RNF5_RAT
ID RNF5_RAT Reviewed; 180 AA.
AC Q5M807;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=E3 ubiquitin-protein ligase RNF5 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q99942};
DE AltName: Full=RING finger protein 5 {ECO:0000250|UniProtKB:Q99942};
GN Name=Rnf5 {ECO:0000312|RGD:1588458};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Membrane-bound E3 ubiquitin-protein ligase that mediates
CC ubiquitination of target proteins. May function together with E2
CC ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates
CC ubiquitination of PXN/paxillin,thereby regulating cell motility and
CC localization of PXN/paxillin. Catalyzes ubiquitination of Salmonella
CC type III secreted protein sopA. Mediates the 'Lys-63'-linked
CC polyubiquitination of JKAMP thereby regulating JKAMP function by
CC decreasing its association with components of the proteasome and ERAD;
CC the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme
CC UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of STING1 at
CC 'Lys-150' leading to its proteasomal degradation; the ubiquitination
CC occurs in mitochondria after viral transfection and regulates antiviral
CC responses. Catalyzes ubiquitination and subsequent degradation of
CC ATG4B, thereby inhibiting autophagy. {ECO:0000250|UniProtKB:Q99942}.
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:0000250|UniProtKB:Q99942};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q99942}.
CC -!- SUBUNIT: Interacts with PXN. Interacts with JKAMP. Interacts with
CC STING1; the interaction of endogenous proteins is dependent on viral
CC infection. {ECO:0000250|UniProtKB:Q99942}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99942};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q99942}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99942}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Predominantly located in the plasma membrane, with
CC some localization occurring within cytoplasmic organelles.
CC {ECO:0000250|UniProtKB:Q99942}.
CC -!- SIMILARITY: Belongs to the RNF5 family. {ECO:0000305}.
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DR EMBL; BC088341; AAH88341.1; -; mRNA.
DR RefSeq; NP_001102495.1; NM_001109025.2.
DR AlphaFoldDB; Q5M807; -.
DR SMR; Q5M807; -.
DR STRING; 10116.ENSRNOP00000000501; -.
DR PaxDb; Q5M807; -.
DR GeneID; 407784; -.
DR KEGG; rno:407784; -.
DR UCSC; RGD:1588458; rat.
DR CTD; 6048; -.
DR RGD; 1588458; Rnf5.
DR VEuPathDB; HostDB:ENSRNOG00000000438; -.
DR eggNOG; KOG0823; Eukaryota.
DR HOGENOM; CLU_055198_2_1_1; -.
DR InParanoid; Q5M807; -.
DR OMA; PFGYITT; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q5M807; -.
DR TreeFam; TF317334; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5M807; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000438; Expressed in kidney and 20 other tissues.
DR ExpressionAtlas; Q5M807; baseline and differential.
DR Genevisible; Q5M807; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
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:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:RGD.
DR GO; GO:0036503; P:ERAD pathway; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 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; PTHR12313; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Endoplasmic reticulum; Membrane; Metal-binding;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99942"
FT CHAIN 2..180
FT /note="E3 ubiquitin-protein ligase RNF5"
FT /id="PRO_0000240395"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 27..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99942"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99942"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99942"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99942"
SQ SEQUENCE 180 AA; 19837 MW; 3C00A30201F590CB CRC64;
MAAAEEEDGG PEGPNRERGG ASATFECNIC LETAREAVVS VCGHLYCWPC LHQWLETRPD
RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG QRPAPESRGG FQPFGDAGGF
HFSFGVGAFP FGFFTTVFNA HEPFRRGAGV DLGQGHPASS WQDSLFLFLA IFFFFWLLSI
