaps with sites of active transcription (PubMed:23107491). Other stressors such as osmotic stress, heavy metals, or ethanol do not induce localization to nuclear stress granules (PubMed:23107491). {ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:23107491, ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.
| null | null | null | null | null |
FUNCTION: Functions as a stress-inducible and DNA-binding transcription factor, playing a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:15611166, PubMed:22265419, PubMed:29042483). Upon exposure to heat and other stress stimuli, activates gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of target genes, such as the HSPs (PubMed:15611166, PubMed:22265419, PubMed:27688402, PubMed:29042483). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences in HSEs (PubMed:27688402, PubMed:29042483). Involved in positive modulation of expression of heat shock protein hsp-16.2 in response to heat shock; may act in concert with homeodomain-interacting protein kinase hpk-1 (PubMed:15611166, PubMed:28198373, PubMed:29036198). In response to heat shock or starvation, required for the modulation of lifespan, and protection against aberrant protein aggregation proteotoxicity; may act in parallel with the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:15611166, PubMed:18331616, PubMed:28198373, PubMed:29036198). Plays a role in modulating autophagy, in response to a moderate and short-term heat shock, also known as a hormetic heat shock (PubMed:28198373). Involved in positive modulation of ascaroside pheromone biosynthesis in response to heat shock, perhaps by directly activating transcription of peroxisomal fatty acid beta-oxidation genes (PubMed:26759377). Required in modulating the response to infection by either Gram-negative or Gram-positive bacteria, perhaps acting via regulation of expression of Hsp90/daf-21 and members of the small heat shock protein (HSP20) family (PubMed:16916933, PubMed:29042483). May play a role downstream of the daf-16/FOXO and daf-2 signaling pathway in response to bacterial pathogens (PubMed:16916933). Modulates expression of multiple microRNA genes, in both heat shock-dependent and -independent manner (PubMed:28837599). Independent of heat shock, required to modulate expression of genes involved in larval development, mainly distinct from HSPs; acts in concert with putative transcription factor efl-1/E2F, which may form part of a multiprotein DRM complex (PubMed:15611166, PubMed:27688402). Independent of heat shock, involved in promoting death of the linker cell, a male-specific cell which guides the elongation of the gonad; perhaps acting by modulating expression of ubiquitin-conjugating enzyme let-70 (PubMed:26952214). Plays a role in egg-laying (PubMed:15611166). {ECO:0000269|PubMed:15611166, ECO:0000269|PubMed:16916933, ECO:0000269|PubMed:18331616, ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:26759377, ECO:0000269|PubMed:26952214, ECO:0000269|PubMed:27688402, ECO:0000269|PubMed:28198373, ECO:0000269|PubMed:28837599, ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.
|
Caenorhabditis elegans
|
G5EFU0
|
PK2_CAEEL
|
MNRTFSLRRKVKKSEISTPSNFEHRIHAGFDARSGTYTGLPKQWQALLGPPRSISRPKPMVDPSCITPVDVAELKTVIRGPSSSFRYNSPLPFGMTNSPMPSVARSNSLRISATASPVVNVSSARHSFRPTLPPVSQRGYPFNDPSYAPLPLRNQKPPMSTTFGVEKPHQYQQIITIVAPSRTTTPQLQPKSPSTPQAMRQQPKCTEGVSDEEFRNALKFVVDGTDPRSDLTDYKQIGEGSTGVVEAAYKISTKQIVAVKRMNLRKQQRRELLFNEVSILRQYQHPNIVRFFSSHLVDDELWVVMEFMEGGSLTDIVTATRMTEPQIATISRQVLGALDFLHARKVIHRDIKSDSILLKRDGTVKLTDFGFCGQLSEEVPRRRSLVGTPYWTAAEVIAREPYDTRADIWSFGIMLIEMVEGEPPFFNDQPFQAMKRIRDEHEARFSRHAKVSVELSELLSHCIVKDVNKRWPAKDLLRHPFFAKAQHSSSIAPLLLQLQGNTINGNNPPTHHHSSQITTVIQ
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q17850}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q17850}; Note=Divalent cations such as magnesium or manganese. {ECO:0000250|UniProtKB:Q17850};
|
intracellular signal transduction [GO:0035556]; nematode larval development [GO:0002119]; phosphorylation [GO:0016310]; regulation of MAPK cascade [GO:0043408]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; 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
| null | null |
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:Q17850}; 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:Q17850};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which plays a redundant role with pak-1 in embryogenesis but, in contrast to pak-1, is not involved in commissural axon guidance of ventral cord motoneurons or in distal tip cell (DTC) migration. {ECO:0000269|PubMed:17050621, ECO:0000269|PubMed:19797046}.
