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

 LAT_HUMAN               Reviewed;         262 AA.
O43561; B7WPI0; C7C5T6; G5E9K3; O43919;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
18-JUL-2018, entry version 170.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
32-47 AND 219-233, PHOSPHORYLATION AT TYR-200, IDENTIFICATION BY MASS
SPECTROMETRY, MUTAGENESIS OF TYR-200 AND TYR-220, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH PIK3R1; GRB2; GRAP AND
PLCG1.
TISSUE=Leukemia;
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 [MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=9529333; DOI=10.1084/jem.187.7.1157;
Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F.,
Ryan J.C., Tasken K., Imboden J.B., Vaage J.T.;
"Molecular cloning of the cDNA encoding pp36, a tyrosine-
phosphorylated adaptor protein selectively expressed by T cells and
natural killer cells.";
J. Exp. Med. 187:1157-1161(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Bone marrow;
Muschen M.;
"Inactivation of pre-B cell receptor-mediated tumor suppression by
aberrant splicing in Ph+ acute lymphoblastic leukemia.";
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
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).
[7]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-26 AND CYS-29, AND
MUTAGENESIS OF CYS-26 AND CYS-29.
PubMed=9729044; DOI=10.1016/S1074-7613(00)80606-8;
Zhang W., Trible R.P., Samelson L.E.;
"LAT palmitoylation: its essential role in membrane microdomain
targeting and tyrosine phosphorylation during T cell activation.";
Immunity 9:239-246(1998).
[8]
INTERACTION WITH SHB.
PubMed=10488157; DOI=10.1074/jbc.274.39.28050;
Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.;
"Requirement of the Src homology 2 domain protein Shb for T cell
receptor-dependent activation of the interleukin-2 gene nuclear factor
for activation of T cells element in Jurkat T cells.";
J. Biol. Chem. 274:28050-28057(1999).
[9]
FUNCTION IN NK CELLS, AND INTERACTION WITH PLCG1.
PubMed=10072481;
Jevremovic D., Billadeau D.D., Schoon R.A., Dick C.J., Irvin B.J.,
Zhang W., Samelson L.E., Abraham R.T., Leibson P.J.;
"A role for the adaptor protein LAT in human NK cell-mediated
cytotoxicity.";
J. Immunol. 162:2453-2456(1999).
[10]
INTERACTION WITH GRB2; GRAP2 AND PLCG1.
PubMed=10811803; DOI=10.1074/jbc.M000404200;
Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade C.J., Samelson L.E.;
"Association of Grb2, Gads, and phospholipase C-gamma 1 with
phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations
on T cell antigen receptor-mediated signaling.";
J. Biol. Chem. 275:23355-23361(2000).
[11]
INTERACTION WITH FCGR1A.
PubMed=10781611; DOI=10.1074/jbc.M909462199;
Tridandapani S., Lyden T.W., Smith J.L., Carter J.E., Coggeshall K.M.,
Anderson C.L.;
"The adapter protein LAT enhances fcgamma receptor-mediated signal
transduction in myeloid cells.";
J. Biol. Chem. 275:20480-20487(2000).
[12]
PHOSPHORYLATION, AND INTERACTION WITH LCP2; SKAP2; GRB2; PLCG2 AND
CBL.
PubMed=10942756; DOI=10.1074/jbc.M001439200;
Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A.,
Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J.,
Schraven B., Watson S.P.;
"Interaction of linker for activation of T cells with multiple adapter
proteins in platelets activated by the glycoprotein VI-selective
ligand, convulxin.";
J. Biol. Chem. 275:33427-33434(2000).
[13]
INTERACTION WITH PIK3R1 AND PLCG1, AND MUTAGENESIS OF TYR-161.
PubMed=11368773; DOI=10.1042/0264-6021:3560461;
Paz P.E., Wang S., Clarke H., Lu X., Stokoe D., Abo A.;
"Mapping the Zap-70 phosphorylation sites on LAT (linker for
activation of T cells) required for recruitment and activation of
signalling proteins in T cells.";
Biochem. J. 356:461-471(2001).
[14]
PROBABLE DEPHOSPHORYLATION BY PTPRJ.
