ID A5A8Y3_PIG Unreviewed; 180 AA.
AC A5A8Y3; A0A4X1V593;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=E3 ubiquitin-protein ligase RNF {ECO:0000256|RuleBase:RU369090};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369090};
DE AltName: Full=RING finger protein {ECO:0000256|RuleBase:RU369090};
GN Name=RNF5 {ECO:0000313|EMBL:CAN13266.1,
GN ECO:0000313|Ensembl:ENSSSCP00000001543.2,
GN ECO:0000313|VGNC:VGNC:92396};
GN ORFNames=SBAB-649D6.9-001 {ECO:0000313|EMBL:CAN13266.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:CAN13266.1};
RN [1] {ECO:0000313|EMBL:CAN13266.1}
RP NUCLEOTIDE SEQUENCE.
RA Sehra H.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000001543.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001543.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HDB79361.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000001543.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000256|RuleBase:RU369090}.
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 ECO:0000256|RuleBase:RU369090};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369090}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000256|RuleBase:RU369090}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU369090}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369090}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU369090}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 ligase
CC activity. {ECO:0000256|RuleBase:RU369090}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL773562; CAN13266.1; -; Genomic_DNA.
DR EMBL; DQIR01223884; HDB79361.1; -; Transcribed_RNA.
DR RefSeq; NP_001116696.1; NM_001123224.1.
DR STRING; 9823.ENSSSCP00000001543; -.
DR PaxDb; 9823-ENSSSCP00000001543; -.
DR Ensembl; ENSSSCT00000001585.6; ENSSSCP00000001543.2; ENSSSCG00000001436.6.
DR Ensembl; ENSSSCT00005072719.1; ENSSSCP00005045491.1; ENSSSCG00005045052.1.
DR GeneID; 100144528; -.
DR KEGG; ssc:100144528; -.
DR CTD; 6048; -.
DR VGNC; VGNC:92396; RNF5.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_1_1; -.
DR OMA; PFGYITT; -.
DR OrthoDB; 276791at2759; -.
DR TreeFam; TF317334; -.
DR Reactome; R-SSC-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000001436; Expressed in longissimus lumborum muscle and 44 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 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; PF13920; zf-C3HC4_3; 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 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU369090};
KW Membrane {ECO:0000256|RuleBase:RU369090};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369090};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW Transmembrane {ECO:0000256|RuleBase:RU369090};
KW Transmembrane helix {ECO:0000256|RuleBase:RU369090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369090};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369090"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369090"
FT DOMAIN 27..68
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 180 AA; 19911 MW; F4AFA4CF6DE85942 CRC64;
MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC LHQWLETRPE
RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG QRPAPESRGG FQPFGDTGGF
HFSFGVGAFP FGFFTTVFNT HEPFRRGTGV DLGQGHPASS WQDSLFLFLA IFFFFWLLSI
//