|
Caenorhabditis elegans
|
G5EFV3
|
RSA2_CAEEL
|
MSKIPVFKGSFKSWLAKNDEKPAKSVLLEPKYRDHHEKISFRNKENMEEGEKPVFVSMANPQPTREDYERYDEDRRLKDKARDLRIARRRNSATPEASPSSDQYFTPEPADDEFVTPSTSKKSQKPRSSDATPVSSKPPRYLPRTPLSEQYTSCLSRKMEENFSRMQELMISGHSPHEARQQTIQESSEQLEPRAKVTRSSSQPPPIDTLKPRVPRIESPLVKKTTETPIRRTSYVDTLVATHQIQLQYSDRVVVGVERQMTKLESIKNLAAANRSPIIAEEAKKRRNEAEAVRKLIEVETQNAKKRAVIQELKDRIDKLTQAQLAIHQLVSSQPFSGDPYNQRLLRSIDNWMALPFREFDIQTAREMLELARKMKITIDHFRNVATLHRNSKSLNRSLNTSRKSIAVKINPSSQLNQQSSSDAAPPPSMREASTQMTSRLAESAMTQTSPRRIGVEPLDLSQLLEKHNSSSQTTPPVVEPVLAEVSAEPQRPPVTLSMTAPVSTIAEFDSMLNSISLHNESLETVAEPFSRLKTDISFPSTVEETTPRSGRVSLDSESARRLSAGLSHYLEQVKKERESMEAQESESESMELEIPVVSEVSVTTESENLEEVVSEHSDSKSPETLVASDNGEDSSGGSEDPNATQFEHEIEEHKEPEKLGLIIDPEDEQDETKRFVNHDEFEQSLEEELEPRGNNDSADDSGFLLDNSPAPRLKSIFDNLPPAAASAAVTDTPRVPAEADETTFAGMDMEEYCQREFLKEISPIMVQKAIELQDELRGVDWLTAQDVWQPPSFKDVQMEFDDNFEYFDSFSILIWSAVVDLINKNYLKFGRKMTENEEIAFEAEALKMLQTEHGPESRKSEWCTDVKMSKKLEGMMPMELDYRYDVRRGLPDAEKQKYQWQQVQMTVIAARYANKNLINEANEVYATEKEKLGQMVLESEIDATVTDV
| null | null |
embryonic digestive tract development [GO:0048566]; mitotic spindle organization [GO:0007052]; protein localization to organelle [GO:0033365]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; protein phosphatase type 2A complex [GO:0000159]
|
beta-catenin binding [GO:0008013]; protein-macromolecule adaptor activity [GO:0030674]
| null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:25819561}.
| null | null | null | null | null |
FUNCTION: Recruits rsa-1 and, thereby, phosphatase let-92/paa-1 complex to the centrosomes (PubMed:17218259). Recruits sys-1/beta-catenin to mitotic centrosomes during the first embryonic cell divisions (PubMed:25819561). {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:25819561}.
|
Caenorhabditis elegans
|
G5EFV5
|
CDK7_CAEEL
|
MSRRYDTIKHLGEGQFANVYLAQDLESGECVAIKKIKLGSREEAKDGINRTAIREIKLLKEIHHDNIIGLRDVIGHRTSIQLVFDFMDTDLEHVIKDKEIILMPAHIKNITMQMLLGLEFLHVHWILHRDLKPNNLLMNKMGRVKLTDFGLARFFGSPNRNYTHQVVTRWYRAPELLFGARSYGVGIDIWSVGCIIAELLLRNPIFPGESDIDQLVKIFNILGCPTPETWPNMTEMNSYVIIKPQTEYMALNYYFSAAPQDLLDLMAGMWTFDPIKRLTCTQSLQMEYFRTQPFCCLDEELPLPKKQQPQKRSRRLDDDGTRPVRRLNFD
|
2.7.11.22; 2.7.11.23
| null |
cell division [GO:0051301]; mitotic cell cycle, embryonic [GO:0045448]; mRNA transcription [GO:0009299]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription factor TFIIH holo complex [GO:0005675]; transcription factor TFIIK complex [GO:0070985]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
| null | null |
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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P50613}; 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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P50613}; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; Evidence={ECO:0000269|PubMed:11960010};
| null | null | null | null |
FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Required for maintaining chromosome ploidy. May phosphorylate the large subunit of RNA polymerase II, ama-1. {ECO:0000269|PubMed:11960010}.
