LAT_RAT
ID LAT_RAT Reviewed; 241 AA.
AC O70601;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Linker for activation of T-cells family member 1;
DE AltName: Full=36 kDa phospho-tyrosine adapter protein;
DE Short=pp36;
DE AltName: Full=p36-38;
GN Name=Lat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PVG; TISSUE=Natural killer cell;
RX PubMed=9529333; DOI=10.1084/jem.187.7.1157;
RA Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F.,
RA Ryan J.C., Tasken K., Imboden J.B., Vaage J.T.;
RT "Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated
RT adaptor protein selectively expressed by T cells and natural killer
RT cells.";
RL J. Exp. Med. 187:1157-1161(1998).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
RA Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
RA Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
RA Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
RT "Transmembrane adaptor molecules: a new category of lymphoid-cell
RT markers.";
RL Blood 107:213-221(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-109; SER-112
RP AND SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-
CC mediated signaling, both in mature T-cells and during their
CC development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc
CC region receptor III)-mediated signaling in natural killer cells and
CC FCER1 (high affinity immunoglobulin epsilon receptor)-mediated
CC signaling in mast cells. Couples activation of these receptors and
CC their associated kinases with distal intracellular events such as
CC mobilization of intracellular calcium stores, PKC activation, MAPK
CC activation or cytoskeletal reorganization through the recruitment of
CC PLCG1, GRB2, GRAP2, and other signaling molecules (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: When phosphorylated, interacts directly with the PIK3R1
CC subunit of phosphoinositide 3-kinase and the SH2 domains of GRB2, GRAP,
CC GRAP2, PLCG1 and PLCG2. Interacts indirectly with CBL, SOS, VAV, and
CC LCP2. Interacts with SHB, SKAP2 and CLNK. Interacts with FCGR1A.
CC Interacts with GRB2, PLCG1 and THEMIS upon TCR activation in thymocytes
CC (By similarity). Interacts with THEMIS2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O54957}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}. Note=Present in lipid rafts.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in NK cells. Present in lymph node,
CC spleen and thymus (at protein level). {ECO:0000269|PubMed:16160011}.
CC -!- PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by
CC SYK upon other immunoreceptor activation; which leads to the
CC recruitment of multiple signaling molecules. Is one of the most
CC prominently tyrosine-phosphorylated proteins detected following TCR
CC engagement. May be dephosphorylated by PTPRJ (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Palmitoylation of Cys-27 and Cys-30 is required for raft targeting
CC and efficient phosphorylation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Engagement of killer inhibitory receptors (KIR) disrupts
CC the interaction of PLCG1 with LAT and blocks target cell-induced
CC activation of PLC, maybe by inducing the dephosphorylation of LAT.
CC {ECO:0000250}.
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DR EMBL; AJ001184; CAA04577.1; -; mRNA.
DR RefSeq; NP_110480.1; NM_030853.1.
DR AlphaFoldDB; O70601; -.
DR STRING; 10116.ENSRNOP00000023563; -.
DR iPTMnet; O70601; -.
DR PhosphoSitePlus; O70601; -.
DR PaxDb; O70601; -.
DR Ensembl; ENSRNOT00000023563; ENSRNOP00000023563; ENSRNOG00000017429.
DR GeneID; 81511; -.
DR KEGG; rno:81511; -.
DR UCSC; RGD:620802; rat.
DR CTD; 27040; -.
DR RGD; 620802; Lat.
DR eggNOG; ENOG502SXAZ; Eukaryota.
DR GeneTree; ENSGT00390000014223; -.
DR HOGENOM; CLU_093883_0_0_1; -.
DR InParanoid; O70601; -.
DR OMA; WGPSWAR; -.
DR OrthoDB; 1328822at2759; -.
DR PhylomeDB; O70601; -.
DR TreeFam; TF337741; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-202433; Generation of second messenger molecules.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR PRO; PR:O70601; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017429; Expressed in thymus and 19 other tissues.
DR Genevisible; O70601; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0002260; P:lymphocyte homeostasis; ISO:RGD.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0050863; P:regulation of T cell activation; ISO:RGD.
DR InterPro; IPR008359; Linker_for_activat_Tcells_prot.
DR PANTHER; PTHR15586; PTHR15586; 2.
DR Pfam; PF15234; LAT; 1.
DR PRINTS; PR01781; LATPROTEIN.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Immunity; Lipoprotein;
KW Mast cell degranulation; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..241
FT /note="Linker for activation of T-cells family member 1"
FT /id="PRO_0000083327"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..28
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 78..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..139
FT /note="Interaction with PLCG1"
FT /evidence="ECO:0000250"
FT REGION 175..178
FT /note="Interaction with GRB2, GRAP2 and PIK3R1"
FT /evidence="ECO:0000250"
FT REGION 195..198
FT /note="Interaction with GRB2, GRAP2 and PIK3R1"
FT /evidence="ECO:0000250"
FT REGION 209..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43561"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43561"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 175
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O43561"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54957"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43561"
FT MOD_RES 234
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O43561"
FT LIPID 27
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 26193 MW; FBD5C4D4BBCE4275 CRC64;
MEADALSPVE LGLLLLPFVV MLLAALCVRC RELPASYDSA STESLYPRSI LIKPPQITVP
RTPATSYPLV TSFPPLRQPD LLPIPRSPQP LGGSHRMPSS RQNSDDANSV ASYENQEPAR
KNVDEDEDED DYPEGYLVVL PDSSPAAVPV VSSAPVPSNP DLGDSAFSME SCEDYVNVPE
SEESAEASLD GSREYVNVSQ DAQPVIRAEL ASVTSQEVED EEEEDVDGEE APDYENLQEL
N
