TRAT1_MOUSE
ID TRAT1_MOUSE Reviewed; 187 AA.
AC Q3UU67; Q3SXD9; Q3SXE0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=T-cell receptor-associated transmembrane adapter 1;
DE AltName: Full=T-cell receptor-interacting molecule;
DE Short=TRIM;
GN Name=Trat1;
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11439161; DOI=10.1046/j.1365-3083.2001.00953.x;
RA Huynh T., Wuerch A., Bruyns E., Korinek V., Schraven B., Eichmann K.;
RT "Developmentally regulated expression of the transmembrane adaptor protein
RT TRIM in fetal and adult T cells.";
RL Scand. J. Immunol. 54:146-154(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 MRNA] (ISOFORMS 1 AND 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Stabilizes the TCR (T-cell antigen receptor)/CD3 complex at
CC the surface of T-cells. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with CD3Z. When
CC phosphorylated, interacts with PIK3R1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UU67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UU67-2; Sequence=VSP_016638, VSP_016640;
CC Name=3; Synonyms=DeltaTM-TRIM;
CC IsoId=Q3UU67-3; Sequence=VSP_016639;
CC -!- TISSUE SPECIFICITY: Present in T-cells (at protein level).
CC {ECO:0000269|PubMed:11439161}.
CC -!- DEVELOPMENTAL STAGE: Present in thymocytes from 16.5 dpc (at protein
CC level). {ECO:0000269|PubMed:11439161}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR activation. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Strongly expressed at 13.5 dpc, then down-
CC regulated. Marginal in adult. Protein may be unstable. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI04352.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK138735; BAE23761.1; -; mRNA.
DR EMBL; BC104350; AAI04351.1; -; mRNA.
DR EMBL; BC104351; AAI04352.2; ALT_INIT; mRNA.
DR CCDS; CCDS37352.1; -. [Q3UU67-1]
DR RefSeq; NP_938039.2; NM_198297.3. [Q3UU67-1]
DR RefSeq; XP_006522795.1; XM_006522732.3. [Q3UU67-2]
DR AlphaFoldDB; Q3UU67; -.
DR STRING; 10090.ENSMUSP00000129808; -.
DR iPTMnet; Q3UU67; -.
DR PhosphoSitePlus; Q3UU67; -.
DR jPOST; Q3UU67; -.
DR PaxDb; Q3UU67; -.
DR PRIDE; Q3UU67; -.
DR ProteomicsDB; 259303; -. [Q3UU67-1]
DR Antibodypedia; 1192; 262 antibodies from 31 providers.
DR DNASU; 77647; -.
DR Ensembl; ENSMUST00000231701; ENSMUSP00000155986; ENSMUSG00000030775. [Q3UU67-1]
DR GeneID; 77647; -.
DR KEGG; mmu:77647; -.
DR UCSC; uc007zjr.1; mouse. [Q3UU67-1]
DR UCSC; uc007zjs.1; mouse. [Q3UU67-2]
DR CTD; 50852; -.
DR MGI; MGI:1924897; Trat1.
DR VEuPathDB; HostDB:ENSMUSG00000030775; -.
DR eggNOG; ENOG502S7P1; Eukaryota.
DR GeneTree; ENSGT00390000004910; -.
DR InParanoid; Q3UU67; -.
DR OrthoDB; 1572760at2759; -.
DR PhylomeDB; Q3UU67; -.
DR TreeFam; TF336066; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 77647; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q3UU67; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UU67; protein.
DR Bgee; ENSMUSG00000030775; Expressed in thymus and 41 other tissues.
DR ExpressionAtlas; Q3UU67; baseline and differential.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001920; P:negative regulation of receptor recycling; ISO:MGI.
DR GO; GO:0051051; P:negative regulation of transport; ISO:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR InterPro; IPR020399; T-cell_rcpt-assoc_TM_adapter-1.
DR PANTHER; PTHR15951; PTHR15951; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Immunity; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..187
FT /note="T-cell receptor-associated transmembrane adapter 1"
FT /id="PRO_0000083345"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 80..83
FT /note="Interaction with PIK3R1"
FT /evidence="ECO:0000250"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIZ9"
FT DISULFID 7
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016638"
FT VAR_SEQ 3..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11439161"
FT /id="VSP_016639"
FT VAR_SEQ 19..51
FT /note="GLALVISLIFNISHYVEKQRRDEIYRYSDDYIP -> MPLLPLGTSSLLGLG
FT SGYIVDLQYFPLCREAET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016640"
SQ SEQUENCE 187 AA; 21330 MW; 0FE50E7DED590647 CRC64;
MSGSSGCPFF LWGLLAFLGL ALVISLIFNI SHYVEKQRRD EIYRYSDDYI PRVDEYYVED
APIYGNLENI IPEPLDENCY EQMKGRPQRS ASDPQEVAAP AQVPAEAQMC YASLDHSVKG
KRRRPRKQNT NVSDRGKDTQ VYTMDANVSQ INMVESFPPD NQVVEESIHD DPARLFGLIR
AKREPVI
