ETC1_CAEEL
ID ETC1_CAEEL Reviewed; 1001 AA.
AC O17736; Q18992;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=E3 ubiquitin-protein ligase etc-1 {ECO:0000305};
DE EC=2.3.2.26 {ECO:0000269|PubMed:23578927};
DE AltName: Full=HECT-type E3 ubiquitin transferase {ECO:0000305};
GN Name=etc-1 {ECO:0000303|PubMed:23578927};
GN ORFNames=D2085.4 {ECO:0000312|WormBase:D2085.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH IFY-1 AND CYB-1, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23578927; DOI=10.1242/dev.090688;
RA Wang R., Kaul Z., Ambardekar C., Yamamoto T.G., Kavdia K., Kodali K.,
RA High A.A., Kitagawa R.;
RT "HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic abundance
RT to promote timely anaphase during meiosis in C. elegans.";
RL Development 140:2149-2159(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes, such as ubc-18, in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates. Ubiquitinates ify-1 and cyb-1 targeting them for
CC degradation in post-meiotic embryos. {ECO:0000269|PubMed:23578927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000255, ECO:0000269|PubMed:23578927};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23578927}.
CC -!- SUBUNIT: Interacts with ify-1 and cyb-1. {ECO:0000269|PubMed:23578927}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC progeny viability. ify-1 and cyb-1 accumulate in the cytoplasm during
CC meiosis II. Also extents the length of meiosis II and causes retention
CC of rec-8, a component of the cohesin complex, at sister chromatid
CC cohesion. Causes a delay in oocyte budding.
CC {ECO:0000269|PubMed:23578927}.
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DR EMBL; BX284602; CAA91061.1; -; Genomic_DNA.
DR PIR; T20373; T20373.
DR RefSeq; NP_495842.1; NM_063441.4.
DR AlphaFoldDB; O17736; -.
DR SMR; O17736; -.
DR STRING; 6239.D2085.4; -.
DR EPD; O17736; -.
DR PaxDb; O17736; -.
DR PeptideAtlas; O17736; -.
DR EnsemblMetazoa; D2085.4.1; D2085.4.1; WBGene00008429.
DR GeneID; 174388; -.
DR KEGG; cel:CELE_D2085.4; -.
DR UCSC; D2085.4; c. elegans.
DR CTD; 174388; -.
DR WormBase; D2085.4; CE15744; WBGene00008429; etc-1.
DR eggNOG; KOG0942; Eukaryota.
DR GeneTree; ENSGT00940000156321; -.
DR HOGENOM; CLU_002173_2_2_1; -.
DR InParanoid; O17736; -.
DR OMA; IRVQMVN; -.
DR OrthoDB; 1163565at2759; -.
DR PhylomeDB; O17736; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O17736; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008429; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1902104; P:positive regulation of metaphase/anaphase transition of meiotic cell cycle; IMP:WormBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:1905189; P:regulation of metaphase/anaphase transition of meiosis II; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR044611; E3B/C.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR45700; PTHR45700; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Meiosis; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1001
FT /note="E3 ubiquitin-protein ligase etc-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440175"
FT DOMAIN 28..57
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 658..1001
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT COILED 66..115
FT /evidence="ECO:0000255"
FT ACT_SITE 969
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1001 AA; 116415 MW; C879F6082C86AF43 CRC64;
MIKSLNERDN FLNRLREMEH KREKDEKQEK AARKVQKFWR GHRVQHNQRL LFRAEFDAVS
DRQRGLEETI KMAQLLVNFY ETNKDEERLV MTLSELVKLK TSDKEFEKRI RETQRLLLAR
CCIKFLKNAT ENTIFFHIFR YLEDYVTCHS KLFEASSKLG LFNAEFHLLE ALIGKPTGKT
VERASLNPRI LQLLTRIFET FVNPSRSTSV SVNVANRLLK TICVNITDLN FSNYILYYIK
DHIKPTSPNF TNLFEAMKSV DILNNWKVRP EIAETASLRL QSIFVSQIVH VSNTQSEDVK
QYFNSLAVFL EHHSKIMRSL NVKEDLSEFG RLRTSVNNHL KQYCEEMLIS NEFRRAACIY
ANLPGVQVET IISLRKYFSQ FLDLLAASNT FVEALYAFIA RLCPNGEFDP IDAKSPKVNA
LELFCNCLNK RVSSVADSDF VPTDIFVDFD HTVEFLRDVS IKLIHLMFPT MARGDLYSGN
LKEKMYKAET DWKDVTESVF SILGAIYQKD IRLKYFPEEF WTNHGREVLS GIGEHRRMPR
RRMPNGRLQI ERTMDTEFVE RLAAIYEMDS DSENDDEDED NNLPAVLRRA ICVMKHIPFI
VPFMDRVKLF TRLLNQDKEK HYTSTFGMGF NGPSVTVRRD QVYMDAFETF APKMQGDKVN
DLKSMVRVKM VNWAGMNESG IDGGGIFREF LSELLKTAFN VERGFFTFTE SKLLYPNPTA
PFLLGVDCLA HFQFIGRMIG KLIYERQLQE VRFAEFFIAQ IFETDKNKDV DLQHMKSFDP
IIFKHLKALQ KMNNRELDEL QLDFSVVTSD MGLVRNVNLK PNGSKFRVTV ENVHEYVRLY
VNYHLKQRIA SMVDAVRKGI SEIISIEWMR MFAPHELQIM IAGYEEVFTA KELRKFCELR
FAAGTQDINY EEMFWDVIDK LSNDDKKALL KFVTGCSRAP VDGFKSIQPR MGVLVIPSSD
DELPTSATCM NMLRIPKYSN RTKLEEKLRY AINSGAGFEL A
