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SH21A_PIG
ID   SH21A_PIG               Reviewed;         128 AA.
AC   Q06AA1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=SH2 domain-containing protein 1A;
GN   Name=SH2D1A;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ972963; ABI96199.1; -; mRNA.
DR   RefSeq; NP_001072143.1; NM_001078675.1.
DR   AlphaFoldDB; Q06AA1; -.
DR   SMR; Q06AA1; -.
DR   STRING; 9823.ENSSSCP00000013442; -.
DR   PaxDb; Q06AA1; -.
DR   GeneID; 780420; -.
DR   KEGG; ssc:780420; -.
DR   CTD; 4068; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   InParanoid; Q06AA1; -.
DR   OrthoDB; 1417830at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   Reference proteome; SH2 domain.
FT   CHAIN           1..128
FT                   /note="SH2 domain-containing protein 1A"
FT                   /id="PRO_0000356884"
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          103..128
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   128 AA;  14300 MW;  14C88E44F43C75A0 CRC64;
     MDAVTVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYQGY IYTYRVSHTE
     TGSWIADTAP GVHKRFFRKI KNLISAFQKP DQGIVIPLQY PVEKKSSARS TQGATGRRED
     PDVFLKTP
 
 
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