ID A0A5A9NTV4_9TELE Unreviewed; 464 AA.
AC A0A5A9NTV4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma {ECO:0000256|ARBA:ARBA00071518};
DE AltName: Full=p55PIK {ECO:0000256|ARBA:ARBA00082483};
GN ORFNames=E1301_Tti005105 {ECO:0000313|EMBL:KAA0712948.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0712948.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0712948.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0712948.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0712948.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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 {ECO:0000256|ARBA:ARBA00057933}.
CC -!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R3 and a p110
CC catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL.
CC {ECO:0000256|ARBA:ARBA00066175}.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0712948.1}.
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DR EMBL; SOYY01000013; KAA0712948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9NTV4; -.
DR Proteomes; UP000324632; Chromosome 13.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:TreeGrafter.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:TreeGrafter.
DR CDD; cd12925; iSH2_PIK3R3; 1.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR FunFam; 3.30.505.10:FF:000006; Phosphatidylinositol 3-kinase regulatory subunit alpha; 1.
DR FunFam; 3.30.505.10:FF:000017; Phosphatidylinositol 3-kinase regulatory subunit gamma b; 1.
DR FunFam; 1.10.287.1490:FF:000001; Putative phosphatidylinositol 3-kinase regulatory subunit alpha; 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:SF1; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT BETA; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000324632};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 67..162
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 360..454
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT COILED 176..203
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 464 AA; 54544 MW; 636C4D3D258832DD CRC64;
MYNTVWTTEK EDDDWRDVMM PYSSELIFYI EMDQPPALPP KPAKPMTPVN GNGVKEAASG
SLQDAEWYWG DISREEVNDK LRDMPDGTFL IRDASTKMQG DYTLTLRKGG NNKLIKIYHR
DGKYGFSDPL TFASVVELIS HYRHESLAQY NTKLDVKLMF PISRYQQDQL VKEDNIDAVG
RKLQEYHNQY QEKSKEYDRL YEEHTKTSQE IQMKRTAIEA FNETIKIFEE QCHTQERYSK
EYIERFRREG NDTEIERIMM NYEKLKSRLG EIHESKTRLE QDLKTQALDN RETDKKMNSL
KPDLIQLRKI RDQYLVWLNH KGVRQKRIND WLGIKNENTD EAYFVSEEDE NLPHYDEKSW
FVGDLNRTQA EDLLLGKPEG AFLIRESSKK GCYACSVVVD GEVKHCVIYS TPRGFGFAEP
YNLYSTLKDL VLHYHQTSLV QHNDSLNVRL AYPVYAKMPS GPRR
//
