ID A0A7L0KY53_9SYLV Unreviewed; 713 AA.
AC A0A7L0KY53;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma {ECO:0000256|ARBA:ARBA00071518};
DE AltName: Full=p55PIK {ECO:0000256|ARBA:ARBA00082483};
DE Flags: Fragment;
GN Name=Pik3r1_0 {ECO:0000313|EMBL:NXK61441.1};
GN ORFNames=SYLVIR_R07184 {ECO:0000313|EMBL:NXK61441.1};
OS Sylvietta virens (Green crombec).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Sylvietta.
OX NCBI_TaxID=208069 {ECO:0000313|EMBL:NXK61441.1, ECO:0000313|Proteomes:UP000567822};
RN [1] {ECO:0000313|EMBL:NXK61441.1, ECO:0000313|Proteomes:UP000567822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-009-59 {ECO:0000313|EMBL:NXK61441.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXK61441.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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 {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:NXK61441.1}.
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DR EMBL; VXAN01000068; NXK61441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0KY53; -.
DR Proteomes; UP000567822; Unassembled WGS sequence.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 2.30.30.40:FF:000075; phosphatidylinositol 3-kinase regulatory subunit alpha; 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; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00678; PI3KINASEP85.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:NXK61441.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000567822};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:NXK61441.1}.
FT DOMAIN 2..77
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 109..314
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 320..415
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 613..707
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..463
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 288..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXK61441.1"
FT NON_TER 713
FT /evidence="ECO:0000313|EMBL:NXK61441.1"
SQ SEQUENCE 713 AA; 81368 MW; CB3C54FCBBE6ABD2 CRC64;
SSDGLQYRAL YEYQKDREED LALCPGDVLT VSRAALLSSP GYKDGDERNP QGWLHGVNER
TKERGDFPGT YVEYLGPARI AATAAKARPR PLPLPPAGTP TPWGLPGQAE LTEHPALPEQ
ALPTVARLIE ALEKQAPSSV PEGKNDWLRV PPVSLLQDAS AVDMDLYEAQ TLADALKWYL
QELPTPLIPP ALYSDLVHMA QETPGLEECG QRARALLAPP ALPQPQALLL RQLARHFCHL
CQGSHRSRLS PRLLGELFGE LLLRPYMQGC EAGTGIASHP DFEAASPSSP PSKAPPKPMT
PVNTNGIKDN SSFSLQEAEW YWGDISREEV NDKLRDMPDG TFLVRDASTK MQGDYTLTLR
KGGNNKLIKI YHRDGKYGFS DPLTFNSVVE LINHYRNESL AQYNPKLDVK LMYPVSRYQQ
DQLVKEDNID AVGKKLQEYH AQYQEKSKEY DKLYEEYTRT SQEIQMKRTA IEAFNETIKI
FEEQCHSQER YSKEYIERFR REGNDKEIER IMMNYEKLKS RLGEIHDSKM RLEQDLKKQA
LDNRETDKKM NSIKPDLIQL RKIRDQYLVW LNHKGVRQKR INDWLGIKNE NIDDTYFVNE
EDENLPHHDE KTWFVGDLNR IQAEDLLCGK PDGAFLIRES SKKGCYACSV VADGEVKHCV
IYSTPRGYGF AEPYNLYSTL KDLVLHYQQT SLVQHNDSLN VRLAYPVYAQ MPP
//
