P85AA_XENLA
ID P85AA_XENLA Reviewed; 722 AA.
AC Q8UUU2;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha;
DE Short=PI3-kinase regulatory subunit alpha;
DE Short=PI3K regulatory subunit alpha;
DE Short=PtdIns-3-kinase regulatory subunit alpha;
DE AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha;
DE Short=PI3-kinase subunit p85-alpha;
DE Short=PtdIns-3-kinase regulatory subunit p85-alpha;
GN Name=pik3r1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAL68953.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Al-Khalili O.K., Eaton D.C.;
RT "Molecular cloning of Xenopus laevis phosphoinositide-3-kinase (regulatory
RT subunit, polypeptide 1, P85 alpha).";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to activated (phosphorylated) protein-Tyr kinases,
CC through its SH2 domain, and acts as an adapter, mediating the
CC association of the p110 catalytic unit to the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a p110 (catalytic) and a p85 (regulatory)
CC subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000250|UniProtKB:P27986}.
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DR EMBL; AY062922; AAL68953.1; -; mRNA.
DR RefSeq; NP_001083940.1; NM_001090471.1.
DR AlphaFoldDB; Q8UUU2; -.
DR SMR; Q8UUU2; -.
DR GeneID; 399202; -.
DR KEGG; xla:399202; -.
DR CTD; 399202; -.
DR Xenbase; XB-GENE-6254212; pik3r1.S.
DR OrthoDB; 737926at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399202; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISS:UniProtKB.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR CDD; cd12924; iSH2_PIK3R1; 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; 1.10.555.10; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
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 Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..722
FT /note="Phosphatidylinositol 3-kinase regulatory subunit
FT alpha"
FT /id="PRO_0000080761"
FT DOMAIN 3..80
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 112..300
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 332..427
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 622..716
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 83129 MW; C2E9247C20B459C0 CRC64;
MSAEGYKYRA LYPYKKEREE DIDLRVGDTL SVSRATLLAL GCFAEGMEAR PEQIGWLNGC
NENTGQRGDF PGTYVEYLGR KRISPPTPKP RPPRPLPVAP GAARGEAEAQ AFTLPDLAEQ
FSPPDIGPPV LIKLIEAIEK KGLESATLYR SQSSSSLTEL RQILECDAAS VDFEQFDIAI
LSDALKRYFL DLPHPVIPAL MYSEMLSAAR ESISSDEYVQ LLRKIIRCAN VPQQYWLTLQ
YLLKHFFQLC QSSSKNLLSA KSLAEIFSPL LFRIQVSSSD SSEFSTQILE VLIASEWNEK
QAAPALPPKP SKSTAVTNNG TNHVMSLQDA EWYWGDISRE EVNEKLRDTT DGTFLVRDAS
TIMHGDYTLT LRKGGNNKLI KIFHRDGKYG FSDPLTFNSV VELITHYRNE SLAQYNPKLD
VKLLYPVSRF QQDQVVKEDS IDAVGKKLRE YNVQFEEKNQ EYDRLYEDYT RTSQEIQMKR
TAIEAFNETI KIFEEQCQTQ EKYSKEYIEK FRREGNEKEI QRLLHNYEKL KSRISEIVDS
KRRLEEDLKK QTAENREIDK RMNSIKPDLI QLRKTRDQYL MWLTQKGVRQ KKLNEWMGNE
NTEDQYSVVE EEDLPHQDER TWNVGNINRN QAENLLRGKR DGTFLVRESS KAGCFACSVM
AEGEVKHCVI NKTHTGFGFA EPYNLYSSLK ELVLHYQYTS LVQHNDSLNV TLAHPVYAQQ
RR
