TESP1_MOUSE
ID TESP1_MOUSE Reviewed; 458 AA.
AC Q3U132; Q3TR68; Q8CEN9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein TESPA1;
DE AltName: Full=Thymocyte-expressed positive selection-associated protein 1;
GN Name=Tespa1;
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), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Thymocyte;
RX PubMed=22561606; DOI=10.1038/ni.2301;
RA Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C.,
RA Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.;
RT "Tespa1 is involved in late thymocyte development through the regulation of
RT TCR-mediated signaling.";
RL Nat. Immunol. 13:560-568(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; 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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 INTERACTION WITH ITPR1 AND ITPR3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23650607; DOI=10.1016/j.fob.2012.08.005;
RA Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K.,
RA Hamabashiri M., Tanaka M., Shirasawa S.;
RT "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding protein in
RT T and B lymphocytes.";
RL FEBS Open Bio 2:255-259(2012).
RN [6]
RP PHOSPHORYLATION, AND INTERACTION WITH ITPR3.
RX PubMed=23541577; DOI=10.1016/j.bbrc.2013.02.128;
RA Fujimoto T., Matsuzaki H., Tanaka M., Shirasawa S.;
RT "Tespa1 protein is phosphorylated in response to store-operated calcium
RT entry.";
RL Biochem. Biophys. Res. Commun. 434:162-165(2013).
CC -!- FUNCTION: May play a role in the regulation of inositol 1,4,5-
CC trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+)
CC uptake via the mitochondria-associated endoplasmic reticulum membrane
CC (MAM) compartment (By similarity). Required for the development and
CC maturation of T-cells, its function being essential for the late stages
CC of thymocyte development. Plays a role in T-cell antigen receptor
CC (TCR)-mediated activation of the ERK and NFAT signaling pathways,
CC possibly by serving as a scaffolding protein that promotes the assembly
CC of the LAT signalosome in thymocytes. {ECO:0000250,
CC ECO:0000269|PubMed:22561606}.
CC -!- SUBUNIT: Interacts with PLCG1 and GRB2; the association is increased
CC with prolonged stimulation of the TCR and may facilitate the assembly
CC of the LAT signalosome (By similarity). Interacts with ITPR1 and ITPR3.
CC Interacts with HSPA9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2RU30}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:23650607}. Note=May
CC localize to mitochondria-associated endoplasmic reticulum membrane
CC (MAM). {ECO:0000250|UniProtKB:A2RU30}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U132-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U132-2; Sequence=VSP_030491, VSP_030492;
CC Name=3;
CC IsoId=Q3U132-3; Sequence=VSP_030490;
CC -!- TISSUE SPECIFICITY: Expressed in lymphoid tissues, with highest
CC expression levels detected in thymus and lower levels in spleen and
CC lymph nodes (at protein level). Detected in CD4(+) and CD8(+) T-cells,
CC B-cells and mast cells. Not detected in monocytes/macrophages.
CC {ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23650607}.
CC -!- DEVELOPMENTAL STAGE: Present in fetal thymus at 14.5 dpc. Expressed
CC during thymocyte maturation, the expression being highest in
CC CD4(+)CD8(+) thymocytes and decreasing with maturation.
CC {ECO:0000269|PubMed:22561606}.
CC -!- PTM: May be phosphorylated in response to store-operated Ca(+2) entry.
CC {ECO:0000269|PubMed:23541577}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice display defective T-cell development,
CC resulting in notably fewer mature CD4(+) and CD8(+) cells in the
CC thymus. The architecture of the thymus is altered, as characterized by
CC smaller areas of the medulla. Mice also have fewer peripheral T-cells
CC in spleen and display diminished T-cell antigen receptor (TCR)-mediated
CC responses. {ECO:0000269|PubMed:22561606}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64065.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK017900; BAC25532.1; ALT_INIT; mRNA.
DR EMBL; AK156313; BAE33668.1; -; mRNA.
DR EMBL; AK163027; BAE37162.1; -; mRNA.
DR EMBL; BC064065; AAH64065.2; ALT_INIT; mRNA.
DR CCDS; CCDS48735.1; -. [Q3U132-1]
DR RefSeq; NP_899087.2; NM_183264.4. [Q3U132-1]
DR RefSeq; XP_006514069.1; XM_006514006.3. [Q3U132-1]
DR AlphaFoldDB; Q3U132; -.
