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P55G_BOVIN
ID   P55G_BOVIN              Reviewed;         461 AA.
AC   O46404;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma;
DE            Short=PI3-kinase regulatory subunit gamma;
DE            Short=PI3K regulatory subunit gamma;
DE            Short=PtdIns-3-kinase regulatory subunit gamma;
DE   AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit gamma;
DE            Short=PI3-kinase subunit p85-gamma;
DE            Short=PtdIns-3-kinase regulatory subunit p85-gamma;
DE   AltName: Full=p55PIK;
GN   Name=PIK3R3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal cortex;
RA   Varnai P., Balla T.;
RT   "p55gamma, a regulatory subunit of PI 3-kinase from adrenal cortex.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to activated (phosphorylated) protein-tyrosine kinases
CC       through its SH2 domain and regulates their kinase activity. During
CC       insulin stimulation, it also binds to IRS-1.
CC   -!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R3 and a p110
CC       catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL (By
CC       similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest levels in brain and testis. Lower levels in
CC       adipose tissue, kidney, heart, lung and skeletal muscle. Barely
CC       detectable in liver and spleen.
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}.
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DR   EMBL; AF036256; AAB88704.1; -; mRNA.
DR   RefSeq; NP_777221.1; NM_174796.1.
DR   AlphaFoldDB; O46404; -.
DR   SMR; O46404; -.
DR   STRING; 9913.ENSBTAP00000003878; -.
DR   ChEMBL; CHEMBL4524045; -.
DR   PaxDb; O46404; -.
DR   PRIDE; O46404; -.
DR   GeneID; 286865; -.
DR   KEGG; bta:286865; -.
DR   CTD; 8503; -.
DR   eggNOG; KOG4637; Eukaryota.
DR   InParanoid; O46404; -.
DR   OrthoDB; 737926at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; IBA:GO_Central.
DR   CDD; cd09930; SH2_cSH2_p85_like; 1.
DR   CDD; cd09942; SH2_nSH2_p85_like; 1.
DR   Gene3D; 3.30.505.10; -; 2.
DR   InterPro; IPR032498; PI3K_P85_iSH2.
DR   InterPro; IPR035020; PI3kinase_P85_cSH2.
DR   InterPro; IPR035022; PI3kinase_P85_nSH2.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   Pfam; PF16454; PI3K_P85_iSH2; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 2.
DR   SUPFAM; SSF55550; SSF55550; 2.
DR   PROSITE; PS50001; SH2; 2.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; Repeat; SH2 domain.
FT   CHAIN           1..461
FT                   /note="Phosphatidylinositol 3-kinase regulatory subunit
FT                   gamma"
FT                   /id="PRO_0000080766"
FT   DOMAIN          65..160
FT                   /note="SH2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          358..452
FT                   /note="SH2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   MOD_RES         341
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64143"
SQ   SEQUENCE   461 AA;  54388 MW;  C5B77282B9A96DAD CRC64;
     MYNTVWSIDR DDADWREVMM PYSTELIFYI EMDPPALPPK PPKPMTSAIT NGIKDSSVSL
     QDAEWYWGDI SREEVNDKLR DMPDGTFLVR DASTKMQGDY TLTLRKGGNN KLIKIYHRDG
     KYGFSDPLTF NSVVELISHY HHESLAQYNP KLDVKLMYPV SRYQQDQLVK EDNIDAVGKK
     LQEYHSQYQE KSKEYDRLYE EYTRTSQEIQ MKRTAIEAFN ETIKIFEEQC HTQEQHSKEY
     IERFRKEGNE KEIERIMMNY DKLKSRLGEI HDSKMRLEQD LKKQALDNRE IDKKMNSIKP
     DLIRLRKIRD QHLVWLNHKG VRQKRLNAWL GIKNEDADET YFINEEDENL PHYDEKTWFV
     EDINRVQAED LLYGKPDGAF LIRESSKKGC YACSVVADGE VKHCVIYSTA RGYGFAEPYN
     LYGSLKELVL HYQRTSLVQH NDSLNVRLAY PVHAQMPTLC R
 
 
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