NTAL_HUMAN
ID NTAL_HUMAN Reviewed; 243 AA.
AC Q9GZY6; A6NFK6; A8K209; A8K4F1; D3DXF9; Q9BXX8; Q9NZY9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Linker for activation of T-cells family member 2;
DE AltName: Full=Linker for activation of B-cells;
DE AltName: Full=Membrane-associated adapter molecule;
DE AltName: Full=Non-T-cell activation linker;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 15 protein;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 5 protein;
GN Name=LAT2; Synonyms=LAB, NTAL, WBS15, WBSCR15, WBSCR5; ORFNames=HSPC046;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE, AND TISSUE SPECIFICITY.
RX PubMed=11124535; DOI=10.1159/000056790;
RA Doyle J.L., DeSilva U., Miller W., Green E.D.;
RT "Divergent human and mouse orthologs of a novel gene (WBSCR15/Wbscr15)
RT reside within the genomic interval commonly deleted in Williams syndrome.";
RL Cytogenet. Cell Genet. 90:285-290(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISEASE.
RX PubMed=11003705; DOI=10.1007/s003350010166;
RA Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V.,
RA Koop B.F.;
RT "Comparative genomic sequence analysis of the Williams syndrome region
RT (LIMK1-RFC2) of human chromosome 7q11.23.";
RL Mamm. Genome 11:890-898(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH GRB2; SOS1; GAB1 AND CBL, TISSUE
RP SPECIFICITY, PALMITOYLATION AT CYS-25 AND CYS-28, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233, UBIQUITINATION, AND
RP FUNCTION.
RC TISSUE=Leukocyte;
RX PubMed=12486104; DOI=10.1084/jem.20021405;
RA Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O., Spicka J.,
RA Hilgert I., Luskova P., Draber P., Novak P., Engels N., Wienands J.,
RA Simeoni L., Oesterreicher J., Aguado E., Malissen M., Schraven B.,
RA Horejsi V.;
RT "Non-T cell activation linker (NTAL): a transmembrane adaptor protein
RT involved in immunoreceptor signaling.";
RL J. Exp. Med. 196:1617-1626(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, INTERACTION WITH GRB2, AND FUNCTION.
RC TISSUE=B-cell;
RX PubMed=12514734; DOI=10.1038/ni882;
RA Janssen E., Zhu M., Zhang W., Koonpaew S., Zhang W.;
RT "LAB: a new membrane-associated adaptor molecule in B cell activation.";
RL Nat. Immunol. 4:117-123(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DISEASE.
RA Tassabehji M., Heather L., Gladwin A., Metcalfe K., Donnai D., Read A.,
RA Wilmot C.;
RT "A novel gene, WBS15, is deleted in patients with Williams syndrome.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neutrophil, Placenta, Spleen, and Substantia nigra;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Lymph;
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 [11]
RP FUNCTION.
RX PubMed=15010370; DOI=10.1182/blood-2003-08-2769;
RA Tkaczyk C., Horejsi V., Iwaki S., Draber P., Samelson L.E.,
RA Satterthwaite A.B., Nahm D.H., Metcalfe D.D., Gilfillan A.M.;
RT "NTAL phosphorylation is a pivotal link between the signaling cascades
RT leading to human mast cell degranulation following Kit activation and Fc
RT epsilon RI aggregation.";
RL Blood 104:207-214(2004).
RN [12]
RP MUTAGENESIS OF TYR-58; TYR-84; TYR-95; TYR-110; TYR-118; TYR-136; TYR-193
RP AND TYR-233, PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233, AND
RP INTERACTION WITH GRB2.
RX PubMed=14722116; DOI=10.1074/jbc.m311394200;
RA Koonpaew S., Janssen E., Zhu M., Zhang W.;
RT "The importance of three membrane-distal tyrosines in the adaptor protein
RT NTAL/LAB.";
RL J. Biol. Chem. 279:11229-11235(2004).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in FCER1 (high affinity immunoglobulin epsilon
CC receptor)-mediated signaling in mast cells. May also be involved in BCR
CC (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high
CC affinity immunoglobulin gamma Fc receptor I)-mediated signaling in
CC myeloid cells. Couples activation of these receptors and their
CC associated kinases with distal intracellular events through the
CC recruitment of GRB2. {ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:15010370}.
CC -!- SUBUNIT: When phosphorylated, interacts with GRB2. May also interact
CC with SOS1, GAB1 and CBL. {ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:14722116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:12514734}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:12486104, ECO:0000269|PubMed:12514734}.
