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Linker for activation of T-cells family member 2 (Linker for activation of B-cells) (Membrane-associated adapter molecule) (Non-T-cell activation linker) (Williams-Beuren syndrome chromosomal region 15 protein homolog)

 NTAL_MOUSE              Reviewed;         203 AA.
Q9JHL0; Q3UYF6; Q9JJ29;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 122.
RecName: Full=Linker for activation of T-cells family member 2;
AltName: Full=Linker for activation of B-cells;
AltName: Full=Membrane-associated adapter molecule;
AltName: Full=Non-T-cell activation linker;
AltName: Full=Williams-Beuren syndrome chromosomal region 15 protein homolog;
Name=Lat2; Synonyms=Lab, Ntal, Wbscr15, Wbscr5;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=11124535;
Doyle J.L., DeSilva U., Miller W., Green E.D.;
"Divergent human and mouse orthologs of a novel gene (WBSCR15/Wbscr15)
reside within the genomic interval commonly deleted in Williams
syndrome.";
Cytogenet. Cell Genet. 90:285-290(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
STRAIN=129/SvJ;
PubMed=11003705; DOI=10.1007/s003350010166;
Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X.,
Duronio V., Koop B.F.;
"Comparative genomic sequence analysis of the Williams syndrome region
(LIMK1-RFC2) of human chromosome 7q11.23.";
Mamm. Genome 11:890-898(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=12514734; DOI=10.1038/ni882;
Janssen E., Zhu M., Zhang W., Koonpaew S., Zhang W.;
"LAB: a new membrane-associated adaptor molecule in B cell
activation.";
Nat. Immunol. 4:117-123(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Green E.D.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
TISSUE=Aorta, Cecum, Embryo, Medulla oblongata, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=129; TISSUE=Mammary tumor;
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]
TISSUE SPECIFICITY.
PubMed=15539154; DOI=10.1016/j.immuni.2004.09.007;
Stork B., Engelke M., Frey J., Horejsi V., Hamm-Baarke A.,
Schraven B., Kurosaki T., Wienands J.;
"Grb2 and the non-T cell activation linker NTAL constitute a Ca(2+)-
regulating signal circuit in B lymphocytes.";
Immunity 21:681-691(2004).
[8]
TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH GRB2, FUNCTION,
AND SUBCELLULAR LOCATION.
PubMed=15477350; DOI=10.1084/jem.20041223;
Zhu M., Liu Y., Koonpaew S., Granillo O., Zhang W.;
"Positive and negative regulation of FcepsilonRI-mediated signaling by
the adaptor protein LAB/NTAL.";
J. Exp. Med. 200:991-1000(2004).
[9]
FUNCTION, INTERACTION WITH GRB2, AND SUBCELLULAR LOCATION.
PubMed=15477348; DOI=10.1084/jem.20041213;
Volna P., Lebduska P., Draberova L., Simova S., Heneberg P.,
Boubelik M., Bugajev V., Malissen B., Wilson B.S., Horejsi V.,
Malissen M., Draber P.;
"Negative regulation of mast cell signaling and function by the
adaptor LAB/NTAL.";
J. Exp. Med. 200:1001-1013(2004).
[10]
DEVELOPMENTAL STAGE, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15899851; DOI=10.1128/MCB.25.11.4455-4465.2005;
Wang Y., Horvath O., Hamm-Baarke A., Richelme M., Gregoire C.,
Guinamard R., Horejsi V., Angelisova P., Spicka J., Schraven B.,
Malissen B., Malissen M.;
"Single and combined deletions of the NTAL/LAB and LAT adaptors
minimally affect B-cell development and function.";
Mol. Cell. Biol. 25:4455-4465(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-59 AND SER-60, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
-!- FUNCTION: Involved in FCER1 (high affinity immunoglobulin epsilon
receptor)-mediated signaling in mast cells. May also be involved
in BCR (B-cell antigen receptor)-mediated signaling in B-cells and
FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated
signaling in myeloid cells. Couples activation of these receptors
and their associated kinases with distal intracellular events
through the recruitment of GRB2. {ECO:0000269|PubMed:15477348,
ECO:0000269|PubMed:15477350, ECO:0000269|PubMed:15899851}.
-!- SUBUNIT: When phosphorylated, interacts with GRB2. May also
interact with SOS1, GAB1 and CBL. {ECO:0000269|PubMed:15477348,
ECO:0000269|PubMed:15477350}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15477348,
ECO:0000269|PubMed:15477350}; Single-pass type III membrane
protein {ECO:0000269|PubMed:15477348,
ECO:0000269|PubMed:15477350}. Note=Present in lipid rafts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JHL0-1; Sequence=Displayed;
Name=2;
IsoId=Q9JHL0-2; Sequence=VSP_016646;
-!- TISSUE SPECIFICITY: Strongly expressed in testis. Expressed in
heart, spleen and lung. Present in B-cells and mast cells (at
protein level). {ECO:0000269|PubMed:11124535,
ECO:0000269|PubMed:15477350, ECO:0000269|PubMed:15539154}.
-!- DEVELOPMENTAL STAGE: Hardly expressed in pro-B and pre-B cells.
Moderately expressed in immature B-cells, mature B-cells and
plasma cells. Highly expressed in transitional B-cells.
{ECO:0000269|PubMed:15899851}.
