TRI29_MOUSE
ID TRI29_MOUSE Reviewed; 587 AA.
AC Q8R2Q0; Q8CEE2; Q922Y3; Q99PN5; Q9CSC9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tripartite motif-containing protein 29;
GN Name=Trim29;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-587.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [MRNA] OF 339-519.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH NEMO, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27695001; DOI=10.1038/ni.3580;
RA Xing J., Weng L., Yuan B., Wang Z., Jia L., Jin R., Lu H., Li X.C.,
RA Liu Y.J., Zhang Z.;
RT "Identification of a role for TRIM29 in the control of innate immunity in
RT the respiratory tract.";
RL Nat. Immunol. 17:1373-1380(2016).
CC -!- FUNCTION: Plays a crucial role in the regulation of macrophage
CC activation in response to viral or bacterial infections within the
CC respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in
CC the lysosome where it induces its 'Lys-48' ubiquitination and
CC subsequent degradation. In turn, the expression of type I interferons
CC and the production of pro-inflammatory cytokines are inhibited.
CC Additionally, induces the 'Lys-48' ubiquitination of STING1 in a
CC similar way, leading to its degradation.
CC {ECO:0000250|UniProtKB:Q14134}.
CC -!- SUBUNIT: Interacts with VIM and HINT1. Interacts with IKBKG/NEMO.
CC Interacts with STING1. {ECO:0000250|UniProtKB:Q14134}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14134}.
CC Lysosome {ECO:0000250|UniProtKB:Q14134}. Note=Colocalizes with
CC intermediate filaments. {ECO:0000250|UniProtKB:Q14134}.
CC -!- DISRUPTION PHENOTYPE: Absence of TRIM29 enhances macrophage production
CC of type I interferons and protects mice from infection with influenza
CC virus. {ECO:0000269|PubMed:27695001}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25956.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC006699; AAH06699.1; -; mRNA.
DR EMBL; BC027353; AAH27353.1; -; mRNA.
DR EMBL; AK013219; BAB28721.1; -; mRNA.
DR EMBL; AK028448; BAC25956.1; ALT_INIT; mRNA.
DR EMBL; AF230390; AAG50169.1; -; mRNA.
DR CCDS; CCDS52775.1; -.
DR RefSeq; NP_076144.2; NM_023655.2.
DR AlphaFoldDB; Q8R2Q0; -.
DR SMR; Q8R2Q0; -.
DR BioGRID; 215196; 17.
DR IntAct; Q8R2Q0; 1.
DR STRING; 10090.ENSMUSP00000034511; -.
DR iPTMnet; Q8R2Q0; -.
DR PhosphoSitePlus; Q8R2Q0; -.
DR MaxQB; Q8R2Q0; -.
DR PaxDb; Q8R2Q0; -.
DR PeptideAtlas; Q8R2Q0; -.
DR PRIDE; Q8R2Q0; -.
DR ProteomicsDB; 259315; -.
DR Antibodypedia; 18856; 607 antibodies from 40 providers.
DR Ensembl; ENSMUST00000034511; ENSMUSP00000034511; ENSMUSG00000032013.
DR GeneID; 72169; -.
DR KEGG; mmu:72169; -.
DR UCSC; uc009pbi.2; mouse.
DR CTD; 23650; -.
DR MGI; MGI:1919419; Trim29.
DR VEuPathDB; HostDB:ENSMUSG00000032013; -.
DR eggNOG; ENOG502QWDV; Eukaryota.
DR GeneTree; ENSGT00940000161416; -.
DR HOGENOM; CLU_039304_0_0_1; -.
DR InParanoid; Q8R2Q0; -.
DR OMA; TNGHSGE; -.
DR OrthoDB; 429763at2759; -.
DR PhylomeDB; Q8R2Q0; -.
DR TreeFam; TF351086; -.
DR BioGRID-ORCS; 72169; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Trim29; mouse.
DR PRO; PR:Q8R2Q0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R2Q0; protein.
DR Bgee; ENSMUSG00000032013; Expressed in lip and 97 other tissues.
DR Genevisible; Q8R2Q0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Lysosome; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="Tripartite motif-containing protein 29"
FT /id="PRO_0000056243"
FT ZN_FING 220..260
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..348
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14134"
FT CONFLICT 220..227
FT /note="FEARKCPL -> SRPENVPC (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 65820 MW; D6E5C65F6A05EA98 CRC64;
MEGADACRSN GASPEARDTR SPPGPSGSLE NGTKADSKDT KTTNGHSGEV TEGKTLGSAL
KSGEGKSGLF SSNEWRRPII QFVESVDDKG SSYFSMDSAE GRRSPYAGLQ LGASKKPPVT
FAEKGELRKS IFSEPRKPTV TIVEPGEVRR NSYPRADSSL LARAKSGSEE VLCDSCIGNK
QKAVKSCLVC QASFCELHLK PHLEGAAFRD HQLLEPIRDF EARKCPLHGK TMELFCQTDQ
TCICYLCMFQ EHKNHSTVTV EEAKAEKETE LSLQKEQLQL KIIEIEDDVE KWQKEKDRIK
SFTTNEKAIL EQNFRDLVRE LEKQKEEVRA ALEQREQDAV DQVKVIVDAL DERAKVLHED
KQTREQLHNI SDSVLFLQEF GALMSNYSLP PPLPTYHVLL EGEGLGQSLG NCKDDLLNVC
MRHVEKMCKA DLSRNFIERN HMENGGDHRY MNSYTSSYGN EWSTPDTMKR YSMYLTPKGG
GRTSYQPSSP SRLSKETNQK NFNNLYGTKG NYTSRVWEYT STVQNSEDMP TVQGNSSFSL
KGFPSLLRSQ VPKAQPQTWK SGKQTLLSHY RPFYVNKGSG IGSNEAP