|
Caenorhabditis elegans
|
G5EFV8
|
VPS52_CAEEL
|
MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQLHNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDANDRGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEFLLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFSIGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVLKSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDARPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESKHTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECIQLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY
| null | null |
endocytic recycling [GO:0032456]; Golgi to vacuole transport [GO:0006896]; lysosomal transport [GO:0007041]; negative regulation of dense core granule transport [GO:1904810]; positive regulation of dense core granule transport [GO:1904811]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]
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cytosol [GO:0005829]; GARP complex [GO:0000938]; Golgi medial cisterna [GO:0005797]; Golgi trans cisterna [GO:0000138]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]
|
small GTPase binding [GO:0031267]; syntaxin binding [GO:0019905]
|
PF20655;PF04129;
| null |
VPS52 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. Co-localizes with the small GTPases rab-6.1 and rab-6.2 at Golgi structures (PubMed:21613545). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
|
Caenorhabditis elegans
|
G5EFW7
|
IF122_CAEEL
|
MRPNLLWVDKILDENNEAGVCIYDLAFKPDGSELLLAADNKVYLFDVNEGGQMQTLKGHKDLVYTVAWSHNGELFASGGADKLVILWNEKHEGTLRYSHTDVIQCMMFNPCNQILLTCALNEFGLWSTADKNVIKQRSVVRCCSCAWNTDGTIFAIGHGDGTITLRKGTNATEEPSIIIQRDNEPIWGIAFSSNRTFASRDSQGNPMGIDEIMAVIDWNKTLSFYSLDGTFIESKNLEFEPHCISYCLNGEYLLIGGSDKILKIYTRKGVLLGTVAQMDHWIWSVTVRPNSQTVAMGCVDGTIACYNLVFSTVHCVDHARYANRKSMTDVFVQNLEYRTSSNICCHDLVKKMSLYDTKLAVQLSDKIQIYKQTGGVSKNERRKQLKYTLQDTIRKDLSFSLMVVTHGHLVVCNDEKLECYDFKGIKKRSWNMKSIVRYLRVLGGPAHRETLVLGTTDGGVYKVFIDNDYPILLDSRKTAIKCIDINANRTVLASIEDTLVCKWSDIATGETLLQEPGCYSVVFNTVNENLFAFTTNNMLHVRTLAAPGHTTRGVGYVLGFVKNRTFCLVQYNLIPLEVPYTIHLYQYIERGDFKEALRIACLGVVKNDWKYLANKALDALEFDVARKAYKRVRDRKMLRMVWELKKMKSNGEPDAILRATILAYTKKFREAAKIFKENGFENRAMELFTDMRMFDDVQEVMTTASGETKKMLMRKRASWARDANQPKIAAEMLISSGDLDKAALLIIDNDWLELAIEISHKIDRSDLETMKKLSAYFIRKHEFGLASRIFQSINDMKSIVDMHVNAGHWTDAFAIADRHPKYVEDVYLPYARFLAERDRFEEAQKAFHRAGKEQEAMHVLEQLTSNSVNENRFADAGFYYWLLSQQYLDRSQTEENLTLLNKAKEAASLADAYYAYYPVFIFCSQPFSFERNENILNMARYLTFTPYIDNISKVFVYFTIAKIANEMGAYKSARTALDQLTNLRVLPQFELDGQIEVMTLNIRAKPFTDVESMQPMCYRCGLNNPLLGGMSCIHCETPFIISFVSFDILPLIEFKIENDISFDEAKELIESEPPLSDDDYNPLRGLKKGIKEIILNRESLSKLEQGHVIIQTFPPPLAPKFLFNVMPSITIAQCKGCNKVFDLDDFEMACLRKGHCPFCRTSYDRNEAFFVDEEEDEDNTNIPSFGQFSRFS
| null | null |
chemotaxis [GO:0006935]; cilium assembly [GO:0060271]; intraciliary retrograde transport [GO:0035721]; non-motile cilium assembly [GO:1905515]; positive regulation of dauer larval development [GO:0061066]; protein localization to cilium [GO:0061512]; receptor localization to non-motile cilium [GO:0097500]; regulation of dauer larval development [GO:0061065]; regulation of insulin receptor signaling pathway [GO:0046626]
|
ciliary basal body [GO:0036064]; cilium [GO:0005929]; intraciliary transport particle A [GO:0030991]; non-motile cilium [GO:0097730]
| null |
PF00400;
|
1.25.40.470;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000305|PubMed:11301258}. Note=Shuttles at the same rate as intraflagellar transport (IFT) complex B proteins such as osm-1, osm-5 and osm-6 along the cilia of the amphid and phasmid sensory neurons. {ECO:0000269|PubMed:11301258}.
