ID G3P9I6_GASAC Unreviewed; 641 AA.
AC G3P9I6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 2.
DT 18-JUN-2025, entry version 72.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000014260.2, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000014260.2, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000014260.2,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000014260.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR RefSeq; XP_040016693.1; XM_040160759.1.
DR RefSeq; XP_040016694.1; XM_040160760.1.
DR AlphaFoldDB; G3P9I6; -.
DR STRING; 69293.ENSGACP00000014260; -.
DR Ensembl; ENSGACT00000014285.2; ENSGACP00000014260.2; ENSGACG00000010774.2.
DR GeneID; 120808121; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000165084; -.
DR InParanoid; G3P9I6; -.
DR OMA; FPVFETD; -.
DR TreeFam; TF324777; -.
DR Proteomes; UP000007635; Chromosome XVIII.
DR Bgee; ENSGACG00000010774; Expressed in camera-type eye and 3 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20338; BRcat_RBR_RNF19; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 349..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..339
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 120..167
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 70041 MW; 1D50A44FDCAA6E93 CRC64;
MKRPKQQTGP LSFLNFFTRK PKSEPKVERP LEAWPREEVA ITLTPSEQPR QDLSLTAEEA
GGEREEGGGP PPAAAAAAVA VEDNAAAAEC AGGVLSGSTG VLSVSSSSQE QLLDEHLEEC
PLCLLSQPRC HFPRLTSCSH RTCSDCLRQY LRIEISESRV GIACPQCPET LAPLDVRAIL
DDQALLERYE EYQLRRYLAA DPDTRWCPAP DCSYAVIAYG CAECPKLSCG REGCDTEFCY
HCRQLWHPNQ TCDQARRQRA RHTSGGTDAS TLYVFNEEPG GDAEEIKACP RCGAYIMKTN
DGSCNRMNCT VCACQFCWLC MQEITDVHYL SPSGCTFWGK KPWSQTRKVL WQVGMLLGAP
VVISLIAGIA IPVIIVGIPI YMGRKVHGRC KKNNISGSKH YLTVASGVMM SVFVSPVIAA
ITVGVGVPLM LTYVYGVVPM SLCRNGWCRP QSEPPETHKI QLEDLASYLL FSHVVSDHWT
GQNKSTPSDT SVQEVRVSVQ EVGVLPSTSA TPPELDSYEE LDEATKPHGY SQSDCQVVIV
PDGALNDPQA TPLREGTNIE VRVEIETHPR GARQSSLSSI LSSRSLSVES LGHSRSLSQD
YLCASELEGR REGGEGEEQE GREKPGGDEG TVLPVFEIEG V
//
