ID A0A287DCB8_ICTTR Unreviewed; 724 AA.
AC A0A287DCB8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=PIK3R1 {ECO:0000313|Ensembl:ENSSTOP00000031217.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000031217.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000031217.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; AGTP01013973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01013974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005319599.1; XM_005319542.2.
DR RefSeq; XP_013211556.1; XM_013356102.1.
DR STRING; 43179.ENSSTOP00000026032; -.
DR Ensembl; ENSSTOT00000037431.1; ENSSTOP00000031217.1; ENSSTOG00000005560.3.
DR Ensembl; ENSSTOT00000039721.1; ENSSTOP00000026032.1; ENSSTOG00000005560.3.
DR GeneID; 101962360; -.
DR CTD; 5295; -.
DR eggNOG; KOG4637; Eukaryota.
DR GeneTree; ENSGT00940000155553; -.
DR OMA; EMIDVQV; -.
DR OrthoDB; 2880119at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:Ensembl.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:Ensembl.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; IEA:Ensembl.
DR GO; GO:0043559; F:insulin binding; IEA:Ensembl.
DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; IEA:Ensembl.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
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}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 3..79
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 113..301
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 333..428
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 624..718
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 79..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..562
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 83756 MW; 488D0CAB8B509086 CRC64;
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLLAH GFSDGQEARP EDIGWLNGYN
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG SSKTEADNEQ QALTLPDLAE
QFAPPDIAPP LLIKLVEAIE KKGLECSTLY RTQSSSNPAE LRQLLDCDAA SLDLEMIDVQ
VLADAFKRYL LDLPNPVIPV AVYSEMISLA QEVQSSEDYT QLLKKLIRSP NIPHQYWLTL
QYLLKHFFKL SQTSSKNFLN ARVLSEIFSP MLFRFPAASS DNTEHFIKVI EILISTEWNE
RQPAPALPPK PPKPTTAANN SMNNNISLQD AEWYWGEISR EEVNEKLRDT ADGTFLVRDA
STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL
DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEEY TRTSQEIQMK
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRIMHNYDK LKSRISEIID
SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS
VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA
QQRR
//
