ID A0A091DY72_FUKDA Unreviewed; 838 AA.
AC A0A091DY72;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=H920_10865 {ECO:0000313|EMBL:KFO27746.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27746.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27746.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27746.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN122864; KFO27746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DY72; -.
DR STRING; 885580.ENSFDAP00000020905; -.
DR eggNOG; KOG4637; Eukaryota.
DR Proteomes; UP000028990; 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: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; -; 2.
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; 2.
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:KFO27746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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:KFO27746.1}.
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 738..832
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 80..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 608..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 97776 MW; 42A8B5AB3835E21C CRC64;
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAH GFSDGQEARP EEIGWLNGYN
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG SSKTEADIEQ QALTLPDLAE
QFAPPDIAPP LLIRLVEAIE KKGLECATLY RTQSSSNSVE LRQLLDCDAA SVDLEMVDVQ
VLADACKRYL LDLPNPVIPV AVYSEMISLA QEVQSSEDYI QLLKKLIRSP NIPHQYWLTL
QYLLKHFFKL SQSSSKNLLS ARVLAEIFSP MLFRFPAASS DSTENLIKVI EILISTEWNE
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA
STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL
DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEEY TRTSQEIQMK
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRWVNHEHF FFFFFFFFIG
KKLHEYNTQF QEKSREYDRL YEEYTRTSQE IQMKRTAIEA FNETIKIFEE QCQTQERYSK
EYIEKFKREG NEKEIQRIMH NYDKLKSRIS EIIDSRRRLE EDLKKQAAEY REIDKRMNSI
KPDLIQLRKT RDQYLMWLTQ KGVRQKKLNE WLGNENTEEY LSVIADLKTE IAEVIANNFQ
YSLVEDDEDL PHHDEKTWNV GSSNRNKAEN LLRGKRDGTF LVRESSKQGC YACSVVVDGE
VKHCVINKTA TGYGFAEPYN LYSSLKELVL HYQHTSLVQH NDSLNVTLAY PVYAQQRR
//
