P55G_RAT
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 25-MAY-2022, entry version 128.
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; Q63789; -.
DR GeneID; 60664; -.
DR KEGG; rno:60664; -.
DR UCSC; RGD:621042; rat.
DR CTD; 8503; -.
DR RGD; 621042; Pik3r3.
DR eggNOG; KOG4637; Eukaryota.
DR InParanoid; Q63789; -.
DR OrthoDB; 737926at2759; -.
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-1266695; Interleukin-7 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: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 GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
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_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
