ID A0A093FKG9_TYTAL Unreviewed; 723 AA.
AC A0A093FKG9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha {ECO:0000256|ARBA:ARBA00013911};
DE AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha {ECO:0000256|ARBA:ARBA00031433};
GN ORFNames=N341_06416 {ECO:0000313|EMBL:KFV54784.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV54784.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV54784.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV54784.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; KK391138; KFV54784.1; -; Genomic_DNA.
DR RefSeq; XP_009967785.1; XM_009969483.1.
DR AlphaFoldDB; A0A093FKG9; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd12924; iSH2_PIK3R1; 1.
DR CDD; cd04388; RhoGAP_p85; 1.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR CDD; cd11910; SH3_PI3K_p85alpha; 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; IPR044124; ISH2_PIK3R1.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035591; PI3K_p85alpha_SH3.
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:SF10; PI3K21B, ISOFORM B; 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:KFV54784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
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:KFV54784.1}.
FT DOMAIN 3..79
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 112..300
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 332..427
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 623..717
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 80..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 83473 MW; 77B069CAAC21A6D1 CRC64;
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGTLLAL GFSEGEEAKP EEIGWLNGFN
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPS PVKVEAESEQ AFSLPDLTEQ
FAPPDVAPPI LIKIVETIEK KGLECSTLYG TQGSSSSAEL RQILECDASS LDLETFDVHT
LSDALKRYLL DLPNPIIPAA VYSDMVSVAQ EVQSAEEYAQ LLKKLIRSPN IPPQYWVTLQ
YLLKHFLRVC QASSKNLLNA RSLAEIFSPL LFKFQIASSD NTEHHVKILE VLITSEWNER
QPLPALPPKP PKPNTVTNNG MNNNMSLQDA EWYWGDISRE EVNEKLRDTA DGTFLVRDAS
TKMHGDYTLT LRKGGNNKLI KIFHRDGKYG FSDPLTFNSV VELINHYRNE SLAQYNPKLD
VKLLYPVSKY QQDQVVKEDS IEAVGKKLHE YNTQFQEKSR EYDRLYEDYT RTSQEIQMKR
TAIEAFNETI KIFEEQCQTQ ERYSKEYIEK FKREGNEKEI QRIMHNYEKL KSRISEIVDS
RRRLEEDLKK QAAEYREIDK RMNSIKPDLI QLRKTRDQYL MWLTQKGVRQ KKLNEWLGNE
NAEDQYSMVE DDEDLPHHDE RTWNVGNINR SQAENLLRGK RDGTFLVRES SKQGCYACSV
VVDGEVKHCV INKTPTGYGF AEPYNLYNSL KELVLHYQHT SLVQHNDSLN VTLAYPVYAQ
QRR
//
