RNF5_MOUSE
ID RNF5_MOUSE Reviewed; 180 AA.
AC O35445;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
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:0000303|PubMed:12861019};
GN Name=Rnf5 {ECO:0000303|PubMed:12861019, ECO:0000312|MGI:MGI:1860076};
GN Synonyms=Ng2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12861019; DOI=10.1128/mcb.23.15.5331-5345.2003;
RA Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K.,
RA Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.;
RT "RNF5, a RING finger protein that regulates cell motility by targeting
RT paxillin ubiquitination and altered localization.";
RL Mol. Cell. Biol. 23:5331-5345(2003).
RN [4]
RP INTERACTION WITH JKAMP.
RX PubMed=16166642; DOI=10.1128/mcb.25.19.8619-8630.2005;
RA Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C., Broday L.,
RA Asahara T., Bhoumik A., Ronai Z.;
RT "JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
RT regulates duration of JNK activity.";
RL Mol. Cell. Biol. 25:8619-8630(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=23093945; DOI=10.1371/journal.pgen.1003007;
RA Kuang E., Okumura C.Y., Sheffy-Levin S., Varsano T., Shu V.C., Qi J.,
RA Niesman I.R., Yang H.J., Lopez-Otin C., Yang W.Y., Reed J.C., Broday L.,
RA Nizet V., Ronai Z.A.;
RT "Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and
RT influences susceptibility to bacterial infection.";
RL PLoS Genet. 8:e1003007-e1003007(2012).
CC -!- FUNCTION: Membrane-bound E3 ubiquitin-protein ligase that mediates
CC ubiquitination of target proteins (PubMed:23093945). May function
CC together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and
CC UBE2D2/UBC4 (By similarity). Mediates ubiquitination of
CC PXN/paxillin,thereby regulating cell motility and localization of
CC PXN/paxillin (By similarity). 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 (By similarity). Mediates the 'Lys-48'-linked polyubiquitination
CC of STING1 at 'Lys-150' leading to its proteasomal degradation; the
CC ubiquitination occurs in mitochondria after viral transfection and
CC regulates antiviral responses (By similarity). Catalyzes ubiquitination
CC and subsequent degradation of ATG4B, thereby inhibiting autophagy
CC (PubMed:23093945). {ECO:0000250|UniProtKB:Q99942,
CC ECO:0000269|PubMed:23093945}.
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:0000269|PubMed:23093945}.
CC -!- SUBUNIT: Interacts with PXN (By similarity). Interacts with JKAMP
CC (PubMed:16166642). Interacts with STING1; the interaction of endogenous
CC proteins is dependent on viral infection (By similarity).
CC {ECO:0000250|UniProtKB:Q99942, ECO:0000269|PubMed:16166642}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12861019};
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 -!- DISRUPTION PHENOTYPE: Mice are more resistant to lethal infections by
CC group A Streptococcus due to increased autophagy (PubMed:23093945).
CC Macrophages show increased autophagosomes and more efficient bacterial
CC clearance (PubMed:23093945). {ECO:0000269|PubMed:23093945}.
CC -!- SIMILARITY: Belongs to the RNF5 family. {ECO:0000305}.
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DR EMBL; AF030001; AAB82008.1; -; Genomic_DNA.
DR EMBL; BC016449; AAH16449.1; -; mRNA.
DR CCDS; CCDS28650.1; -.
DR PIR; T09063; T09063.
DR RefSeq; NP_062276.1; NM_019403.3.
DR AlphaFoldDB; O35445; -.
DR SMR; O35445; -.
DR BioGRID; 207597; 1.
DR MINT; O35445; -.
DR STRING; 10090.ENSMUSP00000015622; -.
DR iPTMnet; O35445; -.
DR PhosphoSitePlus; O35445; -.
DR EPD; O35445; -.
DR MaxQB; O35445; -.
DR PaxDb; O35445; -.
DR PeptideAtlas; O35445; -.
DR PRIDE; O35445; -.
DR ProteomicsDB; 301627; -.
DR Antibodypedia; 28471; 239 antibodies from 29 providers.
DR DNASU; 54197; -.
DR Ensembl; ENSMUST00000015622; ENSMUSP00000015622; ENSMUSG00000015478.
DR GeneID; 54197; -.
DR KEGG; mmu:54197; -.
DR UCSC; uc008ccy.1; mouse.
DR CTD; 6048; -.
DR MGI; MGI:1860076; Rnf5.
DR VEuPathDB; HostDB:ENSMUSG00000015478; -.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_1_1; -.
DR InParanoid; O35445; -.
DR OMA; PFGYITT; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; O35445; -.
DR TreeFam; TF317334; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 54197; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rnf5; mouse.
DR PRO; PR:O35445; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35445; protein.
DR Bgee; ENSMUSG00000015478; Expressed in embryonic brain and 140 other tissues.
DR Genevisible; O35445; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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; IDA:MGI.
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:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; ISO:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; IDA:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
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 1: Evidence at protein 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_0000240394"
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
