TRI11_MOUSE
ID TRI11_MOUSE Reviewed; 467 AA.
AC Q99PQ2; A2A868; A2AB84; Q3TCL5; Q8VDX5;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM11;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM11 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 11;
GN Name=Trim11;
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 [MRNA] (ISOFORM 1).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex, and Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP FUNCTION, AND INTERACTION WITH HUMANIN.
RX PubMed=12670303; DOI=10.1046/j.1460-9568.2003.02553.x;
RA Niikura T., Hashimoto Y., Tajima H., Ishizaka M., Yamagishi Y.,
RA Kawasumi M., Nawa M., Terashita K., Aiso S., Nishimoto I.;
RT "A tripartite motif protein TRIM11 binds and destabilizes Humanin, a
RT neuroprotective peptide against Alzheimer's disease-relevant insults.";
RL Eur. J. Neurosci. 17:1150-1158(2003).
RN [7]
RP INTERACTION WITH PHOX2B.
RX PubMed=18275850; DOI=10.1016/j.bbrc.2008.01.165;
RA Hong S.J., Chae H., Lardaro T., Hong S., Kim K.S.;
RT "Trim11 increases expression of dopamine beta-hydroxylase gene by
RT interacting with Phox2b.";
RL Biochem. Biophys. Res. Commun. 368:650-655(2008).
RN [8]
RP FUNCTION, INTERACTION WITH PAX6, DOMAIN B30.2, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=18628401; DOI=10.1101/gad.471708;
RA Tuoc T.C., Stoykova A.;
RT "Trim11 modulates the function of neurogenic transcription factor Pax6
RT through ubiquitin-proteosome system.";
RL Genes Dev. 22:1972-1986(2008).
RN [9]
RP FUNCTION.
RX PubMed=18248090; DOI=10.1371/journal.ppat.0040016;
RA Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W.;
RT "TRIM E3 ligases interfere with early and late stages of the retroviral
RT life cycle.";
RL PLoS Pathog. 4:E16-E16(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of
CC insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln
CC repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6
CC ubiquitination leading to proteasomal degradation, thereby modulating
CC cortical neurogenesis. May also inhibit PAX6 transcriptional activity,
CC possibly in part by preventing the binding of PAX6 to its consensus
CC sequences. May contribute to the regulation of the intracellular level
CC of HN (humanin) or HN-containing proteins through the proteasomal
CC degradation pathway. Mediates MED15 ubiquitination leading to
CC proteasomal degradation. May contribute to the innate restriction of
CC retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia
CC virus infectivity, by suppressing viral gene expression. Antiviral
CC activity depends on a functional E3 ubiquitin-protein ligase domain.
CC May regulate TRIM5 turnover via the proteasome pathway, thus
CC counteracting the TRIM5-mediated cross-species restriction of
CC retroviral infection at early stages of the retroviral life cycle.
CC {ECO:0000269|PubMed:12670303, ECO:0000269|PubMed:18248090,
CC ECO:0000269|PubMed:18628401}.
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: Binds cytoplasmic tail of integrin alpha-1 (By similarity).
CC Interacts with MED15/ARC105; this interaction leads to MED15
CC ubiquitination and proteasomal degradation (By similarity). Interacts
CC with the HN peptide. Interacts with PHOX2B. Interacts with PAX6.
CC {ECO:0000250, ECO:0000269|PubMed:12670303, ECO:0000269|PubMed:18275850,
CC ECO:0000269|PubMed:18628401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18628401}. Nucleus
CC {ECO:0000269|PubMed:18628401}. Note=In the nucleus, colocalizes with
CC PAX6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99PQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PQ2-2; Sequence=VSP_012059;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic central nervous system
CC (CNS), kidney, thymus and gut.
CC -!- INDUCTION: By PAX6. {ECO:0000269|PubMed:18628401}.
CC -!- DOMAIN: The coiled-coil domain and the B30.2 domain are both necessary
CC for interaction with HN and PAX6. They are also involved in MED15-
CC binding. {ECO:0000250}.
