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Linker for activation of T-cells family member 1 (36 kDa phospho-tyrosine adapter protein) (pp36) (p36-38)

 LAT_MOUSE               Reviewed;         242 AA.
O54957;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
20-JUN-2018, entry version 142.
RecName: Full=Linker for activation of T-cells family member 1;
AltName: Full=36 kDa phospho-tyrosine adapter protein;
Short=pp36;
AltName: Full=p36-38;
Name=Lat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=9489702; DOI=10.1016/S0092-8674(00)80901-0;
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.;
"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor
to cellular activation.";
Cell 92:83-92(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION IN MAST CELLS, AND TISSUE SPECIFICITY.
PubMed=10843385; DOI=10.1016/S1074-7613(00)80204-6;
Saitoh S., Arudchandran R., Manetz T.S., Zhang W., Sommers C.L.,
Love P.E., Rivera J., Samelson L.E.;
"LAT is essential for Fc(epsilon)RI-mediated mast cell activation.";
Immunity 12:525-535(2000).
[4]
INTERACTION WITH CLNK.
PubMed=11463797; DOI=10.1074/jbc.M106390200;
Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
"MIST functions through distinct domains in immunoreceptor signaling
in the presence and absence of LAT.";
J. Biol. Chem. 276:36043-36050(2001).
[5]
PALMITOYLATION.
PubMed=12626544; DOI=10.4049/jimmunol.170.6.2932;
Van Laethem F., Liang X., Andris F., Urbain J., Vandenbranden M.,
Ruysschaert J.-M., Resh M.D., Stulnig T.M., Leo O.;
"Glucocorticoids alter the lipid and protein composition of membrane
rafts of a murine T cell hybridoma.";
J. Immunol. 170:2932-2939(2003).
[6]
REVIEW ON FUNCTION IN T-CELLS.
PubMed=14696041; DOI=10.1002/bies.10384;
Sommers C.L., Samelson L.E., Love P.E.;
"LAT: a T lymphocyte adapter protein that couples the antigen receptor
to downstream signaling pathways.";
Bioessays 26:61-67(2004).
[7]
PALMITOYLATION AT CYS-27 AND CYS-30.
PubMed=19592663; DOI=10.4049/jimmunol.0803921;
Hundt M., Harada Y., De Giorgio L., Tanimura N., Zhang W., Altman A.;
"Palmitoylation-dependent plasma membrane transport but lipid raft-
independent signaling by linker for activation of T cells.";
J. Immunol. 183:1685-1694(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-109;
SER-112; SER-199; SER-212 AND SER-215, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH GRB2; PLCG1 AND THEMIS.
TISSUE=Thymocyte;
PubMed=22561606; DOI=10.1038/ni.2301;
Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J.,
Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J.,
Cao X., Lu L.;
"Tespa1 is involved in late thymocyte development through the
regulation of TCR-mediated signaling.";
Nat. Immunol. 13:560-568(2012).
-!- FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-
mediated signaling, both in mature T-cells and during their
development. Involved in FCGR3 (low affinity immunoglobulin gamma
Fc region receptor III)-mediated signaling in natural killer cells
and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated
signaling in mast cells. Couples activation of these receptors and
their associated kinases with distal intracellular events such as
mobilization of intracellular calcium stores, PKC activation, MAPK
activation or cytoskeletal reorganization through the recruitment
of PLCG1, GRB2, GRAP2, and other signaling molecules.
{ECO:0000269|PubMed:10843385}.
-!- SUBUNIT: When phosphorylated, interacts directly with the PIK3R1
subunit of phosphoinositide 3-kinase and the SH2 domains of GRB2,
GRAP, GRAP2, PLCG1 and PLCG2. Interacts indirectly with CBL, SOS,
VAV, and LCP2. Interacts with SHB and SKAP2. Interacts with FCGR1A
(By similarity). Interacts with CLNK. Interacts with GRB2, PLCG1
and THEMIS upon TCR activation in thymocytes. {ECO:0000250,
ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:22561606}.
-!- INTERACTION:
Q60631:Grb2; NbExp=5; IntAct=EBI-6390034, EBI-1688;
Q60787:Lcp2; NbExp=8; IntAct=EBI-6390034, EBI-5324248;
Q62077:Plcg1; NbExp=5; IntAct=EBI-6390034, EBI-300133;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane
protein. Note=Present in lipid rafts.
-!- TISSUE SPECIFICITY: Expressed in T-cells and mast cells.
{ECO:0000269|PubMed:10843385}.
-!- PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or
by SYK upon other immunoreceptor activation; which leads to the
recruitment of multiple signaling molecules. Is one of the most
prominently tyrosine-phosphorylated proteins detected following
TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated
by ITK leading to the recruitment of VAV1 to LAT-containing
complexes (By similarity). {ECO:0000250}.
