ID Q1LYI3_DANRE Unreviewed; 1552 AA. AC Q1LYI3; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 2. DT 31-JUL-2019, entry version 111. DE SubName: Full=HECT, C2 and WW domain-containing E3 ubiquitin protein ligase 1b {ECO:0000313|Ensembl:ENSDARP00000116253}; GN Name=hecw1b {ECO:0000313|Ensembl:ENSDARP00000116253, GN ECO:0000313|ZFIN:ZDB-GENE-060503-2}; GN Synonyms=hecw1 {ECO:0000313|ZFIN:ZDB-GENE-060503-2}, si:ch211-106n13.1 GN {ECO:0000313|ZFIN:ZDB-GENE-060503-2}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116253, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000116253, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116253, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.26; CC Evidence={ECO:0000256|SAAS:SAAS00628607}; 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; Q1LYI3; -. DR Ensembl; ENSDART00000142835; ENSDARP00000116253; ENSDARG00000004291. DR GeneID; 563730; -. DR KEGG; dre:563730; -. DR CTD; 563730; -. DR ZFIN; ZDB-GENE-060503-2; hecw1b. DR eggNOG; KOG0940; Eukaryota. DR eggNOG; COG5021; LUCA. DR GeneTree; ENSGT00940000158294; -. DR HOGENOM; HOG000069940; -. DR InParanoid; Q1LYI3; -. DR KO; K12167; -. DR OrthoDB; 117748at2759; -. DR PhylomeDB; Q1LYI3; -. DR TreeFam; TF313938; -. DR Proteomes; UP000000437; Chromosome 2. DR Bgee; ENSDARG00000004291; Expressed in 9 organ(s), highest expression level in brain. 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:0045732; P:positive regulation of protein catabolic process; 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: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; 2.60.40.150; -; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR037795; C2_HECW. 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 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; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF51045; SSF51045; 2. DR SUPFAM; SSF56204; SSF56204; 1. 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 Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|SAAS:SAAS00628615}; KW Ubl conjugation pathway {ECO:0000256|PROSITE-ProRule:PRU00104, KW ECO:0000256|SAAS:SAAS00593691}. FT DOMAIN 196 310 C2. {ECO:0000259|PROSITE:PS50004}. FT DOMAIN 770 803 WW. {ECO:0000259|PROSITE:PS50020}. FT DOMAIN 967 1000 WW. {ECO:0000259|PROSITE:PS50020}. FT DOMAIN 1217 1552 HECT. {ECO:0000259|PROSITE:PS50237}. FT REGION 355 381 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 425 505 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 558 727 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 831 870 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1147 1167 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 490 504 Acidic. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 576 591 Acidic. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 606 620 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 831 847 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 848 870 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 1147 1162 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT ACT_SITE 1520 1520 Glycyl thioester intermediate. FT {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 //