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SH2 domain-containing protein 1A (Signaling lymphocytic activation molecule-associated protein) (SLAM-associated protein) (T-cell signal transduction molecule SAP)

 SH21A_MOUSE             Reviewed;         126 AA.
O88890; A2ANL8; Q9QWV6;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 136.
RecName: Full=SH2 domain-containing protein 1A;
AltName: Full=Signaling lymphocytic activation molecule-associated protein;
Short=SLAM-associated protein;
AltName: Full=T-cell signal transduction molecule SAP;
Name=Sh2d1a; Synonyms=Xlp;
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 LONG).
STRAIN=BALB/cJ;
PubMed=9774102; DOI=10.1038/26683;
Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S.,
Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E.,
Aversa G., Terhorst C.;
"The X-linked lymphoproliferative-disease gene product SAP regulates
signals induced through the co-receptor SLAM.";
Nature 395:462-469(1998).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT).
STRAIN=C57BL/6J;
Garrity D.B., Amemiya C.T.;
"cDNA sequence of the mouse homolog of the human X-linked
lymphoproliferative-disease gene.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
PubMed=10970095; DOI=10.1007/s002510000215;
Wu C., Sayos J., Wang N., Howie D., Coyle A., Terhorst C.;
"Genomic organization and characterization of mouse SAP, the gene that
is altered in X-linked lymphoproliferative disease.";
Immunogenetics 51:805-815(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
INTERACTION WITH FYN, AND MUTAGENESIS OF ARG-32; PRO-70;
74-LYS-ARG-75; 78-ARG-LYS-79 AND PRO-90.
PubMed=12545173; DOI=10.1038/ncb919;
Latour S., Roncagalli R., Chen R., Bakinowski M., Shi X.,
Schwartzberg P.L., Davidson D., Veillette A.;
"Binding of SAP SH2 domain to FynT SH3 domain reveals a novel
mechanism of receptor signalling in immune regulation.";
Nat. Cell Biol. 5:149-154(2003).
[6]
FUNCTION IN NTRK2 SIGNALING, AND INTERACTION WITH NTRK1; NTRK2 AND
NTRK3.
PubMed=16223723; DOI=10.1074/jbc.M506554200;
Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.;
"SLAM-associated protein as a potential negative regulator in Trk
signaling.";
J. Biol. Chem. 280:41744-41752(2005).
[7]
FUNCTION.
PubMed=19648922; DOI=10.1038/ni.1763;
Dong Z., Cruz-Munoz M.E., Zhong M.C., Chen R., Latour S.,
Veillette A.;
"Essential function for SAP family adaptors in the surveillance of
hematopoietic cells by natural killer cells.";
Nat. Immunol. 10:973-980(2009).
[8]
FUNCTION.
PubMed=20962259; DOI=10.4049/jimmunol.1001974;
Wang N., Calpe S., Westcott J., Castro W., Ma C., Engel P.,
Schatzle J.D., Terhorst C.;
"The adapters EAT-2A and -2B are positive regulators of CD244- and
CD84-dependent NK cell functions in the C57BL/6 mouse.";
J. Immunol. 185:5683-5687(2010).
[9]
REVIEW.
PubMed=21219180; DOI=10.1146/annurev-immunol-030409-101302;
Cannons J.L., Tangye S.G., Schwartzberg P.L.;
"SLAM family receptors and SAP adaptors in immunity.";
Annu. Rev. Immunol. 29:665-705(2011).
[10]
FUNCTION, AND MUTAGENESIS OF ARG-78.
PubMed=22683124; DOI=10.1016/j.immuni.2012.03.023;
Dong Z., Davidson D., Perez-Quintero L.A., Kurosaki T., Swat W.,
Veillette A.;
"The adaptor SAP controls NK cell activation by regulating the enzymes
Vav-1 and SHIP-1 and by enhancing conjugates with target cells.";
Immunity 36:974-985(2012).
-!- FUNCTION: Cytoplasmic adapter regulating receptors of the
signaling lymphocytic activation molecule (SLAM) family such as
SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling
seems to cooperate with SH2D1B/EAT-2. Initially it has been
proposed that association with SLAMF1 prevents SLAMF1 binding to
inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2.
However, by simultaneous interactions, recruits FYN which
subsequently phosphorylates and activates SLAMF1 (By similarity).
Positively regulates CD244/2B4- and CD84-mediated natural killer
(NK) cell functions (PubMed:22683124). Can also promote CD48-,
SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation
(PubMed:19648922). In the context of NK cell-mediated cytotoxicity
enhances conjugate formation with target cells (PubMed:22683124).
May also regulate the activity of the neurotrophin receptors
NTRK1, NTRK2 and NTRK3. {ECO:0000250|UniProtKB:B2RZ59,
ECO:0000250|UniProtKB:O60880, ECO:0000269|PubMed:16223723,
ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20962259,
ECO:0000269|PubMed:22683124, ECO:0000305|PubMed:21219180}.
-!- SUBUNIT: Interacts with CD84, CD244, LY9, SLAMF1 and FYN (By
similarity). Interacts with NTRK1, NTRK2 and NTRK3.
{ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880,
ECO:0000269|PubMed:16223723}.
-!- INTERACTION:
Q9QUM4:Slamf1; NbExp=3; IntAct=EBI-7910438, EBI-7910086;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=O88890-1; Sequence=Displayed;
Name=Short;
IsoId=O88890-2; Sequence=VSP_004391;
-!- TISSUE SPECIFICITY: T-cells.
-----------------------------------------------------------------------
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EMBL; AF072903; AAC62629.1; -; mRNA.
EMBL; AF097633; AAC95999.1; -; mRNA.
EMBL; AF097632; AAC95998.1; -; mRNA.
EMBL; AF154505; AAF14526.1; -; Genomic_DNA.
EMBL; AF154503; AAF14526.1; JOINED; Genomic_DNA.
EMBL; AF154504; AAF14526.1; JOINED; Genomic_DNA.
EMBL; AL831716; CAM19525.1; -; Genomic_DNA.
CCDS; CCDS30099.1; -. [O88890-1]
CCDS; CCDS85770.1; -. [O88890-2]
RefSeq; NP_001300617.1; NM_001313688.1.
RefSeq; NP_001300618.1; NM_001313689.1. [O88890-2]
RefSeq; NP_001300620.1; NM_001313691.1.
RefSeq; NP_035494.1; NM_011364.4. [O88890-1]
UniGene; Mm.441197; -.
ProteinModelPortal; O88890; -.
SMR; O88890; -.
CORUM; O88890; -.
IntAct; O88890; 3.
MINT; O88890; -.
STRING; 10090.ENSMUSP00000005839; -.
iPTMnet; O88890; -.
PhosphoSitePlus; O88890; -.
PaxDb; O88890; -.
PRIDE; O88890; -.
Ensembl; ENSMUST00000005839; ENSMUSP00000005839; ENSMUSG00000005696. [O88890-1]
Ensembl; ENSMUST00000115070; ENSMUSP00000110722; ENSMUSG00000005696. [O88890-2]
Ensembl; ENSMUST00000189753; ENSMUSP00000141070; ENSMUSG00000005696. [O88890-1]
GeneID; 20400; -.
KEGG; mmu:20400; -.
UCSC; uc009tbb.1; mouse. [O88890-1]
CTD; 4068; -.
MGI; MGI:1328352; Sh2d1a.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00510000046904; -.
HOGENOM; HOG000231700; -.
HOVERGEN; HBG003702; -.
InParanoid; O88890; -.
KO; K07990; -.
OMA; CLCVLCK; -.
OrthoDB; EOG091G0ULG; -.
PhylomeDB; O88890; -.
TreeFam; TF343096; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
PRO; PR:O88890; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000005696; Expressed in 44 organ(s), highest expression level in thymus.
CleanEx; MM_SH2D1A; -.
ExpressionAtlas; O88890; baseline and differential.
Genevisible; O88890; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
GO; GO:0006968; P:cellular defense response; IEA:InterPro.
GO; GO:0006959; P:humoral immune response; IMP:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
CDD; cd10400; SH2_SAP1a; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR017289; SH2_prot_1A.
InterPro; IPR035876; SH2D1A_SH2.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF037828; SH2_p1A; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Acetylation; Adaptive immunity; Alternative splicing;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Reference proteome; SH2 domain.
CHAIN 1 126 SH2 domain-containing protein 1A.
/FTId=PRO_0000097723.
DOMAIN 6 104 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 67 92 Interaction with FYN SH3 domain.
{ECO:0000269|PubMed:12545173}.
MOD_RES 89 89 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60880}.
VAR_SEQ 44 46 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_004391.
MUTAGEN 32 32 R->K: No effect on interaction with FYN
SH3 domain.
{ECO:0000269|PubMed:12545173}.
MUTAGEN 68 68 T->I: No effect on interaction with FYN
SH3 domain.
{ECO:0000269|PubMed:12545173}.
MUTAGEN 70 70 P->A: No effect on interaction with FYN
SH3 domain.
{ECO:0000269|PubMed:12545173}.
MUTAGEN 74 75 KR->AA: Disrupts interaction with FYN SH3
domain. {ECO:0000269|PubMed:12545173}.
MUTAGEN 78 79 RK->AA: Disrupts interaction with FYN SH3
domain. {ECO:0000269|PubMed:12545173}.
MUTAGEN 78 78 R->A: No effect on NK cell development,
impairs promotion of NK cell cytotoxicity
and IFN-gamma production in response to
hematopoietic cells.
{ECO:0000269|PubMed:22683124}.
MUTAGEN 90 90 P->K: No effect on interaction with FYN
SH3 domain.
{ECO:0000269|PubMed:12545173}.
SEQUENCE 126 AA; 13904 MW; D78FA7CE425AA680 CRC64;
MDAVTVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYQGY IYTYRVSQTE
TGSWSAETAP GVHKRFFRKV KNLISAFQKP DQGIVTPLQY PVEKSSGRGP QAPTGRRDSD
ICLNAP


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