RN114_BOVIN
ID RN114_BOVIN Reviewed; 230 AA.
AC Q4U5R4; A5D9G2; Q3T0F8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=ZNF313;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cao S.Z., Lee H.B., Wang A.H., Zhao X.X., Du L.X.;
RT "Molecular cloning and characterization of bovine zinc finger protein 313
RT (Znf313) gene.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-230.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; DQ010409; AAY33866.1; -; mRNA.
DR EMBL; BC102412; AAI02413.1; -; mRNA.
DR EMBL; BT030581; ABQ13021.1; -; mRNA.
DR RefSeq; NP_001019702.1; NM_001024531.3.
DR RefSeq; XP_005214742.1; XM_005214685.3.
DR RefSeq; XP_005214743.1; XM_005214686.2.
DR AlphaFoldDB; Q4U5R4; -.
DR STRING; 9913.ENSBTAP00000038956; -.
DR PaxDb; Q4U5R4; -.
DR PRIDE; Q4U5R4; -.
DR Ensembl; ENSBTAT00000039156; ENSBTAP00000038956; ENSBTAG00000027317.
DR GeneID; 513479; -.
DR KEGG; bta:513479; -.
DR CTD; 55905; -.
DR VEuPathDB; HostDB:ENSBTAG00000027317; -.
DR VGNC; VGNC:34012; RNF114.
DR eggNOG; ENOG502QW3F; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q4U5R4; -.
DR OMA; DYIEEGV; -.
DR OrthoDB; 1097558at2759; -.
DR TreeFam; TF331012; -.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000027317; Expressed in thyroid gland and 106 other tissues.
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 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..230
FT /note="E3 ubiquitin-protein ligase RNF114"
FT /id="PRO_0000056306"
FT ZN_FING 31..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 93..112
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
SQ SEQUENCE 230 AA; 25669 MW; AFFFD09B02C26138 CRC64;
MAAQAQAPAR DGGAQLAGPA AEADPLGRFT CPVCLEVYEK PVQVPCGHVF CSACLQECLK
PKKPVCGVCR SALAPGVRAV ELERQIESTE TSCHGCRKNF FLSKIRAHVA TCSKYQNYIM
EGVKATTKDA SRQPRSVPNR YTFPCPYCPE KNFDQEGLVE HCKLSHSTDT KSVVCPICAS
MPWGDPNYRS ANFIEHLQRR HQFSYDTFVD YDVDEEDMIN QVLQRSIIDQ
