LOCUS       NP_001004075             381 aa            linear   ROD 02-JUN-2024
DEFINITION  E3 ubiquitin-protein ligase RNF34 [Rattus norvegicus].
ACCESSION   NP_001004075 XP_341083
VERSION     NP_001004075.1
DBSOURCE    REFSEQ: accession NM_001004075.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Yamaoka,S., Oshima,Y., Horiuchi,H., Morino,T., Hino,M., Miura,H.
            and Ogata,T.
  TITLE     Altered Gene Expression of RNF34 and PACAP Possibly Involved in
            Mechanism of Exercise-Induced Analgesia for Neuropathic Pain in
            Rats
  JOURNAL   Int J Mol Sci 18 (9), 1962 (2017)
   PUBMED   28902127
  REMARK    GeneRIF: Results suggest that exercise therapy possibly involves
            pain relief in SNL rats by suppressing Rnf34 and Pacap expression
            in the spinal cord.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Jin,H., Chiou,T.T., Serwanski,D.R., Miralles,C.P., Pinal,N. and De
            Blas,A.L.
  TITLE     Ring finger protein 34 (RNF34) interacts with and promotes
            gamma-aminobutyric acid type-A receptor degradation via
            ubiquitination of the gamma2 subunit
  JOURNAL   J Biol Chem 289 (42), 29420-29436 (2014)
   PUBMED   25193658
  REMARK    GeneRIF: RNF34 regulates postsynaptic gamma2-GABAAR clustering and
            GABAergic synaptic innervation by interacting with and
            ubiquitinating the gamma2-GABAAR subunit promoting GABAAR
            degradation
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Zhang,R., Zhao,J., Song,Y., Wang,X., Wang,L., Xu,J., Song,C. and
            Liu,F.
  TITLE     The E3 ligase RNF34 is a novel negative regulator of the NOD1
            pathway
  JOURNAL   Cell Physiol Biochem 33 (6), 1954-1962 (2014)
   PUBMED   25012219
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Wei,P., Pan,D., Mao,C. and Wang,Y.X.
  TITLE     RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and
            modulates brown fat cell metabolism
  JOURNAL   Mol Cell Biol 32 (2), 266-275 (2012)
   PUBMED   22064484
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Yang,W., Dicker,D.T., Chen,J. and El-Deiry,W.S.
  TITLE     CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
            MDM2
  JOURNAL   Cell Cycle 7 (5), 670-682 (2008)
   PUBMED   18382127
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Yang,W., Rozan,L.M., McDonald,E.R. 3rd, Navaraj,A., Liu,J.J.,
            Matthew,E.M., Wang,W., Dicker,D.T. and El-Deiry,W.S.
  TITLE     CARPs are ubiquitin ligases that promote MDM2-independent p53 and
            phospho-p53ser20 degradation
  JOURNAL   J Biol Chem 282 (5), 3273-3281 (2007)
   PUBMED   17121812
REFERENCE   7  (residues 1 to 381)
  AUTHORS   McDonald,E.R. 3rd and El-Deiry,W.S.
  TITLE     Suppression of caspase-8- and -10-associated RING proteins results
            in sensitization to death ligands and inhibition of tumor cell
            growth
  JOURNAL   Proc Natl Acad Sci U S A 101 (16), 6170-6175 (2004)
   PUBMED   15069192
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Araki,K., Kawamura,M., Suzuki,T., Matsuda,N., Kanbe,D., Ishii,K.,
            Ichikawa,T., Kumanishi,T., Chiba,T., Tanaka,K. and Nawa,H.
  TITLE     A palmitoylated RING finger ubiquitin ligase and its homologue in
            the brain membranes
  JOURNAL   J Neurochem 86 (3), 749-762 (2003)
   PUBMED   12859687
  REMARK    GeneRIF: identified two novel Ub ligases, Momo and Sakura, carrying
            double zinc finger motif and RING finger domain; momo expression is
            enriched in the brain gray matter and testis
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079044.1.
            
            On Sep 3, 2004 this sequence version replaced XP_341083.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079044.1, SRR8487231.120655.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..381
                     /product="E3 ubiquitin-protein ligase RNF34"
                     /EC_number="2.3.2.27"
                     /note="RING finger protein MOMO; ring finger protein 34,
                     E3 ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase RNF34"
                     /calculated_mol_wt=42550
     Region          59..105
                     /region_name="FYVE_CARP1"
                     /note="FYVE-like domain found in caspase regulator CARP1
                     and similar proteins; cd15769"
                     /db_xref="CDD:277308"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Region          216..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            241..242
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99KR6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Region          328..381
                     /region_name="RING-HC_CARP1"
                     /note="RING finger, HC subclass, found in caspases-8 and
                     -10-associated RING finger protein 1 (CARP1) and similar
                     proteins; cd16706"
                     /db_xref="CDD:438366"
     CDS             1..381
                     /gene="Rnf34"
                     /gene_synonym="Momo"
                     /coded_by="NM_001004075.1:96..1241"
                     /db_xref="GeneID:282845"
                     /db_xref="RGD:628636"
ORIGIN      
        1 mkagatsmwa sccgllnevm gtgavrgqqa gfpgstgpfr ftpssdfpty ppaategpni
       61 vckacglsfs vfrkkhvccd ckkdfcslcs vsqenlrrcs tchllqetaf qrpqlmrlkv
      121 kdlrqylllr nvptdtcrek edlvdlvlch rglgsgdgld srslsssrsq tssfftqsyf
      181 snytppsatv ssfqgelmdr egtfrsevlt qvqselasan tddedgeedd dddddddded
      241 ddeqeenlee qnpglskkka raslsdlssl eevegmsvrq lkeilarnfv nysgccekwe
      301 lvekvnrlyk eneenqksyg ermqlqdeed dslcricmda vidcvllecg hmvtctkcgk
      361 rmsecpicrq yvvravhvfk s
//