| null | null | null | null | null |
FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs) (PubMed:28479320). Plays a role in chemotaxis and sensory perception (PubMed:7240452, PubMed:7705621). Required for entry into and exit from the dauer larval stage and this may be mediated by daf-12, daf-16 and daf-41 (PubMed:23284299, PubMed:25830239, PubMed:7240452). Controls the behavioral response, namely the avoidance response, and pathogen-responsive gene expression in the response to pathogenic bacteria such as E.coli and P. aeruginosa (PubMed:23284299). {ECO:0000269|PubMed:11301258, ECO:0000269|PubMed:23284299, ECO:0000269|PubMed:25830239, ECO:0000269|PubMed:28479320, ECO:0000269|PubMed:7240452, ECO:0000269|PubMed:7705621}.
|
Caenorhabditis elegans
|
G5EFX6
|
SLIT1_CAEEL
|
MLICFIFILLIPESATCPAECVCVDRTVSCVGQQLTEVPQNIPNDTIRLDLQDNEITKIGPNDFSSLMNLKALQLMDNQIVTIHNQSFSSLVFLQKLRLSRNRIRHLPDNVFQNNLKLTHLDLSENDITVVSDAQLQGPEFLEVLNLDKNHIFCLENNVISSWVSLEVLTLNGNRLTTFEEPSNARFRQLDLFNNPWNCDCRLRWMRKWLEKAEGQNKTVCATPLNLQGSSIEILQDKFMTCSGNRKRRYKKTCETAEICPLPCTCTGTTVDCRDSGLTYVPTNLPPSTTEIRLEQNQISSIPSHSFKNLKNLTRLDLSKNIITEIQPKAFLGLHNLHTLVLYGNNITDLKSDTFEGLGSLQLLLLNANQLTCIRRGTFDHVPKLSMLSLYDNDIKSISEVTFQNLTSLSTLHLAKNPLICDCNLQWLAQINLQKNIETSGARCEQPKRLRKKKFATLPPNKFKCKGSESFVSMYADSCFIDSICPTQCDCYGTTVDCNKRGLNTIPTSIPRFATQLLLSGNNISTVDLNSNIHVLENLEVLDLSNNHITFINDKSFEKLSKLRELRLNDNKLHHFSSMVLDEQSNLEILDLSGNNIQCFSSIFFNKATRIREIKVIGNDLLCDCRILPLMSWLRSNSSHSIDIPPCQQFQYSDNESDKQRCAAFPEETCSDDSNLCPPKCSCLDRVVRCSNKNLTSFPSRIPFDTTELYLDANYINEIPAHDLNRLYSLTKLDLSHNRLISLENNTFSNLTRLSTLIISYNKLRCLQPLAFNGLNALRILSLHGNDISFLPQSAFSNLTSITHIAVGSNSLYCDCNMAWFSKWIKSKFIEAGIARCEYPNTVSNQLLLTAQPYQFTCDSKVPTKLATKCDLCLNSPCKNNAICETTSSRKYTCNCTPGFYGVHCENQIDACYGSPCLNNATCKVAQAGRFNCYCNKGFEGDYCEKNIDDCVNSKCENGGKCVDLINSYRCDCPMEYEGKHCEDKLEYCTKKLNPCENNGKCIPINGSYSCMCSPGFTGNNCETNIDDCKNVECQNGGSCVDGILSYDCLCRPGYAGQYCEIPPMMDMEYQKTDACQQSACGQGECVASQNSSDFTCKCHEGFSGPSCDRQMSVGFKNPGAYLALDPLASDGTITMTLRTTSKIGILLYYGDDHFVSAELYDGRVKLVYYIGNFPASHMYSSVKVNDGLPHRISIRTSERKCFLQIDKNPVQIVENSGKSDQLITKGKEMLYIGGLPIEKSQDAKRRFHVKNSESLKGCISSITINEVPINLQQALENVNTEQSCSATVNFCAGIDCGNGKCTNNALSPKGYMCQCDSHFSGEHCDEKRIKCDKQKFRRHHIENECRSVDRIKIAECNGYCGGEQNCCTAVKKKQRKVKMICKNGTTKISTVHIIRQCQCEPTKSVLSEK
| null | null |
axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; dorsal/ventral axon guidance [GO:0033563]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neuron migration [GO:0001764]; regulation of sensory neuron axon guidance [GO:1905489]; sensory neuron axon guidance [GO:0097374]
|
extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]; signaling receptor binding [GO:0005102]
|
PF00008;PF12661;PF02210;PF00560;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as a ligand for sax-3 receptor during larval development. Acts via the sax-3/Robo receptor to direct ventral axon guidance and guidance at the midline during embryonic development. {ECO:0000269|PubMed:11604136}.
|
Caenorhabditis elegans
|
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