PubMed=11259588; DOI=10.1128/MCB.21.7.2393-2403.2001;
Baker J.E., Majeti R., Tangye S.G., Weiss A.;
"Protein tyrosine phosphatase CD148-mediated inhibition of T-cell
receptor signal transduction is associated with reduced LAT and
phospholipase Cgamma1 phosphorylation.";
Mol. Cell. Biol. 21:2393-2403(2001).
[15]
PHOSPHORYLATION BY ITK.
PubMed=12186560; DOI=10.1021/bi025554o;
Perez-Villar J.J., Whitney G.S., Sitnick M.T., Dunn R.J.,
Venkatesan S., O'Day K., Schieven G.L., Lin T.A., Kanner S.B.;
"Phosphorylation of the linker for activation of T-cells by Itk
promotes recruitment of Vav.";
Biochemistry 41:10732-10740(2002).
[16]
PROBABLE DEPHOSPHORYLATION BY PTPRJ.
PubMed=12913111; DOI=10.1083/jcb.200303040;
Lin J., Weiss A.;
"The tyrosine phosphatase CD148 is excluded from the immunologic
synapse and down-regulates prolonged T cell signaling.";
J. Cell Biol. 162:673-682(2003).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[18]
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).
[19]
TISSUE SPECIFICITY.
PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L.,
Pozzobon M., Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T.,
Horejsi V.;
"Transmembrane adaptor molecules: a new category of lymphoid-cell
markers.";
Blood 107:213-221(2006).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-101 AND SER-224,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; SER-40; SER-41;
SER-43; SER-101; SER-106; SER-240; SER-241 AND TYR-255, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
INVOLVEMENT IN IMD52.
PubMed=27242165; DOI=10.1084/jem.20151110;
Keller B., Zaidman I., Yousefi O.S., Hershkovitz D., Stein J.,
Unger S., Schachtrup K., Sigvardsson M., Kuperman A.A., Shaag A.,
Schamel W.W., Elpeleg O., Warnatz K., Stepensky P.;
"Early onset combined immunodeficiency and autoimmunity in patients
with loss-of-function mutation in LAT.";
J. Exp. Med. 213:1185-1199(2016).
[24]
INVOLVEMENT IN IMD52.
PubMed=27522155; DOI=10.1016/j.jaci.2016.05.036;
Bacchelli C., Moretti F.A., Carmo M., Adams S., Stanescu H.C.,
Pearce K., Madkaikar M., Gilmour K.C., Nicholas A.K., Woods C.G.,
Kleta R., Beales P.L., Qasim W., Gaspar H.B.;
"Mutations in linker for activation of T cells (LAT) lead to a novel
form of severe combined immunodeficiency.";
J. Allergy Clin. Immunol. 139:634-642(2017).
-!- 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:10072481}.
-!- 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, SKAP2 and CLNK (By similarity).
Interacts with FCGR1A. Interacts with GRB2, PLCG1 and THEMIS upon
TCR activation in thymocytes (By similarity). {ECO:0000250}.
-!- INTERACTION:
P00533:EGFR; NbExp=2; IntAct=EBI-1222766, EBI-297353;
P62993:GRB2; NbExp=7; IntAct=EBI-1222766, EBI-401755;
P62993-1:GRB2; NbExp=3; IntAct=EBI-8070286, EBI-15787932;
P06239:LCK; NbExp=2; IntAct=EBI-1222766, EBI-1348;
P27986:PIK3R1; NbExp=4; IntAct=EBI-1222766, EBI-79464;
P08487:PLCG1 (xeno); NbExp=4; IntAct=EBI-8070286, EBI-8013886;
P19174:PLCG1; NbExp=7; IntAct=EBI-1222766, EBI-79387;
P18031:PTPN1; NbExp=3; IntAct=EBI-1222766, EBI-968788;
O43765:SGTA; NbExp=3; IntAct=EBI-1222766, EBI-347996;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9489702,
ECO:0000269|PubMed:9729044}; Single-pass type III membrane protein
{ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9729044}.
Note=Present in lipid rafts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Long;
IsoId=O43561-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=O43561-2; Sequence=VSP_004303;
Name=3;
IsoId=O43561-3; Sequence=VSP_054758, VSP_004303;
Note=Gene prediction based on EST data.;
Name=4;
IsoId=O43561-4; Sequence=VSP_054759, VSP_004303;
Name=5;
IsoId=O43561-5; Sequence=VSP_054759;
-!- TISSUE SPECIFICITY: Expressed in thymus, T-cells, NK cells, mast
cells and, at lower levels, in spleen. Present in T-cells but not
B-cells (at protein level). {ECO:0000269|PubMed:16160011,
ECO:0000269|PubMed:9489702}.