-!- PTM: Palmitoylation of Cys-27 and Cys-30 is required for raft
targeting and efficient phosphorylation. {ECO:0000250}.
-!- MISCELLANEOUS: Engagement of killer inhibitory receptors (KIR)
disrupts the interaction of PLCG1 with LAT and blocks target cell-
induced activation of PLC, maybe by inducing the dephosphorylation
of LAT. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF036907; AAC40054.1; -; mRNA.
EMBL; BC013337; AAH13337.1; -; mRNA.
CCDS; CCDS21825.1; -.
RefSeq; NP_034819.1; NM_010689.3.
UniGene; Mm.10280; -.
ProteinModelPortal; O54957; -.
BioGrid; 201112; 2.
ELM; O54957; -.
IntAct; O54957; 58.
MINT; O54957; -.
STRING; 10090.ENSMUSP00000032997; -.
iPTMnet; O54957; -.
PhosphoSitePlus; O54957; -.
SwissPalm; O54957; -.
EPD; O54957; -.
PaxDb; O54957; -.
PRIDE; O54957; -.
Ensembl; ENSMUST00000032997; ENSMUSP00000032997; ENSMUSG00000030742.
GeneID; 16797; -.
KEGG; mmu:16797; -.
UCSC; uc009jqx.1; mouse.
CTD; 27040; -.
MGI; MGI:1342293; Lat.
eggNOG; ENOG410IW3X; Eukaryota.
eggNOG; ENOG4111EFT; LUCA.
GeneTree; ENSGT00390000014223; -.
HOGENOM; HOG000081810; -.
HOVERGEN; HBG018198; -.
InParanoid; O54957; -.
KO; K07362; -.
OMA; GSHRMPS; -.
OrthoDB; EOG091G0QKO; -.
PhylomeDB; O54957; -.
TreeFam; TF337741; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
PRO; PR:O54957; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030742; -.
CleanEx; MM_LAT; -.
ExpressionAtlas; O54957; baseline and differential.
Genevisible; O54957; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005070; F:SH3/SH2 adaptor activity; ISS:HGNC.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; ISS:HGNC.
GO; GO:0006968; P:cellular defense response; TAS:MGI.
GO; GO:0010467; P:gene expression; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0006955; P:immune response; ISS:HGNC.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:HGNC.
GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC.
GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; ISS:HGNC.
GO; GO:0050863; P:regulation of T cell activation; ISS:HGNC.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:MGI.
InterPro; IPR008359; Linker_for_activat_Tcells_prot.
PANTHER; PTHR15586; PTHR15586; 2.
Pfam; PF15234; LAT; 1.
PRINTS; PR01781; LATPROTEIN.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome; Immunity;
Lipoprotein; Mast cell degranulation; Membrane; Palmitate;
Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 242 Linker for activation of T-cells family
member 1.
/FTId=PRO_0000083326.
TOPO_DOM 1 4 Extracellular. {ECO:0000255}.
TRANSMEM 5 28 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 29 242 Cytoplasmic. {ECO:0000255}.
REGION 136 139 Interaction with PLCG1. {ECO:0000250}.
REGION 175 178 Interaction with GRB2, GRAP2 and PIK3R1.
{ECO:0000250}.
REGION 195 198 Interaction with GRB2, GRAP2 and PIK3R1.
{ECO:0000250}.
MOD_RES 40 40 Phosphothreonine.
{ECO:0000250|UniProtKB:O43561}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:O43561}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000250|UniProtKB:O43561}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 175 175 Phosphotyrosine.
{ECO:0000250|UniProtKB:O43561}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 235 235 Phosphotyrosine.
{ECO:0000250|UniProtKB:O43561}.
LIPID 27 27 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19592663}.
LIPID 30 30 S-palmitoyl cysteine.
{ECO:0000269|PubMed:19592663}.
SEQUENCE 242 AA; 26015 MW; 6AC25F7AE6E1A5C1 CRC64;
MEADALSPVG LGLLLLPFLV TLLAALCVRC RELPVSYDST STESLYPRSI LIKPPQITVP
RTPAVSYPLV TSFPPLRQPD LLPIPRSPQP LGGSHRMPSS QQNSDDANSV ASYENQEPAC
KNVDADEDED DYPNGYLVVL PDSSPAAVPV VSSAPVPSNP DLGDSAFSVE SCEDYVNVPE
SEESAEASLD GSREYVNVSP EQQPVTRAEL ASVNSQEVED EGEEEGVDGE EAPDYENLQE
LN


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