ID H0ZND1_TAEGU Unreviewed; 925 AA.
AC H0ZND1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=WWP1 {ECO:0000313|Ensembl:ENSTGUP00000012107.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000012107.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000012107.1, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000012107.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR RefSeq; XP_002199845.1; XM_002199809.3.
DR AlphaFoldDB; H0ZND1; -.
DR STRING; 59729.ENSTGUP00000012107; -.
DR Ensembl; ENSTGUT00000012241.2; ENSTGUP00000012107.1; ENSTGUG00000011745.2.
DR GeneID; 100219204; -.
DR KEGG; tgu:100219204; -.
DR CTD; 11059; -.
DR GeneTree; ENSGT00940000154635; -.
DR HOGENOM; CLU_002173_0_1_1; -.
DR InParanoid; H0ZND1; -.
DR OrthoDB; 5480520at2759; -.
DR TreeFam; TF323658; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007754; Chromosome 2.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
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; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 353..386
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 385..418
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 460..493
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 500..533
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 591..925
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 161..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..125
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 176..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 893
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 925 AA; 104964 MW; 092725D8A0FA2E9D CRC64;
MATASPRSDT SHNCNGRLQM QVTVSSAKLK RKKNWFGTTF YTELTADGEI KKTAKSSSSS
NPKWDEQLTV NVTPQTTLEF RVWSHHTLKA DALLGRATVD LRQALEVHNR KLEKVKEQLK
LSLENKSGMV QTGELTVVLD GLVVEQESLT NLSSSATIEV QQNGEAVHES RDASARSSSR
SACDISNGID NQVPSSSVMQ NTFCVEAVNG DSTQSPNHVA ARPKNTPVPK PLEAQPVNST
VNGESSASAP EAGNSSVSEA PTGSVEAPVS SADCTNDTAE PQSATEATSC SESHSSASPV
VSAGLEPAAA TECAQPNARN SIAADAAKPR ESSSTPSASA EPVRQQPSST STEPLPPGWE
QRKDPHGRTY YVDHNTRTTT WERPQPLPPG WERRVDDRGR VYYVDHNTRT TTWQRPTMES
VRNFEQWQSQ RNQLQGAMQQ FNQRYLYSAS MLSAENDPLG PLPPGWERRV DSNDRVYFVN
HNTKTTQWED PRTQGLQNED PLPEGWEIRY TREGVRYFVD HNTRTTTFND PRTGKSSVNK
GPQIAYERSF RWKLAHFRYL CQSNALPSHV KINVSRQTLF EDSFQQIMAL KPYDLRRRLY
VIFRGEEGLD YGGLAREWFF LLSHEVLNPM YCLFEYAGKS NYCLQINPAS TINPDHLSYF
CFIGRFIAMA LFHGKFIDTG FSLPFYKRML SKKLTIKDLE SIDTEFYNSL IWIRDNNIEE
CNLEMYFCVD MELLGKVTSH ELKSGGSNIL VTEENKEEYI GLMAEWRFSR GVREQTKAFL
DGFNEVVPLQ WLHYFDEKEL EVMLCGMQEV DLADWQRNTV YRHYTRNSKQ IIWFWQFVKE
TDNEVRMRLL QFVTGTCRLP LGGFAELMGS NGPQKFCIEK VGKETWLPRS HTCFNRLDLP
PYKSYEQLKE KLLFAIEETE GFGQE
//