ID A0A1L8H7Z4_XENLA Unreviewed; 713 AA.
AC A0A1L8H7Z4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 40.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=rnf19b.S {ECO:0000313|RefSeq:XP_018105082.1,
GN ECO:0000313|Xenbase:XB-GENE-17332473};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018105082.1};
RN [1] {ECO:0000313|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J_2021 {ECO:0000313|Proteomes:UP000186698};
RG RefSeq;
RL Submitted (JUN-2024) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_018105082.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018105082.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018105082.1};
RG RefSeq;
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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DR RefSeq; XP_018105082.1; XM_018249593.2.
DR AlphaFoldDB; A0A1L8H7Z4; -.
DR STRING; 8355.A0A1L8H7Z4; -.
DR PaxDb; 8355-A0A1L8H7Z4; -.
DR GeneID; 108709599; -.
DR KEGG; xla:108709599; -.
DR AGR; Xenbase:XB-GENE-17332473; -.
DR CTD; 108709599; -.
DR Xenbase; XB-GENE-17332473; rnf19b.S.
DR OMA; EQEQTCK; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 108709599; Expressed in testis and 19 other cell types or tissues.
DR GO; GO:0044194; C:cytolytic granule; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16776; RING-HC_RBR_RNF19B; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000424; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 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; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW 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}.
FT TRANSMEM 349..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 83..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 77470 MW; 0B25C02E23827448 CRC64;
MLPCLRNIPR SRLTHHFCPY MGGSFNVPSI MRLRNFQLVR LLTSWFGIFC LPEMTEGSAE
PPPCPGARRR RLLLSLPNVF PGRTRAAPEP SVPSPPPSPP PPVSVSPPPS SPGGSESLIE
CPLCLVRQPP EELPELLSCR HRSCLRCLRQ YLRIEICESR VNLRCPECAE RLSPQHVRAI
LRDPLLTRKY EEFLLRRCLA SDPDCRWCPA PDCGYAVIAY GCASCPKLTC EREGCQAEFC
YHCKHVWHPN QTCDMARQQR APSLGVRRKH PSGISYGQES GSADDMKSCP RCSAYIIKMN
DGSCNHMTCS VCGCEFCWLC MKEISDLHYL SPSGCTFWGK KPWSKKKKII WQLGTLIGAP
VGISLIAGIA IPAMVIGIPV YVGRKIHGRF ENKKTSRHKK NLAITGGVIL SVIASPVVAA
VSVGIGVPIM LAYVYGVVPV SLCRGGGCGV STANGKGVKI DFEEDGPITV ADAWRALKNP
SIGESSMEGL TSVLSTSGSP TDGLSVLQGN YSETASFAAL SGGTLTGGML SGGRAKYCRL
EVQADVQKET CQKDSVSLGA VSDSASTRAM AGSIISSYNP QEREVNNVEI QVHIEAKPSR
YQLMSESSTE ESLHAAAPLV EGEDDEACRN QVTACDITLA QPESIRSDLE SSDAQSDDVP
DLASEEYDSP HLCPPSPSNS LQESPPHRMC SQEEGLCARE EGLSKVEFIE VRV
//
