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RN114_RAT
ID   RN114_RAT               Reviewed;         229 AA.
AC   Q6J2U6; Q4G096;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF114;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9Y508};
DE   AltName: Full=RING finger protein 114;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF114 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 313;
GN   Name=Rnf114; Synonyms=Zfp313, Znf313;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RA   Ma Y.-X., Wu Q., Zhang S., Li N., Sun Y., Peng Y., He G., Liu Y., Dong J.;
RT   "Molecular cloning and characterization of rat Znf313 gene.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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 promotes the ubiquitination
CC       of various substrates. In turn, participates in the regulation of many
CC       biological processes including cell cycle, apoptosis,
CC       osteoclastogenesis as well as innate or adaptive immunity. Acts as
CC       negative regulator of NF-kappa-B-dependent transcription by promoting
CC       the ubiquitination and stabilization of the NF-kappa-B inhibitor
CC       TNFAIP3. May promote the ubiquitination of TRAF6 as well. Acts also as
CC       a negative regulator of T-cell activation. Inhibits cellular dsRNA
CC       responses and interferon production by targeting MAVS component for
CC       proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading
CC       to its degradationand probably also CDKN1B and CDKN1C. This activity
CC       stimulates cell cycle G1-to-S phase transition and suppresses cellular
CC       senescence. May play a role in spermatogenesis.
CC       {ECO:0000250|UniProtKB:Q9Y508}.
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:Q9Y508};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9Y508}.
CC   -!- SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability
CC       and proapoptotic effects, and may regulate IFN signaling.
CC       {ECO:0000250|UniProtKB:Q9Y508}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y508}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y508}.
CC   -!- PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes
CC       UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence
CC       of UBE2E1. {ECO:0000250|UniProtKB:Q9Y508}.
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DR   EMBL; AY603473; AAT28739.1; -; mRNA.
DR   EMBL; BC098633; AAH98633.1; -; mRNA.
DR   RefSeq; NP_001001517.1; NM_001001517.1.
DR   AlphaFoldDB; Q6J2U6; -.
DR   STRING; 10116.ENSRNOP00000012675; -.
DR   iPTMnet; Q6J2U6; -.
DR   PhosphoSitePlus; Q6J2U6; -.
DR   jPOST; Q6J2U6; -.
DR   PaxDb; Q6J2U6; -.
DR   PRIDE; Q6J2U6; -.
DR   GeneID; 362277; -.
DR   KEGG; rno:362277; -.
DR   UCSC; RGD:1303139; rat.
DR   CTD; 55905; -.
DR   RGD; 1303139; Rnf114.
DR   VEuPathDB; HostDB:ENSRNOG00000060821; -.
DR   eggNOG; ENOG502QW3F; Eukaryota.
DR   HOGENOM; CLU_092448_1_0_1; -.
DR   InParanoid; Q6J2U6; -.
DR   OMA; DYIEEGV; -.
DR   OrthoDB; 1097558at2759; -.
DR   PhylomeDB; Q6J2U6; -.
DR   TreeFam; TF331012; -.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6J2U6; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000060821; Expressed in heart and 19 other tissues.
DR   Genevisible; Q6J2U6; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd16540; RING-HC_RNF114; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR042716; RNF114_RING-HC.
DR   InterPro; IPR034734; ZF_C2HC_RNF.
DR   InterPro; IPR027370; Znf-RING_LisH.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF05605; zf-Di19; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   Pfam; PF18574; zf_C2HC_14; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW   Metal-binding; Nucleus; Reference proteome; Spermatogenesis; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..229
FT                   /note="E3 ubiquitin-protein ligase RNF114"
FT                   /id="PRO_0000056311"
FT   ZN_FING         30..69
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         92..111
FT                   /note="C2HC RNF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT   MOD_RES         103
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT   MOD_RES         113
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y508"
SQ   SEQUENCE   229 AA;  25664 MW;  72DB48DF7FE1B900 CRC64;
     MAAAQPESRD GAAQSAKPAS ETDPLSRFTC PVCLEVFEKP VQVPCGHVFC SACLQECLKP
     KKPVCGVCRS ALAPGVRAAE LERQIESIET SCHGCRKDFV LSKIRAHVAS CSKYQSYIME
     GVKATTKDAS LQQRNVPNRY TFPCPYCPEK NFDQEGLVEH CKLTHSTDTK SVVCPICASM
     PWGDPSYRSA NFMEHIQRRH RFSYDTFVDY DVDEDDMINQ VLQRSIIDQ
 
 
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