-!- 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.
-!- PTM: Palmitoylation of Cys-26 and Cys-29 is required for raft
targeting and efficient phosphorylation.
{ECO:0000269|PubMed:9729044}.
-!- DISEASE: Immunodeficiency 52 (IMD52) [MIM:617514]: An autosomal
recessive primary immunodeficiency characterized by T-cell
abnormalities, resulting in severe combined immunodeficiency,
autoimmune disease, progressive lymphopenia and
hypogammaglobulinemia, and lymphoproliferation with splenomegaly.
Patients develop severe recurrent infections from infancy.
{ECO:0000269|PubMed:27242165, ECO:0000269|PubMed:27522155}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- 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.
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EMBL; AF036906; AAC39637.1; -; mRNA.
EMBL; AF036905; AAC39636.1; -; mRNA.
EMBL; AJ223280; CAA11218.1; -; mRNA.
EMBL; FN432832; CBA11533.1; -; mRNA.
EMBL; AC109460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471267; EAW52027.1; -; Genomic_DNA.
EMBL; CH471267; EAW52028.1; -; Genomic_DNA.
EMBL; BC011563; AAH11563.1; -; mRNA.
CCDS; CCDS10647.1; -. [O43561-1]
CCDS; CCDS32425.1; -. [O43561-2]
CCDS; CCDS45455.1; -. [O43561-4]
CCDS; CCDS53999.1; -. [O43561-3]
RefSeq; NP_001014987.1; NM_001014987.1. [O43561-2]
RefSeq; NP_001014988.1; NM_001014988.1. [O43561-4]
RefSeq; NP_001014989.2; NM_001014989.1. [O43561-3]
RefSeq; NP_055202.1; NM_014387.3. [O43561-1]
UniGene; Hs.632179; -.
ProteinModelPortal; O43561; -.
BioGrid; 117971; 40.
CORUM; O43561; -.
DIP; DIP-29231N; -.
IntAct; O43561; 73.
MINT; O43561; -.
ChEMBL; CHEMBL5779; -.
iPTMnet; O43561; -.
PhosphoSitePlus; O43561; -.
SwissPalm; O43561; -.
BioMuta; LAT; -.
MaxQB; O43561; -.
PeptideAtlas; O43561; -.
PRIDE; O43561; -.
ProteomicsDB; 49052; -.
ProteomicsDB; 49053; -. [O43561-2]
Ensembl; ENST00000360872; ENSP00000354119; ENSG00000213658. [O43561-1]
Ensembl; ENST00000395456; ENSP00000378841; ENSG00000213658. [O43561-2]
Ensembl; ENST00000395461; ENSP00000378845; ENSG00000213658. [O43561-3]
Ensembl; ENST00000454369; ENSP00000398793; ENSG00000213658. [O43561-4]
Ensembl; ENST00000564277; ENSP00000457036; ENSG00000213658. [O43561-4]
Ensembl; ENST00000566177; ENSP00000456761; ENSG00000213658. [O43561-5]
GeneID; 27040; -.
KEGG; hsa:27040; -.
UCSC; uc002dsb.4; human. [O43561-1]
CTD; 27040; -.
DisGeNET; 27040; -.
EuPathDB; HostDB:ENSG00000213658.10; -.
GeneCards; LAT; -.
HGNC; HGNC:18874; LAT.
HPA; CAB002223; -.
HPA; CAB012978; -.
HPA; HPA011157; -.
MalaCards; LAT; -.
MIM; 602354; gene.
MIM; 617514; phenotype.
neXtProt; NX_O43561; -.
OpenTargets; ENSG00000213658; -.
PharmGKB; PA38728; -.
GeneTree; ENSGT00390000014223; -.
HOGENOM; HOG000081810; -.
HOVERGEN; HBG018198; -.
InParanoid; O43561; -.
KO; K07362; -.
OMA; GSHRMPS; -.
OrthoDB; EOG091G0QKO; -.
PhylomeDB; O43561; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
SignaLink; O43561; -.
