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TRI13_BOVIN
ID   TRI13_BOVIN             Reviewed;         407 AA.
AC   Q32L60; F1MGY4;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM13;
DE            EC=2.3.2.27;
DE   AltName: Full=Putative tumor suppressor RFP2;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM13 {ECO:0000305};
DE   AltName: Full=Ret finger protein 2;
DE   AltName: Full=Tripartite motif-containing protein 13;
GN   Name=TRIM13; Synonyms=RFP2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase
CC       involved in the retrotranslocation and turnover of membrane and
CC       secretory proteins from the ER through a set of processes named ER-
CC       associated degradation (ERAD). This process acts on misfolded proteins
CC       as well as in the regulated degradation of correctly folded proteins.
CC       Enhances ionizing radiation-induced p53/TP53 stability and apoptosis
CC       via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity
CC       through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-
CC       induced autophagy, and may act as a tumor suppressor. Also plays a role
CC       in innate immune response by stimulating NF-kappa-B activity in the
CC       TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked
CC       polyubiquitination chain resulting in NF-kappa-B activation.
CC       Participates as well in T-cell receptor-mediated NF-kappa-B activation.
CC       In the presence of TNF, modulates the IKK complex by regulating
CC       IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.
CC       {ECO:0000250|UniProtKB:O60858}.
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:O60858};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:O60858}.
CC   -!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts with
CC       AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal
CC       degradation. Interacts with MDM2; the interaction ubiquitinates AKT1
CC       and leads to its proteasomal degradation. Interacts with p62/SQSTM1.
CC       Interacts with TRAF6. Interacts with IKBKG/NEMO.
CC       {ECO:0000250|UniProtKB:O60858}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O60858}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:O60858}. Note=Concentrates and colocalizes with
CC       p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:O60858}.
CC   -!- DOMAIN: The coiled-coil domain is required for the induction of
CC       autophagy during endoplasmic reticulum (ER) stress.
CC       {ECO:0000250|UniProtKB:O60858}.
CC   -!- DOMAIN: The RING-type zinc finger is required for auto-
CC       polyubiquitination. {ECO:0000250|UniProtKB:O60858}.
CC   -!- DOMAIN: The C-terminal transmembrane domain is indispensable for the
CC       localization to the ER. {ECO:0000250|UniProtKB:O60858}.
CC   -!- PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-
CC       polyubiquitination leads to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:O60858}.
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DR   EMBL; DAAA02032918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC109749; AAI09750.1; -; mRNA.
DR   RefSeq; NP_001033254.1; NM_001038165.2.
DR   RefSeq; XP_005213714.1; XM_005213657.1.
DR   RefSeq; XP_005213715.1; XM_005213658.3.
DR   AlphaFoldDB; Q32L60; -.
DR   SMR; Q32L60; -.
DR   STRING; 9913.ENSBTAP00000010745; -.
DR   PaxDb; Q32L60; -.
DR   PRIDE; Q32L60; -.
DR   Ensembl; ENSBTAT00000010745; ENSBTAP00000010745; ENSBTAG00000008173.
DR   GeneID; 535190; -.
DR   KEGG; bta:535190; -.
DR   CTD; 10206; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008173; -.
DR   VGNC; VGNC:36314; TRIM13.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000159715; -.
DR   HOGENOM; CLU_053708_0_0_1; -.
DR   InParanoid; Q32L60; -.
DR   OMA; NLQVNYS; -.
DR   OrthoDB; 635534at2759; -.
DR   TreeFam; TF331669; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000008173; Expressed in spermatid and 105 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR   GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IBA:GO_Central.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR027370; Znf-RING_LisH.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW   Metal-binding; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..407
FT                   /note="E3 ubiquitin-protein ligase TRIM13"
FT                   /id="PRO_0000416763"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         10..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         89..131
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          172..200
FT                   /evidence="ECO:0000255"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   CONFLICT        55
FT                   /note="P -> H (in Ref. 2; AAI09750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  47078 MW;  F56BB27F25EB7C9C CRC64;
     MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG NVRNSLWRSS PFKCPTCRKE
     TSATGVNSLQ VNYSLKGIVE KYNKIKVSPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR
     GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD
     KVKEFFEKLQ YTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK
     DVSEPIIFLQ QMQEFREKIK VIKETPLPPS NLPSSPLMKN FDTSQWEDIK LVDVDKLSLP
     QDTGTFISKI PWRLYPLFVV VILLGLLIFF SPTMFLEWSL FDEIATWKDN LSNFSSYLTR
     SADFVEQSVF YWEQLTDGLF IFSERLKSFT LVVLNNVAEF VCKYKLL
 
 
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