RN114_PIG
ID RN114_PIG Reviewed; 228 AA.
AC Q6J1I8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=E3 ubiquitin-protein ligase RNF114;
DE EC=2.3.2.27 {ECO:0000269|PubMed:31413123};
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=ZNF313;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Wu Q., Wang C., Ma Y.-X., Zhang S.Z., Bao J., Sun Y., Liu Y., He G.,
RA Dong J.;
RT "Molecular cloning of pig Znf313 gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, MUTAGENESIS OF CYS-64 AND CYS-67, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=31413123; DOI=10.1128/jvi.01248-19;
RA Zhang Y., Zhang H., Zheng G.L., Yang Q., Yu S., Wang J., Li S., Li L.F.,
RA Qiu H.J.;
RT "Porcine RING finger protein 114 inhibits classical swine fever virus
RT replication via the K27-linked polyubiquitination of viral NS4B.";
RL J. Virol. 0:0-0(2019).
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 (By similarity).
CC Inhibits classical swine fever virus replication by mediating 'K27'-
CC linked ubiquitination of viral NS4B and inducing its degradation via
CC the proteasome (PubMed:31413123). {ECO:0000250|UniProtKB:Q9Y508,
CC ECO:0000269|PubMed:31413123}.
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:31413123};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:31413123}.
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:0000269|PubMed:31413123}. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY606064; AAT36620.1; -; mRNA.
DR RefSeq; NP_001001869.1; NM_001001869.1.
DR AlphaFoldDB; Q6J1I8; -.
DR STRING; 9823.ENSSSCP00000027982; -.
DR PaxDb; Q6J1I8; -.
DR PeptideAtlas; Q6J1I8; -.
DR PRIDE; Q6J1I8; -.
DR Ensembl; ENSSSCT00000044278; ENSSSCP00000049061; ENSSSCG00000036129.
DR Ensembl; ENSSSCT00070034635; ENSSSCP00070028932; ENSSSCG00070017549.
DR GeneID; 414917; -.
DR KEGG; ssc:414917; -.
DR CTD; 55905; -.
DR VGNC; VGNC:108733; RNF114.
DR eggNOG; ENOG502QW3F; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_1_1; -.
DR InParanoid; Q6J1I8; -.
DR OMA; DYIEEGV; -.
DR OrthoDB; 1097558at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Proteomes; UP000314985; Chromosome 17.
DR Bgee; ENSSSCG00000036129; Expressed in oocyte and 43 other tissues.
DR Genevisible; Q6J1I8; SS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; 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 PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein 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..228
FT /note="E3 ubiquitin-protein ligase RNF114"
FT /id="PRO_0000056310"
FT ZN_FING 29..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 91..110
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT MUTAGEN 64
FT /note="C->A: Complete loss of viral NS4B ubiquitination; in
FT association with A-67."
FT /evidence="ECO:0000269|PubMed:31413123"
FT MUTAGEN 67
FT /note="C->A: Complete loss of viral NS4B ubiquitination; in
FT association with A-64."
FT /evidence="ECO:0000269|PubMed:31413123"
SQ SEQUENCE 228 AA; 25629 MW; 893F780E3CD4EF14 CRC64;
MAAQPQDREG GAQLAGPAAE ADPLGRFTCP VCLEVYEKPV QVPCGHVFCS ACLQECLKPK
KPVCGVCRST LAPGVRAVEL ERQIESTETS CHGCRKNFFL SKIRAHVATC SKYQNYIMEG
VKATTKDASL QPRNVPNRYT FPCPYCPEKN FDQEGLVEHC KLVHSTDTKS VVCPICASMP
WGDPNYRSAN FIEHIQRRHQ FSYDTFVDYD VDEEDMMNQV LQRSLLDQ
