HECW1_CAEEL
ID HECW1_CAEEL Reviewed; 1247 AA.
AC Q09291; A0A1C3NSJ1; G5EEJ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=E3 ubiquitin-protein ligase hecw-1 {ECO:0000305};
DE EC=2.3.2.26 {ECO:0000250|UniProtKB:Q76N89};
GN Name=hecw-1 {ECO:0000303|PubMed:22089131, ECO:0000312|WormBase:F45H7.6c};
GN ORFNames=F45H7.6 {ECO:0000312|WormBase:F45H7.6c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22089131; DOI=10.1038/nature10643;
RA Chang H.C., Paek J., Kim D.H.;
RT "Natural polymorphisms in C. elegans HECW-1 E3 ligase affect pathogen
RT avoidance behaviour.";
RL Nature 480:525-529(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity). Functions in the
CC OLL neurons in the anterior ganglion to inhibit avoidance to microbial
CC pathogens such as P.aeruginosa although worms do display avoidance
CC behavior, vacating a P.aeruginosa lawn within 24 hours
CC (PubMed:22089131). Likely to act by inhibiting the neuropeptide
CC receptor npr-1 (PubMed:22089131). {ECO:0000250|UniProtKB:Q76N89,
CC ECO:0000269|PubMed:22089131}.
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:0000250|UniProtKB:Q76N89};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q76N89}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q76N89}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:F45H7.6b};
CC IsoId=Q09291-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F45H7.6a};
CC IsoId=Q09291-2; Sequence=VSP_059536;
CC Name=c {ECO:0000312|WormBase:F45H7.6c};
CC IsoId=Q09291-3; Sequence=VSP_059537;
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system throughout the
CC body. In the anterior ganglion, expression is limited to the two
CC lateral outer labial neurons OLLL and OLLR.
CC {ECO:0000269|PubMed:22089131}.
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DR EMBL; BX284603; CAA84325.2; -; Genomic_DNA.
DR EMBL; BX284603; CAA86770.1; -; Genomic_DNA.
DR EMBL; BX284603; SBV53365.1; -; Genomic_DNA.
DR PIR; T20271; T20271.
DR RefSeq; NP_001317872.1; NM_001330981.1. [Q09291-1]
DR RefSeq; NP_497697.2; NM_065296.3. [Q09291-2]
DR RefSeq; NP_497698.1; NM_065297.1.
DR AlphaFoldDB; Q09291; -.
DR SMR; Q09291; -.
DR BioGRID; 48680; 1.
DR STRING; 6239.F45H7.6; -.
DR PaxDb; Q09291; -.
DR PeptideAtlas; Q09291; -.
DR EnsemblMetazoa; F45H7.6a.1; F45H7.6a.1; WBGene00009738. [Q09291-2]
DR EnsemblMetazoa; F45H7.6b.1; F45H7.6b.1; WBGene00009738. [Q09291-1]
DR GeneID; 175438; -.
DR KEGG; cel:CELE_F45H7.6; -.
DR UCSC; C56G7.2; c. elegans. [Q09291-1]
DR CTD; 175438; -.
DR WormBase; F45H7.6a; CE44269; WBGene00009738; hecw-1. [Q09291-2]
DR WormBase; F45H7.6b; CE51746; WBGene00009738; hecw-1. [Q09291-1]
DR WormBase; F45H7.6c; CE01532; WBGene00009738; hecw-1. [Q09291-3]
DR eggNOG; ENOG502TGI5; Eukaryota.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000173012; -.
DR HOGENOM; CLU_324458_0_0_1; -.
DR InParanoid; Q09291; -.
DR OMA; QWMELAG; -.
DR OrthoDB; 25515at2759; -.
DR PhylomeDB; Q09291; -.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q09291; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00009738; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:WormBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR012885; F-box-assoc_dom_typ2.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF07735; FBA_2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1247
FT /note="E3 ubiquitin-protein ligase hecw-1"
FT /id="PRO_0000065258"
FT DOMAIN 602..635
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 745..777
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 914..1247
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 633..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1215
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT VAR_SEQ 1..373
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059536"
FT VAR_SEQ 368..1247
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_059537"
SQ SEQUENCE 1247 AA; 144050 MW; 47AAECB3C04FC738 CRC64;
MGDEFPFHHL GYVCLNEIYK HLTLKEIFQL SFSSNQIKRS LGIASIPVKS IFVNFDSQYP
KIKLIGESSQ LEWVFGIPDG LEYTDVGVYK IGHFKFQCKT SGTAFYTEHY DLENAMLVVI
RYMISIFKCS NSIITYLSID LGVIEDSRAI CENFVAFKKV ERLSIFQTNY GVERNTLNFA
QSFDWICDNL EIKNIHIGAD VLEPKMVQKT NGEFDIKLCA RRFEQVLTMD HIYLQHADWI
TSEDLLNLDV QTAMLIENNL TEQDLNAFIK QWLRSDSDKL WWLEVKGKMM FNREEVLKDL
DVQDDAYRSL NTRWYVARRS RANPSGNGCA RKKMGSLRPK LTELWPFKVY IIFGSILIVF
GPAALNRMIT LRRMDVETDR PSGSETGIFV SKSAVYPFGN KNEVVKVWWN IDKPENCLDW
IGLFDNNDSS FYLDQKSLRQ HISPVVFTLT SKNLLNASEV YFGLIDGMTG RLLAKSENVE
ICKSASLVVH EVKKPENINV YLNTNHGRIE IPKKRSFSRK NGSFRSSFEF DFDVEDLHIS
LVENSEKLNF DHFIASNQLQ NNYIQSKSFS HSHVVEIVFS IEPKTSKKSA PDIMEIASSS
QTPPESHWKT YLDAKKRKFY VNHVTKETRW TKPDTLNNNH IEPETPVHKR LSDRSASPRN
SFITPRRTIT VRSAGCPKSD LIQFFQRDEF KTALYENQDA MQIYNECSVV RHAIHRIQKD
LDPPSKFENQ PLFVRFVNLF ADITQPLPSG WECITMNNRT VFLNHANKET SFYDPRIRRF
ETKTSRRGRS VPSRSSTAHK GKIDHALISK CEDLRKIAQD NFPQIAERIS KKLMLIERFG
GLAVASLAND LDITLALSML DSNTEKLAGE GDNIKMFYED MKKEKLGKGP SRLCWKVSRD
RLLDDAFRII LNVDPFVLKK SRLHIRFEGE LALDYGGLSR EFFILLSREL FHPKNGYFEY
EGNDYHLQLR PRGCETEKEK KWLILCGRVL ALAVIHRCYI DVFFTNVFYK SLQKRPVTLM
DFKESDAEFY KSMNWLLEND VVDLEMSFVY SSMVNGKLAE QELVPGGESQ MVTEANKAEF
IDLMCQKKAI RGVEKPLEIL LTSFNQILND NLLNSLESSD LKRILSGSLE LDLNDWRTNT
IYKGGYSDCH IVVEWFWEVI ETMTNQERFD LLLFVTGSSS VPFEGFSALR GNEEISKFCI
EKWGDATSFP RAHTCFNRLQ LPSYNTKQQL KSKLQQAIVN GMSYSIE
