ID   SH21A_SAGOE             Reviewed;         127 AA.
AC   Q9BG88;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=SH2 domain-containing protein 1A;
GN   Name=SH2D1A;
OS   Saguinus oedipus (Cotton-top tamarin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Saguinus.
OX   NCBI_TaxID=9490;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Peripheral blood lymphocyte;
RX   PubMed=11477068; DOI=10.1074/jbc.m101305200;
RA   Morra M., Simarro-Grande M., Martin M., Chen A.S.-I., Lanyi A.,
RA   Silander O., Calpe S., Davis J., Pawson T., Eck M.J., Sumegi J., Engel P.,
RA   Li S.-C., Terhorst C.;
RT   "Characterization of SH2D1A missense mutations identified in X-linked
RT   lymphoproliferative disease patients.";
RL   J. Biol. Chem. 276:36809-36816(2001).
CC   -!- FUNCTION: Cytoplasmic adapter regulating receptors of the signaling
CC       lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244,
CC       LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with
CC       SH2D1B/EAT-2. Initially it has been proposed that association with
CC       SLAMF1 prevents SLAMF1 binding to inhibitory effectors including
CC       INPP5D/SHIP1 and PTPN11/SHP-2. However, by simultaneous interactions,
CC       recruits FYN which subsequently phosphorylates and activates SLAMF1.
CC       Positively regulates CD244/2B4- and CD84-mediated natural killer (NK)
CC       cell functions. Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-
CC       mediated NK cell activation. In the context of NK cell-mediated
CC       cytotoxicity enhances conjugate formation with target cells (By
CC       similarity). May also regulate the activity of the neurotrophin
CC       receptors NTRK1, NTRK2 and NTRK3 (By similarity).
CC       {ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880,
CC       ECO:0000250|UniProtKB:O88890}.
CC   -!- SUBUNIT: Interacts with CD84, CD244, LY9, SLAMF1 and FYN. Interacts
CC       with NTRK1, NTRK2 and NTRK3 (By similarity).
CC       {ECO:0000250|UniProtKB:B2RZ59, ECO:0000250|UniProtKB:O60880}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60880}.
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DR   EMBL; AF322913; AAK11579.1; -; mRNA.
DR   AlphaFoldDB; Q9BG88; -.
DR   SMR; Q9BG88; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   GO; GO:0006968; P:cellular defense response; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   CDD; cd10400; SH2_SAP1a; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR017289; SH2_prot_1A.
DR   InterPro; IPR035876; SH2D1A_SH2.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF037828; SH2_p1A; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Adaptive immunity; Cytoplasm; Immunity; Innate immunity;
KW   SH2 domain.
FT   CHAIN           1..127
FT                   /note="SH2 domain-containing protein 1A"
FT                   /id="PRO_0000356886"
FT   DOMAIN          6..102
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          67..92
FT                   /note="Interaction with FYN SH3 domain"
FT                   /evidence="ECO:0000250|UniProtKB:O88890"
FT   REGION          104..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60880"
SQ   SEQUENCE   127 AA;  14085 MW;  7E34B95191E4D492 CRC64;
     MDAVAVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYHGY IYTYRVSQTE
     TGSWSAETAP GVHKRYFRKI KNLISAFQKP DQGIVIPLQY PVEKSSPRST QGTTGIREDP
     DVCLKAP