CC -!- DOMAIN: The B30.2 domain may be involved cellular protein quality
CC control by promoting the degradation of insoluble ubiquitinated
CC proteins. {ECO:0000269|PubMed:18628401}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220124; AAG53497.1; -; mRNA.
DR EMBL; AK139477; BAE24028.1; -; mRNA.
DR EMBL; AK170656; BAE41941.1; -; mRNA.
DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466628; EDL07693.1; -; Genomic_DNA.
DR EMBL; BC020102; AAH20102.1; -; mRNA.
DR CCDS; CCDS36168.1; -. [Q99PQ2-1]
DR CCDS; CCDS70195.1; -. [Q99PQ2-2]
DR RefSeq; NP_001277917.1; NM_001290988.1. [Q99PQ2-2]
DR RefSeq; NP_444398.1; NM_053168.2. [Q99PQ2-1]
DR AlphaFoldDB; Q99PQ2; -.
DR SMR; Q99PQ2; -.
DR BioGRID; 220446; 5.
DR STRING; 10090.ENSMUSP00000104438; -.
DR iPTMnet; Q99PQ2; -.
DR PhosphoSitePlus; Q99PQ2; -.
DR EPD; Q99PQ2; -.
DR MaxQB; Q99PQ2; -.
DR PaxDb; Q99PQ2; -.
DR PRIDE; Q99PQ2; -.
DR ProteomicsDB; 258969; -. [Q99PQ2-1]
DR ProteomicsDB; 258970; -. [Q99PQ2-2]
DR Antibodypedia; 34665; 265 antibodies from 30 providers.
DR DNASU; 94091; -.
DR Ensembl; ENSMUST00000093061; ENSMUSP00000090749; ENSMUSG00000020455. [Q99PQ2-1]
DR Ensembl; ENSMUST00000108810; ENSMUSP00000104438; ENSMUSG00000020455. [Q99PQ2-2]
DR GeneID; 94091; -.
DR KEGG; mmu:94091; -.
DR UCSC; uc007jcy.2; mouse. [Q99PQ2-1]
DR UCSC; uc011xvj.2; mouse. [Q99PQ2-2]
DR CTD; 81559; -.
DR MGI; MGI:2137355; Trim11.
DR VEuPathDB; HostDB:ENSMUSG00000020455; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160371; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q99PQ2; -.
DR OMA; RECIGRC; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q99PQ2; -.
DR TreeFam; TF338674; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94091; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Trim11; mouse.
DR PRO; PR:Q99PQ2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PQ2; protein.
DR Bgee; ENSMUSG00000020455; Expressed in granulocyte and 248 other tissues.
DR ExpressionAtlas; Q99PQ2; baseline and differential.
DR Genevisible; Q99PQ2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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; IDA:UniProtKB.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
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:0044790; P:suppression of viral release by host; IDA:UniProtKB.
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; IPR006574; PRY.
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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 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 Alternative splicing; Antiviral defense; Coiled coil; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="E3 ubiquitin-protein ligase TRIM11"
FT /id="PRO_0000056216"
FT DOMAIN 267..460
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 87..127
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..207
FT /evidence="ECO:0000255"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96F44"
FT VAR_SEQ 244
FT /note="Q -> QLCIECCALEREASIAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012059"
SQ SEQUENCE 467 AA; 52580 MW; 82B7CF68807E9DA8 CRC64;
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS
AQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLT TFCGDDLSLL CPICERSEHW
THRVRPLQEA ADDLKGRLEK SLEHLRKQME DAMLFQAQAE ETCALWQKMV ESQRQNVLGE
FERLRRLLAE EEQQLLQKLE EEELEVLPRL REGAARLGQQ STQLAALISE LESRCQLPAL
GLLQDIKDAL CRVQDVKLQP PAVVPMELRT VCRVPGLVET LRRFRGDITL DPDTANPELV
LSEDRRSVQR GEQRQALPDN PERFDPGPCV LGQERITSGR HYWEVEVGDQ TSWALGVCKE
TANRKEKGEL SAGNGFWILV FLGSFYNSNE PAFSPLRDPP KRVGIFLDYE AGHLSFYSAT
DGSLLFIFPE TLFSGTLRPL FSPLSSSPTP MTICRLIGVS GDTLGPQ