-!- PTM: Phosphorylated on tyrosines following cross-linking of BCR in
B-cells, high affinity IgG receptor (FCGR1) in myeloid cells, or
high affinity IgE receptor (FCER1) in mast cells; which induces
the recruitment of GRB2. {ECO:0000269|PubMed:15477350}.
-!- DISRUPTION PHENOTYPE: Mice exhibit normal T-cell, B-cell and mast
cell development and normal humoral response, but have
hyperresponsive mast cells. {ECO:0000269|PubMed:15899851}.
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EMBL; AF257136; AAF91353.1; -; mRNA.
EMBL; AF139987; AAF75558.1; -; Genomic_DNA.
EMBL; AF139987; AAF75559.1; -; Genomic_DNA.
EMBL; AY190024; AAO63156.1; -; mRNA.
EMBL; AF289664; AAF99331.1; -; Genomic_DNA.
EMBL; AK134721; BAE22256.1; -; mRNA.
EMBL; AK138953; BAE23833.1; -; mRNA.
EMBL; AK143533; BAE25422.1; -; mRNA.
EMBL; AK162321; BAE36852.1; -; mRNA.
EMBL; BC005804; AAH05804.1; -; mRNA.
CCDS; CCDS39311.1; -. [Q9JHL0-2]
CCDS; CCDS39312.1; -. [Q9JHL0-1]
RefSeq; NP_064428.1; NM_020044.3. [Q9JHL0-1]
RefSeq; NP_075253.2; NM_022964.4. [Q9JHL0-2]
RefSeq; XP_006504513.1; XM_006504450.2. [Q9JHL0-1]
RefSeq; XP_006504514.1; XM_006504451.3. [Q9JHL0-1]
RefSeq; XP_006504515.1; XM_006504452.2. [Q9JHL0-2]
UniGene; Mm.391375; -.
CORUM; Q9JHL0; -.
STRING; 10090.ENSMUSP00000046900; -.
iPTMnet; Q9JHL0; -.
PhosphoSitePlus; Q9JHL0; -.
SwissPalm; Q9JHL0; -.
PaxDb; Q9JHL0; -.
PeptideAtlas; Q9JHL0; -.
PRIDE; Q9JHL0; -.
Ensembl; ENSMUST00000036362; ENSMUSP00000046900; ENSMUSG00000040751. [Q9JHL0-1]
Ensembl; ENSMUST00000077636; ENSMUSP00000076824; ENSMUSG00000040751. [Q9JHL0-2]
Ensembl; ENSMUST00000200998; ENSMUSP00000143977; ENSMUSG00000040751. [Q9JHL0-1]
GeneID; 56743; -.
KEGG; mmu:56743; -.
UCSC; uc008zwm.2; mouse. [Q9JHL0-1]
UCSC; uc008zwo.2; mouse. [Q9JHL0-2]
CTD; 7462; -.
MGI; MGI:1926479; Lat2.
eggNOG; ENOG410IZVX; Eukaryota.
eggNOG; ENOG4111816; LUCA.
GeneTree; ENSGT00390000006821; -.
HOGENOM; HOG000113868; -.
HOVERGEN; HBG082063; -.
InParanoid; Q9JHL0; -.
OMA; EDGEPDY; -.
OrthoDB; EOG091G0M21; -.
PhylomeDB; Q9JHL0; -.
TreeFam; TF336203; -.
Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
PRO; PR:Q9JHL0; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000040751; -.
CleanEx; MM_LAT2; -.
ExpressionAtlas; Q9JHL0; baseline and differential.
Genevisible; Q9JHL0; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0045121; C:membrane raft; ISS:HGNC.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042169; F:SH2 domain binding; ISS:HGNC.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0042113; P:B cell activation; ISS:HGNC.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:HGNC.
GO; GO:0019722; P:calcium-mediated signaling; ISS:HGNC.
GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC.
GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
InterPro; IPR031428; LAT2.
PANTHER; PTHR15646; PTHR15646; 1.
Pfam; PF15703; LAT2; 1.
ProDom; PD332876; PD332876; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Immunity; Lipoprotein; Mast cell degranulation;
Membrane; Palmitate; Phosphoprotein; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 203 Linker for activation of T-cells family
member 2.
/FTId=PRO_0000083335.
TOPO_DOM 1 6 Extracellular. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 28 203 Cytoplasmic. {ECO:0000255}.
MOD_RES 59 59 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 139 139 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9GZY6}.
MOD_RES 160 160 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9GZY6}.
MOD_RES 192 192 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9GZY6}.
LIPID 26 26 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 29 29 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 92 103 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_016646.
CONFLICT 114 114 V -> E (in Ref. 5; BAE22256).
{ECO:0000305}.
SEQUENCE 203 AA; 22876 MW; 1B21A87D8FBAE097 CRC64;
MSAELELLWP VSGLLLLLLG ATAWLCVHCS RPGVKRNEKI YEQRNRQENA QSSAAAQTYS
LARQVWPGPQ MDTAPNKSFE RKNKMLFSHL EGPESPRYQN FYKGSNQEPD AAYVDPIPTN
YYNWGCFQKP SEDDDSNSYE NVLVCKPSTP ESGVEDFEDY QNSVSIHQWR ESKRTMGAPM
SLSGSPDEEP DYVNGDVAAA ENI


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