ID Q1LYI3_DANRE Unreviewed; 1552 AA. AC Q1LYI3; A0A8M1NTE1; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 2. DT 02-OCT-2024, entry version 134. DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485}; DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485}; GN Name=hecw1b {ECO:0000313|Ensembl:ENSDARP00000116253, GN ECO:0000313|RefSeq:NP_001139236.1, GN ECO:0000313|ZFIN:ZDB-GENE-060503-2}; GN Synonyms=hecw1 {ECO:0000313|RefSeq:NP_001139236.1}, si:ch211-106n13.1 GN {ECO:0000313|RefSeq:NP_001139236.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116253}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000116253, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116253}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000116253} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116253}; RG Ensembl; RL Submitted (AUG-2013) to UniProtKB. RN [3] {ECO:0000313|RefSeq:NP_001139236.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139236.1}; RX PubMed=25369329; RA Angers A., Drapeau P.; RT "Itch is required for lateral line development in zebrafish."; RL PLoS ONE 9:e111799-e111799(2014). RN [4] {ECO:0000313|RefSeq:NP_001139236.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139236.1}; RX PubMed=27259666; RA Chatterjee A., Lagisz M., Rodger E.J., Zhen L., Stockwell P.A., RA Duncan E.J., Horsfield J.A., Jeyakani J., Mathavan S., Ozaki Y., RA Nakagawa S.; RT "Sex differences in DNA methylation and expression in zebrafish brain: a RT test of an extended 'male sex drive' hypothesis."; RL Gene 590:307-316(2016). RN [5] {ECO:0000313|RefSeq:NP_001139236.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139236.1}; RX PubMed=28119690; RA Wan F., Hu C.B., Ma J.X., Gao K., Xiang L.X., Shao J.Z.; RT "Characterization of gammadelta T Cells from Zebrafish Provides Insights RT into Their Important Role in Adaptive Humoral Immunity."; RL Front. Immunol. 7:675-675(2017). RN [6] {ECO:0000313|RefSeq:NP_001139236.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139236.1}; RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [7] {ECO:0000313|RefSeq:NP_001139236.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139236.1}; RG RefSeq; RL Submitted (JUN-2024) to UniProtKB. 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:0000256|ARBA:ARBA00000885}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX005176; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX324139; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001139236.1; NM_001145764.1. DR STRING; 7955.ENSDARP00000116253; -. DR PaxDb; 7955-ENSDARP00000116253; -. DR Ensembl; ENSDART00000142835.2; ENSDARP00000116253.1; ENSDARG00000004291.10. DR GeneID; 563730; -. DR KEGG; dre:563730; -. DR AGR; ZFIN:ZDB-GENE-060503-2; -. DR CTD; 563730; -. DR ZFIN; ZDB-GENE-060503-2; hecw1b. DR eggNOG; KOG0940; Eukaryota. DR OMA; DPWTHIR; -. DR OrthoDB; 5480520at2759; -. DR PhylomeDB; Q1LYI3; -. DR TreeFam; TF313938; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000000437; Alternate scaffold 2. DR Proteomes; UP000000437; Chromosome 2. DR Bgee; ENSDARG00000004291; Expressed in retina and 8 other cell types or 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:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd08691; C2_NEDL1-like; 1. DR CDD; cd00078; HECTc; 1. DR CDD; cd00201; WW; 2. