ID TRI31_MOUSE Reviewed; 507 AA.
AC Q8R0K2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM31 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:27992402};
DE AltName: Full=Tripartite motif-containing protein 31 {ECO:0000303|PubMed:19665990};
GN Name=Trim31 {ECO:0000303|PubMed:19665990, ECO:0000312|MGI:MGI:2385051};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 STRAIN=FVB/N; TISSUE=Colon;
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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SHC1.
RX PubMed=19665990; DOI=10.1016/j.bbrc.2009.08.028;
RA Watanabe M., Tsukiyama T., Hatakeyama S.;
RT "TRIM31 interacts with p52(Shc) and inhibits Src-induced anchorage-
RT independent growth.";
RL Biochem. Biophys. Res. Commun. 388:422-427(2009).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27929086; DOI=10.1038/ncomms13727;
RA Song H., Liu B., Huai W., Yu Z., Wang W., Zhao J., Han L., Jiang G.,
RA Zhang L., Gao C., Zhao W.;
RT "The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by
RT promoting proteasomal degradation of NLRP3.";
RL Nat. Commun. 7:13727-13727(2016).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 52-CYS--CYS-55.
RX PubMed=27992402; DOI=10.1038/ni.3641;
RA Liu B., Zhang M., Chu H., Zhang H., Wu H., Song G., Wang P., Zhao K.,
RA Hou J., Wang X., Zhang L., Gao C.;
RT "The ubiquitin E3 ligase TRIM31 promotes aggregation and activation of the
RT signaling adaptor MAVS through Lys63-linked polyubiquitination.";
RL Nat. Immunol. 18:214-224(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of
CC antiviral immune response and inflammation by mediating ubiquitination
CC of substrates (PubMed:27929086, PubMed:27992402). Acts as a regulator
CC of innate immune defense against viruses by mediating 'Lys-63'-linked
CC ubiquitination of MAVS, promoting MAVS polymerization and formation of
CC three-stranded helical filaments on mitochondria (PubMed:27992402).
CC Acts as a negative regulator of the NLRP3 inflammasome by catalyzing
CC 'Lys-48'-linked ubiquitination of NLRP3, leading to its degradation
CC (PubMed:27929086). Regulator of Src-induced anchorage independent cell
CC growth (PubMed:19665990). {ECO:0000269|PubMed:19665990,
CC ECO:0000269|PubMed:27929086, ECO:0000269|PubMed:27992402}.
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:27992402};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:27992402}.
CC -!- SUBUNIT: May form oligomers (By similarity). Interacts with isoform
CC p52shc of SHC1 (PubMed:19665990). {ECO:0000250|UniProtKB:Q9BZY9,
CC ECO:0000269|PubMed:19665990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZY9}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9BZY9}. Note=Predominantly
CC expressed in the cytoplasm but a fraction is associated with the
CC mitochondria. {ECO:0000250|UniProtKB:Q9BZY9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the gastrointestrinal tract,
CC with high expression in the small intestine, moderate in the large
CC intestine and weak in the stomach and esophagus.
CC {ECO:0000269|PubMed:19665990}.
CC -!- INDUCTION: Up-regulated in response to lipopolysaccharid and IL1B
CC treatment. {ECO:0000269|PubMed:27929086}.
CC -!- PTM: Auto-ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q9BZY9}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, normal in size and without gross
CC physiological or behavioral abnormalities (PubMed:27992402). Mice are
CC however more susceptible to infection with RNA virus due to impaired
CC cellular antiviral response (PubMed:27992402). Mice also show increased
CC inflammatory response, characterized by enhanced NLRP3 inflammasome
CC activation (PubMed:27929086). Increased NLRP3 inflammasome activation
CC leads to an aggravation of alum-induced peritonitis (PubMed:27929086).
CC In contrast, it attenuates the severity of dextran sodium sulfate-
CC induced colitis, an inflammatory bowel diseases model in which NLRP3
CC possesses protective roles (PubMed:27929086).
CC {ECO:0000269|PubMed:27929086, ECO:0000269|PubMed:27992402}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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; AK033650; BAC28407.1; -; mRNA.
