TRI13_RAT
ID TRI13_RAT Reviewed; 407 AA.
AC Q5M7V1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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: 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; CH474023; EDL85281.1; -; Genomic_DNA.
DR EMBL; BC088425; AAH88425.1; -; mRNA.
DR RefSeq; NP_001012210.1; NM_001012210.1.
DR RefSeq; XP_006252199.1; XM_006252137.3.
DR RefSeq; XP_017455253.1; XM_017599764.1.
DR AlphaFoldDB; Q5M7V1; -.
DR SMR; Q5M7V1; -.
DR BioGRID; 264747; 1.
DR STRING; 10116.ENSRNOP00000012035; -.
DR PaxDb; Q5M7V1; -.
DR Ensembl; ENSRNOT00000107093; ENSRNOP00000096302; ENSRNOG00000009075.
DR Ensembl; ENSRNOT00000109510; ENSRNOP00000092048; ENSRNOG00000009075.
DR Ensembl; ENSRNOT00000112782; ENSRNOP00000078168; ENSRNOG00000009075.
DR Ensembl; ENSRNOT00000116555; ENSRNOP00000086916; ENSRNOG00000009075.
DR GeneID; 364398; -.
DR KEGG; rno:364398; -.
DR UCSC; RGD:1307609; rat.
DR CTD; 10206; -.
DR RGD; 1307609; Trim13.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159715; -.
DR HOGENOM; CLU_053708_0_0_1; -.
DR InParanoid; Q5M7V1; -.
DR OMA; NLQVNYS; -.
DR OrthoDB; 635534at2759; -.
DR PhylomeDB; Q5M7V1; -.
DR TreeFam; TF331669; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5M7V1; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000009075; Expressed in lung and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
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_0000416764"
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"
SQ SEQUENCE 407 AA; 46815 MW; 274CC44640290DCE CRC64;
MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGLLEG NVRNSLWRPS PFKCPTCRKE
TSATGVNSLQ VNYSLKGIVE KYNKIKISPK MPVCKEHLGQ PLNIFCVTDM QLICGVCATR
GSHTKHVFSS IEDAYTQERD AFEFLFQSFE TWRRGDALSR LDTLETNKRK SLQLLTKDSD
KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQTYDPEIN KLNSILQEQR MAFNIAEAFK
DVSEPIIFLQ QMQEFREKIK VIKETPLPPS NLPTSPLMKN FDTSQWEDIK LVDVDKLSLP
QDTGVLTSRS PWHPCLLLMA VVLLGLLVFF GPTVFLEWSP LEELATWKDC LSSFNSYLTK
SADFVEQSVF YWEQMTDGLF VFSERVKNVS LVALNNVAEF VCKYKLL
