ID A0A2D0RYM9_ICTPU Unreviewed; 853 AA.
AC A0A2D0RYM9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin-protein ligase E3A {ECO:0000256|PIRNR:PIRNR037201};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR037201};
GN Name=ube3a {ECO:0000313|RefSeq:XP_017335605.1,
GN ECO:0000313|RefSeq:XP_017335606.1, ECO:0000313|RefSeq:XP_017335607.1,
GN ECO:0000313|RefSeq:XP_017335608.1, ECO:0000313|RefSeq:XP_017335609.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017335608.1};
RN [1] {ECO:0000313|RefSeq:XP_017335605.1, ECO:0000313|RefSeq:XP_017335606.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017335605.1,
RC ECO:0000313|RefSeq:XP_017335606.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC transfers it to its substrates. {ECO:0000256|PIRNR:PIRNR037201}.
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|PIRNR:PIRNR037201};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|PIRNR:PIRNR037201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037201}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR037201}.
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DR RefSeq; XP_017335605.1; XM_017480116.2.
DR RefSeq; XP_017335606.1; XM_017480117.3.
DR RefSeq; XP_017335607.1; XM_017480118.3.
DR RefSeq; XP_017335608.1; XM_017480119.3.
DR RefSeq; XP_017335609.1; XM_017480120.3.
DR STRING; 7998.ENSIPUP00000032728; -.
DR Ensembl; ENSIPUT00000034020; ENSIPUP00000032728; ENSIPUG00000021987.
DR Ensembl; ENSIPUT00000034031; ENSIPUP00000032739; ENSIPUG00000021987.
DR GeneID; 108272034; -.
DR KEGG; ipu:108272034; -.
DR CTD; 7337; -.
DR OMA; AHCTNAN; -.
DR OrthoDB; 5471864at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000221080; Chromosome 11.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR017134; UBE3A.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037201};
KW Ligase {ECO:0000313|RefSeq:XP_017335605.1,
KW ECO:0000313|RefSeq:XP_017335606.1};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037201};
KW Proteasome {ECO:0000256|PIRNR:PIRNR037201};
KW Transferase {ECO:0000256|PIRNR:PIRNR037201};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037201}.
FT DOMAIN 525..853
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 821
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 853 AA; 96990 MW; 57AE97F2CDFB7242 CRC64;
MKRAAAKHLI ERYYHQLTEG CGNEACTNEA CGSSPGFRRM DNNAAAIKAL ELYKNNAKLC
DPHPSKKGAS SAFPENSAKG ALNFSACSNG KMNHKDLPPT REDFRDLNYL TEEKVYEILS
VCDETEDYSP LIRVIGRVFS NAESLVQSFR KAKQHTKEEL KSLQAKDEDK DEDEKEAASA
CAAAAMEVDP DAASSSEGAS DVNVRKPVEV SVDIEAVRRV YDRLLSNEKV EAAFLNALVY
LSPNVECDLT YHNAYAADPD YLNVFIIVME NSNLHSPEYL EMALPQFCKA MSKLPLPALA
KLARLWAQHG AEHIRRLLET FQQLITYTVI SNEFNGDNLV NEDDGVVAAT KCLKVVYYAN
ILGGDLDIGH SEDEDDEPIA ESSELTLQEL LGEERRAKKG PRVDPLETEL GVRVSDCRSP
LVPFDEFINE PLNDVLEMDK DYTFFKVETE SKFSFMTCPF ILNAVTKNLG LYYDNRIRMY
SERRITALYS LVQGQQLNPY LRLKVRRDHV IDDALVRLEM IAMENPADLK KQLYVEFEGE
QGVDEGGVSK EFFQLVVEEI FNPDIGMFTY DESTKLFWFN PSSLENEGQF TLIGIVLGLA
IYNNCILDVH FPMVVYRKLM GKKGTFRDLA DSHPILHQSL KELQEYEGNV EDDMMITFQI
SQTDLFGNPL MYDLREGGDK IPVTNDNRKE FVELYAEYML NKSVEKQFKA FRRGFHMVTN
ESPLKYLFRP EEIELLICGS RNLDFQALEE TTEYDGGYSK DCRIIKYFWE TVHSFEQEQK
RLFLQFTTGT DRAPVGGLGK LKMIIAKNGP DSDRLPTSHT CFNVLLLPEY STKEKLRERL
LKAITYAKGF GML
//
