TRI31_MOUSE
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 03-AUG-2022, entry version 154.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM31;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM31 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 31;
GN Name=Trim31;
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).
CC -!- FUNCTION: May have E3 ubiquitin-protein ligase activity (By
CC similarity). Regulator of Src-induced anchorage independent cell
CC growth. {ECO:0000250, ECO:0000269|PubMed:19665990}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with isoform p52shc of
CC SHC1. {ECO:0000250, ECO:0000269|PubMed:19665990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Predomintanly expressed in the cytoplasm but a
CC fraction is associated with the mitochondria. {ECO:0000250}.
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 -!- PTM: Auto-ubiquitinated (in vitro). {ECO:0000250}.
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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 iPTMnet; Q8R0K2; -.
DR PhosphoSitePlus; Q8R0K2; -.
DR MaxQB; Q8R0K2; -.
DR PaxDb; Q8R0K2; -.
DR PeptideAtlas; Q8R0K2; -.
DR PRIDE; Q8R0K2; -.
DR ProteomicsDB; 259316; -.
DR Antibodypedia; 11702; 199 antibodies from 26 providers.
DR DNASU; 224762; -.
DR Ensembl; ENSMUST00000078438; ENSMUSP00000077535; ENSMUSG00000058063.
DR GeneID; 224762; -.
DR KEGG; mmu:224762; -.
DR UCSC; uc008cll.1; mouse.
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; 553601at2759; -.
DR PhylomeDB; Q8R0K2; -.
DR TreeFam; TF342569; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 224762; 1 hit in 72 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 27 other tissues.
DR Genevisible; Q8R0K2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
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; 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:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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 Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 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 Coiled coil; Cytoplasm; 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"
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
