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Database: UniProt
Entry: H0VDF2_CAVPO
LinkDB: H0VDF2_CAVPO
Original site: H0VDF2_CAVPO 
ID   H0VDF2_CAVPO            Unreviewed;      1566 AA.
AC   H0VDF2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=HECW2 {ECO:0000313|Ensembl:ENSCPOP00000008002.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000008002.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000008002.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000008002.3};
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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DR   EMBL; AAKN02051331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003463417.2; XM_003463369.3.
DR   STRING; 10141.ENSCPOP00000008002; -.
DR   Ensembl; ENSCPOT00000008988.3; ENSCPOP00000008002.3; ENSCPOG00000008908.4.
DR   VEuPathDB; HostDB:ENSCPOG00000008908; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   GeneTree; ENSGT00940000155466; -.
DR   HOGENOM; CLU_002173_14_0_1; -.
DR   InParanoid; H0VDF2; -.
DR   OMA; TAGQHRE; -.
DR   OrthoDB; 5480520at2759; -.
DR   TreeFam; TF313938; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000008908; Expressed in frontal cortex and 10 other cell types or tissues.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
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; 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:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 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; 1.
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:UP000005447};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          171..301
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          801..834
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          979..1012
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1231..1566
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          342..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1010..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1534
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1566 AA;  174919 MW;  C9EAF7E0505B181B CRC64;
     MASSAREHLL FVRRRNPQMR YTLSPENLQS LAAQGSLPEN MTLPRANSDT DLVTSESRSS
     LTASMYEYTL GQAQNLIIFW DIKEEVDPSD WIGLYHIDEN SPANFWDSKN RGVTGTQKGQ
     IVWRIEPGPY FMEPEIKICF KYYHGISGAL RATTPCITVK NPAVMMGAEG TEGGMSGSLH
     SRKLVSFTLS DLRAVGLKKG MFFNPDPYLK MSIQPGKKSS FPTCAHHGQE RRSTIISNTT
     NPIWHREKYS FFALLTDVLE IEIKDKFAKS RPIIKRFLGK LTIPVQRLLE RQAIGDQMLS
     YNLGRRLPAD HVSGYLQFKV EVTSSAHEDA SPEAVGTILG VSTVNGDLGS PSDDEDMPGS
     HQDSPGCANG AVSEDSTADG TPKHSFRTSS TLEMDAEELT STSSRTSPPR GRQDSLNDYL
     DALEHDGPAR PGATASERPM GASPKLRSSF PTDTRLSAML HIDSDEEDHE LQQDLGYPSS
     LEEEGGLIML SRPSRADEGS LTSQTKSEDT NLVDLEEHSV LEAVSQEDKP EDLPELADGP
     LDAAPEDGEA AGPDSHPEVE QGSTKLCGSQ EAEQPASGAD TGTPDTSGGS RRAISETESL
     DQGSEPSQVS SETEPSDPAR TESVSEASTR PEGESDLEGA DSSCNDSVAT QLSSLESARP
     PGTPAFSSQE DEDGACAAAA AEPPSRGPGP EPACTPGTGM LPAVQVPEAQ EDAGPEPKDL
     GEIWQRRAGL EGASAIENES RSQALEEEEA QEDMGEDARA CEGAAALEEG AAGGSPANGH
     QPLRSLPSVR QDVSRYQRVD EALPPNWEAR IDSHGRIFYV DHVNRTTTWQ RPTAPPAPQV
     LQRSNSIQQM EQLNRRYQSI RRTMTNERPE ESASAMDGAG EEVDFHQTSA DFRRESVLPH
     STSRSRLALL LQSPPVKFLI SPEFFTVLHS NPSAYRMFTN NTCLKHMITK VRRDTHHFER
     YQHNRDLVGF LNMFANKQLE LPRGWEMKHD HQGKAFFVDH NSRTTTFIDP RLPLQSSRPT
     SALAHRQHLT RQRSHSAGEV GEDSRHAGPP VLPRPSSTFN TVNRPQYQDM VPVAYNDKIV
     AFLRQPNIFE ILQERQPDLT RNHSLREKIQ FIRTEGTPGL VRLSSDADLV MLLSLFEEEI
     MSYVPPHALL HPSYCQSPRG SPVSSPQNSP GTQRANARAP APYKRDFEAK LRNFYRKLET
     KGYGQGPGKL KLIIRRDHLL EDAFNQIMGY SRKDLQRNKL YVTFVGEEGL DYSGPSREFF
     FLVSRELFNP YYGLFEYSAN DTYTVQISPM SAFVDNHHEW FRFSGRILGL ALIHQYLLDA
     FFTRPFYKAL LRILCDLSDL EYLDEEFHQS LQWMKDNDIH DILDLTFTVN EEVFGQITER
     ELKPGGANIP VTEKNKKEYI ERMVKWRIER GVVQQTESLV RGFYEVVDAR LVSVFDAREL
     ELVIAGTAEI DLSDWRSNTE YRGGYHDNHI VIRWFWAAVE RFNNEQRLRL LQFVTGTSSI
     PYEGFASLRG SNGPRRFCVE KWGKITALPR AHTCFNRLDL PPYPSFSMLY EKLLTAVEET
     STFGLE
//
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