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Database: UniProt
Entry: A0A4W2C879_BOBOX
LinkDB: A0A4W2C879_BOBOX
Original site: A0A4W2C879_BOBOX 
ID   A0A4W2C879_BOBOX        Unreviewed;       724 AA.
AC   A0A4W2C879;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   18-JUN-2025, entry version 31.
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:ENSBIXP00000009051.1};
OS   Bos indicus x Bos taurus (Hybrid cattle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000009051.1, ECO:0000313|Proteomes:UP000314981};
RN   [1] {ECO:0000313|Proteomes:UP000314981, ECO:0000313|Proteomes:UP000429181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA   Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT   "Haplotype-resolved cattle genomes.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBIXP00000009051.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009442}.
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DR   RefSeq; XP_027376152.1; XM_027520351.1.
DR   RefSeq; XP_027376153.1; XM_027520352.1.
DR   STRING; 30522.A0A4W2C879; -.
DR   Ensembl; ENSBIXT00000017130.1; ENSBIXP00000009051.1; ENSBIXG00000014789.1.
DR   Ensembl; ENSBIXT00005045310.1; ENSBIXP00005034372.1; ENSBIXG00005015321.1.
DR   GeneID; 113879096; -.
DR   GeneTree; ENSGT00940000155553; -.
DR   OMA; EMIDVQV; -.
DR   Proteomes; UP000314981; Chromosome 20.
DR   Proteomes; UP000429181; Chromosome 20.
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:0035014; F:phosphatidylinositol 3-kinase regulator activity; 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:0042267; P:natural killer cell mediated cytotoxicity; 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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:TreeGrafter.
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:0061470; P:T follicular helper cell differentiation; 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   FunFam; 1.10.555.10:FF:000035; Phosphatidylinositol 3-kinase regulatory subunit alpha; 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:000014; Phosphatidylinositol 3-kinase regulatory subunit alpha; 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; 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: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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314981};
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..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..562
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        84..99
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  83497 MW;  EBDF6E754BBF7321 CRC64;
     MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEAKP EEIGWLNGYN
     ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG PSKTEADSEQ QASTLPDLAE
     QFAPPDVAPP LLIKLVEAIE KKGLECSTLY RTQSSSNPAE LRQLLDCDTA SLDLEMFDVH
     VLADAFKRYL LDLPNPVIPV AVSSELISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL
     QYLLKHFFKL SQTSSKNLLN ARVLSELFSP LLFRFPAASS ENTEHLIKII EILISTEWNE
     RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA
     STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL
     DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEDY TRTSQEIQMK
     RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNETE IQRIMHNYEK LKSRISEIVD
     SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
     ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS
     VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA
     QQRR
//
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