CC Note=Present in lipid rafts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZY6-2; Sequence=VSP_016643;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, peripheral blood
CC lymphocytes, and germinal centers of lymph nodes. Also expressed in
CC placenta, lung, pancreas and small intestine. Present in B-cells, NK
CC cells and monocytes. Absent from T-cells (at protein level).
CC {ECO:0000269|PubMed:11124535, ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:16160011}.
CC -!- PTM: Phosphorylated on tyrosines following cross-linking of BCR in B-
CC cells, FCGR1 in myeloid cells, or FCER1 in mast cells; which induces
CC the recruitment of GRB2. {ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:12514734, ECO:0000269|PubMed:14722116}.
CC -!- PTM: May be polyubiquitinated. {ECO:0000269|PubMed:12486104}.
CC -!- DISEASE: Note=LAT2 is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region. Haploinsufficiency of LAT2 may
CC be the cause of certain cardiovascular and musculo-skeletal
CC abnormalities observed in the disease. {ECO:0000269|PubMed:11003705,
CC ECO:0000269|PubMed:11124535, ECO:0000269|Ref.5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29018.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF257135; AAF91352.1; -; mRNA.
DR EMBL; AF045555; AAF74978.1; -; Genomic_DNA.
DR EMBL; AY190023; AAO63155.1; -; mRNA.
DR EMBL; AF252611; AAK37429.1; -; mRNA.
DR EMBL; AF252612; AAK37430.1; -; mRNA.
DR EMBL; AF252613; AAK37633.1; -; mRNA.
DR EMBL; AF252614; AAK37431.1; -; mRNA.
DR EMBL; AF161531; AAF29018.1; ALT_FRAME; mRNA.
DR EMBL; AK002099; BAA92084.1; -; mRNA.
DR EMBL; AK092904; BAG52627.1; -; mRNA.
DR EMBL; AK290074; BAF82763.1; -; mRNA.
DR EMBL; AK290916; BAF83605.1; -; mRNA.
DR EMBL; AC005081; AAS07404.1; -; Genomic_DNA.
DR EMBL; AC005081; AAS07405.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69610.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69611.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69612.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69613.1; -; Genomic_DNA.
DR EMBL; BC001609; AAH01609.1; -; mRNA.
DR EMBL; BC009204; AAH09204.1; -; mRNA.
DR CCDS; CCDS5566.2; -. [Q9GZY6-1]
DR RefSeq; NP_054865.2; NM_014146.3. [Q9GZY6-1]
DR RefSeq; NP_115852.1; NM_032463.2. [Q9GZY6-1]
DR RefSeq; NP_115853.2; NM_032464.2. [Q9GZY6-1]
DR RefSeq; XP_011514860.1; XM_011516558.2. [Q9GZY6-1]
DR PDB; 3MAZ; X-ray; 1.90 A; B=133-141.
DR PDBsum; 3MAZ; -.
DR AlphaFoldDB; Q9GZY6; -.
DR SMR; Q9GZY6; -.
DR BioGRID; 113301; 6.
DR IntAct; Q9GZY6; 1.
DR STRING; 9606.ENSP00000420494; -.
DR iPTMnet; Q9GZY6; -.
DR PhosphoSitePlus; Q9GZY6; -.
DR SwissPalm; Q9GZY6; -.
DR BioMuta; LAT2; -.
DR CPTAC; CPTAC-972; -.
DR EPD; Q9GZY6; -.
DR jPOST; Q9GZY6; -.
DR MassIVE; Q9GZY6; -.
DR MaxQB; Q9GZY6; -.
DR PaxDb; Q9GZY6; -.
DR PeptideAtlas; Q9GZY6; -.
DR PRIDE; Q9GZY6; -.
DR ProteomicsDB; 80174; -. [Q9GZY6-1]
DR ProteomicsDB; 80175; -. [Q9GZY6-2]
DR Antibodypedia; 1198; 503 antibodies from 40 providers.
DR DNASU; 7462; -.
DR Ensembl; ENST00000275635.11; ENSP00000275635.7; ENSG00000086730.17. [Q9GZY6-1]
DR Ensembl; ENST00000344995.9; ENSP00000344881.5; ENSG00000086730.17. [Q9GZY6-1]
DR Ensembl; ENST00000398475.5; ENSP00000381492.1; ENSG00000086730.17. [Q9GZY6-1]
DR Ensembl; ENST00000460943.6; ENSP00000420494.1; ENSG00000086730.17. [Q9GZY6-1]
DR Ensembl; ENST00000488266.5; ENSP00000433807.1; ENSG00000086730.17. [Q9GZY6-2]
DR GeneID; 7462; -.