DR EMBL; CH466559; EDL23309.1; -; Genomic_DNA.
DR EMBL; BC026666; AAH26666.1; -; mRNA.
DR CCDS; CCDS28728.1; -.
DR RefSeq; NP_666189.1; NM_146077.2.
DR AlphaFoldDB; Q8R0K2; -.
DR SMR; Q8R0K2; -.
DR BioGRID; 230316; 4.
DR STRING; 10090.ENSMUSP00000077535; -.
DR GlyGen; Q8R0K2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8R0K2; -.
DR PhosphoSitePlus; Q8R0K2; -.
DR MaxQB; Q8R0K2; -.
DR PaxDb; 10090-ENSMUSP00000077535; -.
DR PeptideAtlas; Q8R0K2; -.
DR ProteomicsDB; 259316; -.
DR Antibodypedia; 11702; 219 antibodies from 27 providers.
DR DNASU; 224762; -.
DR Ensembl; ENSMUST00000078438.5; ENSMUSP00000077535.5; ENSMUSG00000058063.5.
DR GeneID; 224762; -.
DR KEGG; mmu:224762; -.
DR UCSC; uc008cll.1; mouse.
DR AGR; MGI:2385051; -.
DR CTD; 11074; -.
DR MGI; MGI:2385051; Trim31.
DR VEuPathDB; HostDB:ENSMUSG00000058063; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163585; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q8R0K2; -.
DR OMA; FWALRIA; -.
DR OrthoDB; 3453019at2759; -.
DR PhylomeDB; Q8R0K2; -.
DR TreeFam; TF342569; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 224762; 2 hits in 77 CRISPR screens.
DR PRO; PR:Q8R0K2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R0K2; Protein.
DR Bgee; ENSMUSG00000058063; Expressed in small intestine Peyer's patch and 28 other cell types or tissues.
DR Genevisible; Q8R0K2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR CDD; cd16582; RING-HC_TRIM31_C-V; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
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 PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF87; E3 UBIQUITIN-PROTEIN LIGASE TRIM31; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Coiled coil; Cytoplasm; Immunity; Inflammatory response;
KW Innate immunity; Metal-binding; Mitochondrion; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..507
FT /note="E3 ubiquitin-protein ligase TRIM31"
FT /id="PRO_0000386639"
FT DOMAIN 315..507
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 89..130
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 176..241
FT /evidence="ECO:0000255"
FT COILED 269..298
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 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 52..55
FT /note="CPLC->APLA: Abolished E3 ubiquitin-protein ligase
FT activity and ability to ubiquitinate MAVS."
FT /evidence="ECO:0000269|PubMed:27992402"
SQ SEQUENCE 507 AA; 57127 MW; 086106A2E1BC31FF CRC64;
MAGQPLACQL QEEVTCPICM EILQDPVTID CGHNFCLQCI SQVGKTSEKI QCPLCKLSVN
KNTFRPNKLL ASLAEKIQSM DPADIQAEKE DSRCQRHKEK LHYFCEQDGA FLCVVCRDSK
DHKSHNVTLI DEAAQNYKVQ IESQAQDLGQ KDKKIIEEKK QGEGAIWAFR AQVDLEKLKI
HEEFKLLRQR LDEEESFLLS RLDWLEQQGA KQLRQYVTVT EKQLNSLRKL TKSLKIRLQS
SSMELLKDIK DALSRGKEFQ FLNPNPVPED LEKKCSEAKA RHESIIKTLT ELKDDMNAEG
KRDKSAFMNS LNKEEKESWS LLQKNNSVLP TSVPVTLDKS SADPDLTFSQ DLKKVTLYIV
AGKASNRQAK PRPFYPFHCV RGSPGLSSGR QVWEAEIRGP SGGACIVGVV TELARGAQSQ
TVSAQSYIWA LRISPSGCQP FTNCKAQEYL QVCLKKVGVY VNHDCGEVVF YDAITSKHIY
TFQTSFDGKV FPLFGLQVAC SHITLSP
//
