ID   P70304_MOUSE            Unreviewed;       724 AA.
AC   P70304;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 143.
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|MGI:MGI:97583};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAC52847.1};
RN   [1] {ECO:0000313|EMBL:AAC52847.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AAC52847.1};
RX   PubMed=8921377; DOI=10.1006/geno.1996.0527;
RA   Fruman D.A., Cantley L.C., Carpenter C.L.;
RT   "Structural organization and alternative splicing of the murine
RT   phosphoinositide 3-kinase p85 alpha gene.";
RL   Genomics 37:113-121(1996).
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009442}.
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DR   EMBL; U50413; AAC52847.1; -; mRNA.
DR   PIR; A38747; A38747.
DR   AlphaFoldDB; P70304; -.
DR   SMR; P70304; -.
DR   DIP; DIP-118N; -.
DR   IntAct; P70304; 2.
DR   MINT; P70304; -.
DR   AGR; MGI:97583; -.
DR   MGI; MGI:97583; Pik3r1.
DR   ChiTaRS; Pik3r1; mouse.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; 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.
DR   Genevisible; P70304; MM.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAC52847.1};
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};
KW   Transferase {ECO:0000313|EMBL:AAC52847.1}.
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          80..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..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;  83501 MW;  BCC21211D46F1C17 CRC64;
     MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP EDIGWLNGYN
     ETTGERGDFP GTYVEYIGRK RISPPTPKPR PPRPLPVAPG SSKTEADTEQ QALPLPDLAE
     QFAPPDVAPP LLIKLLEAIE KKGLECSTLY RTQSSSNPAE LRQLLDCDAA SVDLEMIDVH
     VLADAFKRYL ADLPNPVIPV AVYNEMMSLA QELQSPEDCI QLLKKLIRLP NIPHQCWLTL
     QYLLKHFFKL SQASSKNLLN ARVLSEIFSP VLFRFPAASS DNTEHLIKAI EILISTEWNE
     RQPAPALPPK PPKPTTVANN SMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA
     STKMHGDYTL TPRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL
     DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEEY TRTSQEIQMK
     RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRIMHNHDK LKSRISEIID
     SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
     ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS
     VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA
     QQRR
//