ID A0A3P8PVZ7_ASTCA Unreviewed; 787 AA.
AC A0A3P8PVZ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000021064.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000021064.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000021064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8PVZ7; -.
DR Ensembl; ENSACLT00000021546.1; ENSACLP00000021064.1; ENSACLG00000014241.1.
DR GeneTree; ENSGT00940000157014; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265100; Chromosome 20.
DR Bgee; ENSACLG00000014241; Expressed in liver and 8 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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:SF66; E3 UBIQUITIN-PROTEIN LIGASE ITCHY HOMOLOG; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..117
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 216..243
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 242..275
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 322..355
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 362..395
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 453..787
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 755
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 787 AA; 92340 MW; 4820833A16F65D58 CRC64;
MASGATKSGT SNGYPIRAQL QIVVLSAKLK ENKKNWFGPS PYVEVTVDGQ SKKTEKCTNT
HSPKWKQPLT VIVTPFSKLV FRVWSHQTLK SDLLLGMATL DLSETLKSND MKISEVVQTL
QLCADRDESD VVGDLSVCLD GMTVDPDMFA KAEADHHSES RKSTKRNLHW KHVKFFILCC
HFFVLFYRTF IFLFLVVSCT IKKSGLNFII VPFSRWEQRV DQNGRLYYVD HVEKKTTWER
PEPLPHGWER RVDQMGRVYF VDHMTRTTTW QRPTVESVRN YEQWQHQRSQ LQGAMQQFNQ
RFIFGAQDQA TATQNKEYDP LGPLPQGWEK RTDSNGRVYF VHHPTRSTQW EDPRTQGLLN
EKPLPEGWEM RFTVDGIPYF VDHTRRTTTY IDPRTGKSSL ENGPQITYVR DFKAKVQYFR
FWCQQLAMPQ HVKINVSRKT LFEDSFQQIM SLNAQDLRRR LWIIFPGEEG LDYGGVSREW
FFLLSHEVLN PMYCLFEYAG KDNYCLQINP ASYINPDHLK YFKFIGRFIA MALFHGKFID
TGFSLPFYKR ILNKPLTLHD LESIDPEFYN SLMWIKDNNI EECGLEMFFS VDKEILGEIS
THELKPGGGD IQVTEENKEE YIRLVAEWRL SRGVEEQTQA FFEGFNEVLP QQYLQYFDAK
ELEVMLCGMQ EIDLVDWQRN TIYRHYARSS KQIVWFWQLV KEMDNEKRMR LLQFVTGTCR
LPVGGFNDLM GSNGAQKFCI EKVGKENWLP RSHTCFNRLD LPPYKSYEQL KEKLMFAIEE
TEGFGQE
//