DR IntAct; Q3U132; 2.
DR STRING; 10090.ENSMUSP00000047284; -.
DR iPTMnet; Q3U132; -.
DR PhosphoSitePlus; Q3U132; -.
DR EPD; Q3U132; -.
DR jPOST; Q3U132; -.
DR PaxDb; Q3U132; -.
DR PRIDE; Q3U132; -.
DR ProteomicsDB; 259000; -. [Q3U132-1]
DR ProteomicsDB; 259001; -. [Q3U132-2]
DR ProteomicsDB; 259002; -. [Q3U132-3]
DR Antibodypedia; 48438; 86 antibodies from 24 providers.
DR Ensembl; ENSMUST00000042586; ENSMUSP00000047284; ENSMUSG00000034833. [Q3U132-1]
DR Ensembl; ENSMUST00000217702; ENSMUSP00000152009; ENSMUSG00000034833. [Q3U132-2]
DR GeneID; 67596; -.
DR KEGG; mmu:67596; -.
DR UCSC; uc007hrj.3; mouse. [Q3U132-1]
DR UCSC; uc007hrk.2; mouse. [Q3U132-2]
DR CTD; 9840; -.
DR MGI; MGI:1914846; Tespa1.
DR VEuPathDB; HostDB:ENSMUSG00000034833; -.
DR eggNOG; ENOG502QWSR; Eukaryota.
DR GeneTree; ENSGT00940000160763; -.
DR HOGENOM; CLU_040123_0_0_1; -.
DR InParanoid; Q3U132; -.
DR OMA; KAPCCTH; -.
DR OrthoDB; 417705at2759; -.
DR PhylomeDB; Q3U132; -.
DR TreeFam; TF331566; -.
DR BioGRID-ORCS; 67596; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tespa1; mouse.
DR PRO; PR:Q3U132; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3U132; protein.
DR Bgee; ENSMUSG00000034833; Expressed in thymus and 58 other tissues.
DR Genevisible; Q3U132; MM.
DR GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036398; C:TCR signalosome; IDA:MGI.
DR GO; GO:0043274; F:phospholipase binding; IPI:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0010387; P:COP9 signalosome assembly; IMP:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:UniProtKB.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IDA:MGI.
DR GO; GO:0036399; P:TCR signalosome assembly; IMP:MGI.
DR InterPro; IPR029325; ITPR-bd.
DR InterPro; IPR026647; TESPA1.
DR InterPro; IPR043444; TESPA1-like.
DR PANTHER; PTHR17469; PTHR17469; 1.
DR PANTHER; PTHR17469:SF1; PTHR17469:SF1; 1.
DR Pfam; PF14722; KRAP_IP3R_bind; 1.
DR SMART; SM01257; KRAP_IP3R_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Signalosome.
FT CHAIN 1..458
FT /note="Protein TESPA1"
FT /id="PRO_0000315220"
FT REGION 328..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030490"
FT VAR_SEQ 221..238
FT /note="SRFKQVQTLAVTADAFFC -> NVSLTQENIKMSHEHQLP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030491"
FT VAR_SEQ 239..458
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030492"
SQ SEQUENCE 458 AA; 51768 MW; 191D30456E6E5515 CRC64;
MEASVLSPTS WEKRRAWLRQ SRNWQTQVLE EEAAAALQDA LDPEPSSLDD VFQEGNPINK
IEDWLQGCGC RDTEEGLSEE SGQSNYSGYS SHGTSFEDDL SLGAEATLLS TNGNLFSRNF
LQTPRLCQLL DLGSSLASSS MTGGTNKTSS SISEILDQVQ EDAEDILFSL GFGHENHKDT
SRIPARFFSN PSQAKGINFQ LFLKSQVQRM EMEDPCLMLA SRFKQVQTLA VTADAFFCLY
SYVSKTPVQK FTPSNMFWNF DPTDVPSIRI LAPEPEPYSP RERLRRAISK MCLYTGSRDR
LSSSYNNPKK NSLDQIVWEV MDRVKGEKIQ QDPEHRQALG EESVPPIQNT NPSTSSLPCV
SYPKEETQGD MCHAHALARP GPQYHINSTQ VRRQLWVLQD INEKPRSAEN ESPWERKSKA
RKNLFQRVPV DKNIKSLNLP TIQQKQNQGQ ARHELTNL
