P55G_MOUSE
ID P55G_MOUSE Reviewed; 461 AA.
AC Q64143;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION
RP AT TYR-341.
RC TISSUE=Embryo;
RX PubMed=7542745; DOI=10.1128/mcb.15.8.4453;
RA Pons S., Asano T., Glasheen E., Miralpeix M., Zhang Y., Fisher T.L.,
RA Myers M.G. Jr., Sun X.J., White M.F.;
RT "The structure and function of p55PIK reveal a new regulatory subunit for
RT phosphatidylinositol 3-kinase.";
RL Mol. Cell. Biol. 15:4453-4465(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
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; S79169; AAB34938.1; -; mRNA.
DR EMBL; BC053102; AAH53102.1; -; mRNA.
DR CCDS; CCDS18509.1; -.
DR RefSeq; NP_853616.1; NM_181585.5.
DR RefSeq; XP_017175528.1; XM_017320039.1.
DR RefSeq; XP_017175529.1; XM_017320040.1.
DR AlphaFoldDB; Q64143; -.
DR SMR; Q64143; -.
DR BioGRID; 202164; 1.
DR IntAct; Q64143; 3.
DR MINT; Q64143; -.
DR STRING; 10090.ENSMUSP00000030464; -.
DR iPTMnet; Q64143; -.
DR PhosphoSitePlus; Q64143; -.
DR MaxQB; Q64143; -.
DR PaxDb; Q64143; -.
DR PRIDE; Q64143; -.
DR ProteomicsDB; 287755; -.
DR DNASU; 18710; -.
DR Ensembl; ENSMUST00000030464; ENSMUSP00000030464; ENSMUSG00000028698.
DR GeneID; 18710; -.
DR KEGG; mmu:18710; -.
DR UCSC; uc008ugm.1; mouse.
DR CTD; 8503; -.
DR MGI; MGI:109277; Pik3r3.
DR VEuPathDB; HostDB:ENSMUSG00000028698; -.
DR eggNOG; KOG4637; Eukaryota.
DR GeneTree; ENSGT00940000156259; -.
DR InParanoid; Q64143; -.
DR OMA; VRTCEDE; -.
DR OrthoDB; 737926at2759; -.
DR PhylomeDB; Q64143; -.
DR TreeFam; TF102033; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-388841; Costimulation by the CD28 family.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8853659; RET signaling.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR BioGRID-ORCS; 18710; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pik3r3; mouse.
DR PRO; PR:Q64143; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64143; protein.
DR Bgee; ENSMUSG00000028698; Expressed in cerebellar vermis and 219 other tissues.
DR ExpressionAtlas; Q64143; baseline and differential.
DR Genevisible; Q64143; MM.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IPI:MGI.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IDA:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
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 1: Evidence at protein level;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW SH2 domain.
FT CHAIN 1..461
FT /note="Phosphatidylinositol 3-kinase regulatory subunit
FT gamma"
FT /id="PRO_0000080768"
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:0000269|PubMed:7542745"
SQ SEQUENCE 461 AA; 54474 MW; 97A01A0DFAAC661F CRC64;
MYNTVWSMDR DDADWREVMM PYSTELIFYI EMDPPALPPK PPKPMTPAVT NGMKDSFISL
QDAEWYWGDI SREEVNDKLR DMPDGTFLVR DASTKMQGDY TLTLRKGGNN KLIKIYHRDG
KYGFSEPLTF TSVVELINHY HHESLAQYNP KLDVKLTYPV SRFQQDQLVK EDNIDAVGKN
LQEFHSQYQE KSKEYDRLYE EYTRTSQEIQ MKRTAIEAFN ETIKIFEEQC HTQEQHSKDY
IERFRREGNE KEIERIMMNY DKLKSRLGEI HDSKLRLEQD LKKQALDNRE IDKKMNSIKP
DLIQLRKIRD QHLVWLNHRG VRQRRLNAWL GIKNEDSDES YFINEEDENL PHYDEKTWFV
EDINRVQAED LLYGKPDGAF LIRESSKKGC YACSVVADGE VKHCVIYSTA RGYGFAEPYN
LYSSLKELVL HYQQTSLVQH NDSLNVRLAY PVHAQMPTLC R
