RNF34_RAT
ID RNF34_RAT Reviewed; 381 AA.
AC Q6AYH3; Q8CIP0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:12859687};
DE AltName: Full=RING finger protein 34 {ECO:0000312|RGD:628636};
DE AltName: Full=RING finger protein MOMO {ECO:0000303|PubMed:12859687};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000305};
GN Name=Rnf34 {ECO:0000312|RGD:628636};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AUTOUBIQUITINATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=12859687; DOI=10.1046/j.1471-4159.2003.01875.x;
RA Araki K., Kawamura M., Suzuki T., Matsuda N., Kanbe D., Ishii K.,
RA Ichikawa T., Kumanishi T., Chiba T., Tanaka K., Nawa H.;
RT "A palmitoylated RING finger ubiquitin ligase and its homologue in the
RT brain membranes.";
RL J. Neurochem. 86:749-762(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: E3 ubiquitin-protein ligase that regulates several biological
CC processes through the ubiquitin-mediated proteasomal degradation of
CC various target proteins. Ubiquitinates the caspases CASP8 and CASP10,
CC promoting their proteasomal degradation, to negatively regulate cell
CC death downstream of death domain receptors in the extrinsic pathway of
CC apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and
CC its subsequent proteasomal degradation thereby indirectly regulating
CC the tumor necrosis factor-mediated signaling pathway. Negatively
CC regulates p53/TP53 through its direct ubiquitination and targeting to
CC proteasomal degradation. Indirectly, may also negatively regulate
CC p53/TP53 through ubiquitination and degradation of SFN. Mediates
CC PPARGC1A proteasomal degradation probably through ubiquitination
CC thereby indirectly regulating the metabolism of brown fat cells.
CC Possibly involved in innate immunity, through 'Lys-48'-linked
CC polyubiquitination of NOD1 and its subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q969K3, ECO:0000269|PubMed:12859687}.
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:0000269|PubMed:12859687};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBUNIT: Interacts with CASP8 and CASP10. Interacts with p53/TP53;
CC involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc
CC finger) with MDM2; the interaction stabilizes MDM2. Interacts (via
CC RING-type zinc finger) with PPARGC1A. Interacts with NOD1.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969K3};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q969K3}.
CC Endomembrane system {ECO:0000269|PubMed:12859687}; Peripheral membrane
CC protein {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q969K3}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q969K3}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, cerebellum,
CC midbrain, hippocampus, striatum, heart, lung, kidney, muscle, spleen
CC and testis. {ECO:0000269|PubMed:12859687}.
CC -!- DOMAIN: The RING-type zinc finger is required for the ubiquitination of
CC target proteins. {ECO:0000250|UniProtKB:Q969K3}.
CC -!- DOMAIN: The FYVE-type zinc finger domain is required for localization
CC and may confer affinity for cellular compartments enriched in
CC phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate
CC phospholipids. {ECO:0000250|UniProtKB:Q969K3}.
CC -!- PTM: Proteolytically cleaved by caspases upon induction of apoptosis by
CC TNF. {ECO:0000250|UniProtKB:Q969K3}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000269|PubMed:12859687}.
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DR EMBL; AY157968; AAN60073.1; -; mRNA.
DR EMBL; BC079044; AAH79044.1; -; mRNA.
DR RefSeq; NP_001004075.1; NM_001004075.1.
DR AlphaFoldDB; Q6AYH3; -.
DR SMR; Q6AYH3; -.
DR STRING; 10116.ENSRNOP00000001799; -.
DR jPOST; Q6AYH3; -.
DR PaxDb; Q6AYH3; -.
DR Ensembl; ENSRNOT00000001799; ENSRNOP00000001799; ENSRNOG00000001331.
DR GeneID; 282845; -.
DR KEGG; rno:282845; -.
DR UCSC; RGD:628636; rat.
DR CTD; 80196; -.
DR RGD; 628636; Rnf34.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00390000012719; -.
DR HOGENOM; CLU_041431_1_0_1; -.
DR InParanoid; Q6AYH3; -.
DR OMA; NEANHRT; -.
DR OrthoDB; 1361306at2759; -.
DR PhylomeDB; Q6AYH3; -.
DR TreeFam; TF325195; -.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6AYH3; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001331; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q6AYH3; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:CACAO.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000374; P:regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..381
FT /note="E3 ubiquitin-protein ligase RNF34"
FT /id="PRO_0000056075"
FT DOMAIN 115..134
FT /note="SAP 1"
FT DOMAIN 273..287
FT /note="SAP 2"
FT ZN_FING 56..107
FT /note="FYVE-type"
FT ZN_FING 334..369
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 216..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 241..242
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR6"
FT CONFLICT 253
FT /note="P -> L (in Ref. 1; AAN60073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42681 MW; 12A2E7BEB1CEA4EA CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQA GFPGSTGPFR FTPSSDFPTY PPAATEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSLCS VSQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLLLR NVPTDTCREK EDLVDLVLCH RGLGSGDGLD SRSLSSSRSQ TSSFFTQSYF
SNYTPPSATV SSFQGELMDR EGTFRSEVLT QVQSELASAN TDDEDGEEDD DDDDDDDDED
DDEQEENLEE QNPGLSKKKA RASLSDLSSL EEVEGMSVRQ LKEILARNFV NYSGCCEKWE
LVEKVNRLYK ENEENQKSYG ERMQLQDEED DSLCRICMDA VIDCVLLECG HMVTCTKCGK
RMSECPICRQ YVVRAVHVFK S
