ID A5D8L1_XENLA Unreviewed; 168 AA.
AC A5D8L1;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=rnf5.L {ECO:0000313|RefSeq:NP_001092153.1,
GN ECO:0000313|Xenbase:XB-GENE-974974};
GN Synonyms=LOC100049739 {ECO:0000313|EMBL:AAI41717.1}, rnf5
GN {ECO:0000313|RefSeq:NP_001092153.1,
GN ECO:0000313|Xenbase:XB-GENE-974974};
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|EMBL:AAI41717.1};
RN [1] {ECO:0000313|RefSeq:NP_001092153.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI41717.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fat bodies {ECO:0000313|EMBL:AAI41717.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001092153.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; BC141716; AAI41717.1; -; mRNA.
DR RefSeq; NP_001092153.1; NM_001098683.1.
DR GeneID; 100049739; -.
DR KEGG; xla:100049739; -.
DR AGR; Xenbase:XB-GENE-974974; -.
DR CTD; 100049739; -.
DR Xenbase; XB-GENE-974974; rnf5.L.
DR OrthoDB; 276791at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 100049739; Expressed in blastula and 19 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; cd16743; RING-HC_RNF5; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313:SF4; E3 UBIQUITIN-PROTEIN LIGASE RNF5; 1.
DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
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 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 66..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 168 AA; 18460 MW; D508E56DF7A096CD CRC64;
MAAAAGSPVA AYECNICLET AREPVVSVCG HLYCWPCLHQ WLETRPERQE CPVCKAGVSR
EKVIPIYGRG DGNQKDPRLK TPPRPQGQRP EPENRAGGGV PGFTDTGFHM SFGIGAFPFG
FFTTVFNTND LHTAPRADTG LPQSRFFGLP DSLFLIIAAF FFLWLISV
//