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.60.40.2840; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR037795; C2_HECW. DR InterPro; IPR050409; E3_ubiq-protein_ligase. DR InterPro; IPR000569; HECT_dom. DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase. DR InterPro; IPR040524; HECW1_helix. DR InterPro; IPR032348; HECW_N. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1. DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00632; HECT; 1. DR Pfam; PF18436; HECW1_helix; 1. DR Pfam; PF16562; HECW_N; 1. DR Pfam; PF00397; WW; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PROSITE-ProRule:PRU00104}. FT DOMAIN 190..326 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 770..803 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 967..1000 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 1217..1552 FT /note="HECT" FT /evidence="ECO:0000259|PROSITE:PS50237" FT REGION 355..381 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 425..505 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 558..727 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 831..870 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1147..1167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..504 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 576..591 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..620 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 831..847 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 848..870 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1147..1162 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1520 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104" SQ SEQUENCE 1552 AA; 175283 MW; EAA0E4AE10FB279D CRC64; MNEEVMIHRQ VILTQNLYQS RFLGLAAMAS PSRASQGRRR CKDPIRHSFN PEQFPNVDFQ NGVAEDLAAA VLRSTSDTDL LTSHCRSTLT VSTSSYTIGQ TQDITLSWDI KEEVDAGDWI GMYLIDEVLS ENFLDYKNRG VNGSHKGQII WKIEASSYFV EPETKICFKY YHGVSGALRA TTPCVTVKNP SAPVFKPVAT DDVPQSQGRR RLISFSLSDF QATGLKKGMF FNPDPYLKIA IHPGKHSIFP ALPHHGQEKR SGIVCNTINP VWQRERFNFV SLPTDVLEIE VKDKFAKSRP IIKRFLGKLS MPVQRLLEKH AIGDRVVSYT LGRRLPTEHV SGQLQFRFEI TSSIHPDDED MSLSTEQPVA AAEAQAQPQA EDTMSLDLGA PELPLDGDTA SVEMPMDVES GQSCAAEADV IEEECLEEEQ QEGEAAAAAA AMEQSETNAE ETTQVLDPIN GAEEEEAENN CAFAEESSDA RAGEEDEAIS DPQPASEEPD ADLEEDCSLR IRTTPRRKPR PCSLPVSELE TVIASACGEP ETPRSHYIRI HHLLHSLPAT QPQTGDSAGP EPDRPMGVEE EDEEEEEEGV TLEDHALTPN GPRRTLPRSR SHERLSDLIQ MLDGDGHPLG AEGQTGNQRS PDLSPVACCS HMSPRASGPI RAQSLDSARR SESTVFSSQD DEDEMEQPNG ILGSETETEQ GAQCREPGDG SCQWEEAPDS HVQSPHGIVG NGEVAGPSGR RECPLPCNHP AVSQLPALRP DPHHYPTIDE PLPPNWEARI DSHGRVFYVD HINRTTTWQR PTSAATPDGL RRSGSVQQME QLNRRYQTIQ RTMATERREE ESGSPRNDRT ANTETDSPLQ TNGDFTHITH NDRSSCSVKR LRRDTSCSPG HCQKITLLLQ SPAVKFITHP EFFTVLHANY GAYRMFTNSS CLKHMVLKIR RDARNFERYQ HNRDLVTFLN RFADAQLELP RGWEIKTDPQ GKSFFVDHNS RATTFIDPRI PLQNGRLPNH LTHRQHLQRL RSYSAGEASE VSRTRGVSLL ARPGNSLVAA IRNQSQQEPV PLAYNDKIVA FLRQPNIFEV LQERQPSFAR NHSLKDKVHH IRTEGTQRLE KLSCDADLVM LLSLFEEDIM SYVPLASFHP GFNFSPRCSP GSSPQNSPGT QRARAPAPYR RDFEAKLRNF YRKLEAKGYG QGPGKIKLIV RRDHLLEGTF NQVMAYSRKE LQRNKLYITF VGEEGLDYSG PSREFFFLLS QELFNPYYGL FEYSANDTYT VQISPMSAFV ENHLEWFRFS GRILGLALIH QYLLDAFFTR PFYKALLRLP TDLSDLEYLD EEFHQSLQWM KENDITDVLD LTFTVNEEVF GQVTERELKS GGTNVQVTEK NKKEYIERMV KWRVERGVVQ QTQALVRGFY EVVDSRLVSV FDARELELVI AGTAEIDLND WRNNTEYRGG YHDGHIVIRW FWGAVERFNN EQRLRLLQFV TGTSSVPYEG FTALRGSNGL RRFCIEKWGK ITSLPRAHTC FNRLDLPPYP SYTMLYEKLL IAVEETSTFG LE //