SIGNOR; O43561; -.
GeneWiki; Linker_of_activated_T_cells; -.
GenomeRNAi; 27040; -.
PRO; PR:O43561; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000213658; -.
CleanEx; HS_LAT; -.
ExpressionAtlas; O43561; baseline and differential.
Genevisible; O43561; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0001772; C:immunological synapse; IDA:HGNC.
GO; GO:0016021; C:integral component of membrane; IDA:HGNC.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0045121; C:membrane raft; TAS:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:HGNC.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; IMP:HGNC.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0010467; P:gene expression; IEA:Ensembl.
GO; GO:0006955; P:immune response; IDA:HGNC.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:HGNC.
GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC.
GO; GO:0002260; P:lymphocyte homeostasis; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEP:CACAO.
GO; GO:0007265; P:Ras protein signal transduction; IMP:HGNC.
GO; GO:0050863; P:regulation of T cell activation; IMP:HGNC.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
InterPro; IPR008359; Linker_for_activat_Tcells_prot.
PANTHER; PTHR15586; PTHR15586; 1.
Pfam; PF15234; LAT; 1.
PRINTS; PR01781; LATPROTEIN.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Direct protein sequencing; Immunity; Lipoprotein;
Mast cell degranulation; Membrane; Palmitate; Phosphoprotein;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 262 Linker for activation of T-cells family
member 1.
/FTId=PRO_0000083325.
TOPO_DOM 1 4 Extracellular. {ECO:0000255}.
TRANSMEM 5 27 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 28 262 Cytoplasmic. {ECO:0000255}.
REGION 161 164 Interaction with PLCG1.
REGION 200 203 Interaction with GRB2, GRAP2 and PIK3R1.
{ECO:0000269|PubMed:10811803}.
REGION 220 223 Interaction with GRB2, GRAP2 and PIK3R1.
{ECO:0000269|PubMed:10811803}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000250|UniProtKB:O54957}.
MOD_RES 110 110 Phosphotyrosine. {ECO:0000305}.
MOD_RES 156 156 Phosphotyrosine. {ECO:0000305}.
MOD_RES 161 161 Phosphotyrosine. {ECO:0000305}.
MOD_RES 200 200 Phosphotyrosine.
{ECO:0000269|PubMed:9489702}.
MOD_RES 220 220 Phosphotyrosine. {ECO:0000305}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 255 255 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
LIPID 26 26 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9729044}.
LIPID 29 29 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9729044}.
VAR_SEQ 1 1 M -> MEATAASWQVAVPVLGGASRPLGPRGAASLLRAPLQ
M (in isoform 3). {ECO:0000305}.
/FTId=VSP_054758.
VAR_SEQ 83 83 Missing (in isoform 4 and isoform 5).
{ECO:0000303|Ref.3}.
/FTId=VSP_054759.
VAR_SEQ 114 142 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9489702,
ECO:0000303|PubMed:9529333}.
/FTId=VSP_004303.
MUTAGEN 26 26 C->A: Reduces palmitoylation; abolishes
localization to lipid rafts.
{ECO:0000269|PubMed:9729044}.
MUTAGEN 29 29 C->A: Reduces palmitoylation; impairs
localization to lipid rafts.
{ECO:0000269|PubMed:9729044}.
MUTAGEN 161 161 Y->F: Abolishes interaction with PLCG1.
{ECO:0000269|PubMed:11368773}.
MUTAGEN 200 200 Y->F: Abolishes interaction with GRB2 and
PIK3R1; when associated with F-220.
{ECO:0000269|PubMed:9489702}.
MUTAGEN 220 220 Y->F: Abolishes interaction with GRB2 and
PIK3R1; when associated with F-200.
{ECO:0000269|PubMed:9489702}.
SEQUENCE 262 AA; 27930 MW; BCD80AE7DCA64153 CRC64;
MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ FKRPHTVAPW
PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD SDGANSVASY ENEGASGIRG
AQAGWGVWGP SWTRLTPVSL PPEPACEDAD EDEDDYHNPG YLVVLPDSTP ATSTAAPSAP
ALSTPGIRDS AFSMESIDDY VNVPESGESA EASLDGSREY VNVSQELHPG AAKTEPAALS
SQEAEEVEEE GAPDYENLQE LN


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