DR KEGG; hsa:7462; -.
DR MANE-Select; ENST00000460943.6; ENSP00000420494.1; NM_032464.3; NP_115853.2.
DR UCSC; uc003uag.4; human. [Q9GZY6-1]
DR CTD; 7462; -.
DR DisGeNET; 7462; -.
DR GeneCards; LAT2; -.
DR HGNC; HGNC:12749; LAT2.
DR HPA; ENSG00000086730; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605719; gene.
DR neXtProt; NX_Q9GZY6; -.
DR OpenTargets; ENSG00000086730; -.
DR PharmGKB; PA37356; -.
DR VEuPathDB; HostDB:ENSG00000086730; -.
DR eggNOG; ENOG502SH0N; Eukaryota.
DR GeneTree; ENSGT00390000006821; -.
DR HOGENOM; CLU_099084_0_0_1; -.
DR InParanoid; Q9GZY6; -.
DR OMA; ASCRYQN; -.
DR OrthoDB; 1271896at2759; -.
DR PhylomeDB; Q9GZY6; -.
DR TreeFam; TF336203; -.
DR PathwayCommons; Q9GZY6; -.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR SignaLink; Q9GZY6; -.
DR BioGRID-ORCS; 7462; 7 hits in 1075 CRISPR screens.
DR ChiTaRS; LAT2; human.
DR EvolutionaryTrace; Q9GZY6; -.
DR GeneWiki; LAT2; -.
DR GenomeRNAi; 7462; -.
DR Pharos; Q9GZY6; Tbio.
DR PRO; PR:Q9GZY6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9GZY6; protein.
DR Bgee; ENSG00000086730; Expressed in monocyte and 153 other tissues.
DR ExpressionAtlas; Q9GZY6; baseline and differential.
DR Genevisible; Q9GZY6; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042169; F:SH2 domain binding; IMP:HGNC-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; IDA:HGNC-UCL.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IGI:HGNC-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:HGNC-UCL.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR InterPro; IPR031428; LAT2.
DR PANTHER; PTHR15646; PTHR15646; 1.
DR Pfam; PF15703; LAT2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Immunity; Lipoprotein; Mast cell degranulation; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Williams-Beuren syndrome.
FT CHAIN 1..243
FT /note="Linker for activation of T-cells family member 2"
FT /id="PRO_0000083334"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 174..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT MOD_RES 136
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12486104,
FT ECO:0000305|PubMed:14722116"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12486104,
FT ECO:0000305|PubMed:14722116"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12486104,
FT ECO:0000269|PubMed:14722116"
FT LIPID 25
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12486104"
FT LIPID 28
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12486104"
FT VAR_SEQ 112..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_016643"
FT MUTAGEN 58
FT /note="Y->F: No change in phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 84
FT /note="Y->F: No change in phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 95
FT /note="Y->F: Slightly reduces phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 110
FT /note="Y->F: No change in phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 118
FT /note="Y->F: No change in phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 136
FT /note="Y->F: Slightly reduces phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 193
FT /note="Y->F: Reduces phosphorylation upon BCR activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT MUTAGEN 233
FT /note="Y->F: Strongly reduces phosphorylation upon BCR
FT activation."
FT /evidence="ECO:0000269|PubMed:14722116"
FT CONFLICT 39
FT /note="I -> M (in Ref. 7; BAF82763)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="Q -> A (in Ref. 6; AAF29018)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="G -> R (in Ref. 6; AAF29018)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> M (in Ref. 6; AAF29018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 26550 MW; 222D2CCF3C71C503 CRC64;
MSSGTELLWP GAALLVLLGV AASLCVRCSR PGAKRSEKIY QQRSLREDQQ SFTGSRTYSL
VGQAWPGPLA DMAPTRKDKL LQFYPSLEDP ASSRYQNFSK GSRHGSEEAY IDPIAMEYYN
WGRFSKPPED DDANSYENVL ICKQKTTETG AQQEGIGGLC RGDLSLSLAL KTGPTSGLCP
SASPEEDEES EDYQNSASIH QWRESRKVMG QLQREASPGP VGSPDEEDGE PDYVNGEVAA
TEA
