SH21A_RAT
ID SH21A_RAT Reviewed; 126 AA.
AC B2RZ59;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=SH2 domain-containing protein 1A;
GN Name=Sh2d1a;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
RP FUNCTION IN NTRK2 SIGNALING, AND INTERACTION WITH NTRK1; NTRK2 AND NTRK3.
RX PubMed=16223723; DOI=10.1074/jbc.m506554200;
RA Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.;
RT "SLAM-associated protein as a potential negative regulator in Trk
RT signaling.";
RL J. Biol. Chem. 280:41744-41752(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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: 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 (PubMed:16223723).
CC {ECO:0000250|UniProtKB:O60880, ECO:0000250|UniProtKB:O88890,
CC ECO:0000269|PubMed:16223723}.
CC -!- SUBUNIT: Interacts with CD84, CD244, LY9, SLAMF1 and FYN (By
CC similarity). Interacts with NTRK1, NTRK2 and NTRK3.
CC {ECO:0000250|UniProtKB:O88890, ECO:0000269|PubMed:16223723}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88890}.
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DR EMBL; BC167036; AAI67036.1; -; mRNA.
DR EMBL; CH473991; EDM10890.1; -; Genomic_DNA.
DR RefSeq; NP_001102783.2; NM_001109313.2.
DR RefSeq; XP_008771750.1; XM_008773528.2.
DR AlphaFoldDB; B2RZ59; -.
DR SMR; B2RZ59; -.
DR STRING; 10116.ENSRNOP00000008444; -.
DR iPTMnet; B2RZ59; -.
DR PhosphoSitePlus; B2RZ59; -.
DR PaxDb; B2RZ59; -.
DR GeneID; 501502; -.
DR KEGG; rno:501502; -.
DR UCSC; RGD:1562408; rat.
DR CTD; 4068; -.
DR RGD; 1562408; Sh2d1a.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_125532_1_0_1; -.
DR InParanoid; B2RZ59; -.
DR OMA; CVLCNGY; -.
DR OrthoDB; 1417830at2759; -.
DR PhylomeDB; B2RZ59; -.
DR TreeFam; TF343096; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR PRO; PR:B2RZ59; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000006263; Expressed in thymus and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0006959; P:humoral immune response; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Adaptive immunity; Cytoplasm; Immunity; Innate immunity;
KW Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..126
FT /note="SH2 domain-containing protein 1A"
FT /id="PRO_0000356885"
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 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60880"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 126 AA; 13992 MW; 79BE17CC42049E6E CRC64;
MDAVTVYHGK ISREMGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYQGY IYTYRVSQTE
TGSWSAETAP GVHKRFFRKV KNLISAFQKP DQGIVTPLQY PVEKSSARSP QAPTGRRDSD
ICLKAP
