ID   P55G_RAT                Reviewed;         461 AA.
AC   Q63789;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 134.
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 55 kDa regulatory subunit gamma;
DE            Short=PI3-kinase subunit p55-gamma;
DE            Short=PtdIns-3-kinase regulatory subunit p55-gamma;
DE   AltName: Full=p55PIK;
GN   Name=Pik3r3;
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 [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=8621382; DOI=10.1074/jbc.271.10.5317;
RA   Inukai K., Anai M., van Breda E., Hosaka T., Katagiri H., Funaki M.,
RA   Fukushima Y., Ogihara T., Yazaki Y., Kikuchi M., Oka Y., Asano T.;
RT   "A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase
RT   structurally similar to p55PIK is generated by alternative splicing of the
RT   p85alpha gene.";
RL   J. Biol. Chem. 271:5317-5320(1996).
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; D64047; BAA10927.1; -; mRNA.
DR   RefSeq; NP_071549.1; NM_022213.1.
DR   AlphaFoldDB; Q63789; -.
DR   SMR; Q63789; -.
DR   STRING; 10116.ENSRNOP00000000157; -.
DR   iPTMnet; Q63789; -.
DR   PhosphoSitePlus; Q63789; -.
DR   PaxDb; 10116-ENSRNOP00000000157; -.
DR   GeneID; 60664; -.
DR   KEGG; rno:60664; -.
DR   UCSC; RGD:621042; rat.
DR   AGR; RGD:621042; -.
DR   CTD; 8503; -.
DR   RGD; 621042; Pik3r3.
DR   eggNOG; KOG4637; Eukaryota.
DR   InParanoid; Q63789; -.
DR   OrthoDB; 2880119at2759; -.
DR   PhylomeDB; Q63789; -.
DR   Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR   Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR   Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-RNO-388841; Costimulation by the CD28 family.
DR   Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-8853659; RET signaling.
DR   Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR   Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR   PRO; PR:Q63789; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; ISO:RGD.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IDA:RGD.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR   CDD; cd09930; SH2_cSH2_p85_like; 1.
DR   CDD; cd09942; SH2_nSH2_p85_like; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 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   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1.
DR   Pfam; PF16454; PI3K_P85_iSH2; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PRINTS; PR00678; PI3KINASEP85.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 2.
DR   SUPFAM; SSF55550; SH2 domain; 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_0000080769"
FT   DOMAIN          65..163
FT                   /note="SH2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          358..455
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;  54254 MW;  6467D88447CC562B CRC64;
     MYNTVWSMDR DDADWREVMM PYSTELIFYI EMDPPALPPK PPKPVTSAVT NGMKDCFVSL
     QDAEWYWGDI SREEVNDKLR DMPDGTFLVR DASTKMQGDY TLTLRKGGNN KLIKIYHRDG
     NYGFSEPLTF NSVVELINHY HHESLAQYNP KLDVKLMYPV SRYQQDQLVK EDNIDAVGKN
     LQEFHSQYQE KSKEYDRLYE EYTRTSQEIQ MKRTAIEAFN ETIKIFEEQC HTQEQHSKDY
     IERFRREGNE KEIERIMMNY DKLKSRLGEI HDSKVRLEQD LKKQALDNRE IDKKMNSIKP
     DLIQLRKIRD QHLVWLNHRG VRQRRLNAWL GIKSEDTDES YFINEDDESL PHYDEKTWFV
     EDVNRVQAED LLYGKPDGAF LIRESSKKGC YACSVVADGE VKPCVIYSPA RGYGFAEPYN
     LYGSLKELVL HYQQTSLVQH NDSLNVTLAY PVHAQMPSLC R
//