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Database: UniProt
Entry: W5QHQ9_SHEEP
LinkDB: W5QHQ9_SHEEP
Original site: W5QHQ9_SHEEP 
ID   W5QHQ9_SHEEP            Unreviewed;      1069 AA.
AC   W5QHQ9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE            EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
GN   Name=PIK3CA {ECO:0000313|Ensembl:ENSOARP00000022259.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000022259.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000022259.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000022259.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000022259.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153;
CC         Evidence={ECO:0000256|ARBA:ARBA00023981};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293;
CC         Evidence={ECO:0000256|ARBA:ARBA00023981};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004805}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; AMGL01009508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5QHQ9; -.
DR   SMR; W5QHQ9; -.
DR   STRING; 9940.ENSOARP00000022259; -.
DR   PaxDb; 9940-ENSOARP00000022259; -.
DR   Ensembl; ENSOART00000022564.1; ENSOARP00000022259.1; ENSOARG00000020711.1.
DR   eggNOG; KOG0904; Eukaryota.
DR   HOGENOM; CLU_002191_1_1_1; -.
DR   OMA; WSEWLNY; -.
DR   UniPathway; UPA00220; -.
DR   Proteomes; UP000002356; Chromosome 1.
DR   Bgee; ENSOARG00000020711; Expressed in thymus and 54 other cell types or tissues.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR   GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR   CDD; cd00872; PI3Ka_I; 1.
DR   CDD; cd05175; PI3Kc_IA_alpha; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR003113; PI3K_ABD.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR037704; PI3Kalpha_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF107; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA ISOFORM; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF02192; PI3K_p85B; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00143; PI3K_p85B; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          17..106
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          188..290
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          331..488
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          518..695
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          766..1052
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1069 AA;  124429 MW;  AB251BA8369B8CA5 CRC64;
     TMPPRPSSGE LWGIHLMPPR ILVECLLPNG MIVTLECLRE ATLITIKHEL FKEARKYPLH
     QLLQDESSYI FVSVTQEAER EEFFDETRRL CDLRLFQPFL KVIEPVGNRE EKILNREIGF
     AIGMPVCEFD MVKDPEVQDF RRNILNVCKE AVDLRDLNSP HSRAMYVYPP NVESSPELPK
     HIYNKLDKGQ IIVVIWVIVS PNNDKQKYTL KINHDCVPEQ VIAEAIRKKT RSMLLSSEQL
     KLCVLEYQGK YILKVCGCDE YFLEKYPLSQ YKYIRSCIML GRMPNLMLMA KESLYSQLPM
     DCFTMPSYSR RISTATPYMN GETSTKSLWV INSALRIKIL CATYVNVNIR DIDKIYVRTG
     IYHGGEPLCD NVNTQRVPCS NPRWNEWLNY DIYIPDLPRA ARLCLSICSV KGRKGAKEEH
     CPLAWGNINL FDYTDTLVSG KMALNLWPVP HGLEDLLNPI GVTGSNPNKE TPCLELEFDW
     FSSVVKFPDM SVIEEHANWS VSREAGFSYS HAGLSNRLAR DNELRENDKE QLRAICTRDP
     LSEITEQEKD FLWSHRHYCV TIPEILPKLL LSVKWNSRDE VAQMYCLVKD WPPIKPEQAM
     ELLDCNYPDP MVRGFAVRCL EKYLTDDKLS QYLIQLVQVL KYEQYLDNLL VRFLLKKALT
     NQRIGHFFFW HLKSEMHNKT VSQRFGLLLE SYCRACGMYL KHLNRQVEAM EKLINLTDIL
     KQEKKDETQK VQMKFLVEQM RRPDFMDALQ GFLSPLNPAH QLGNLRLEEC RIMSSAKRPL
     WLNWENPDIM SELLFQNNEI IFKNGDDLRQ DMLTLQIIRI MENIWQNQGL DLRMLPYGCL
     SIGDCVGLIE VVRNSHTIMQ IQCKGGLKGA LQFNSHTLHQ WLKDKNKGEI YDAAIDLFTR
     SCAGYCVATF ILGIGDRHNS NIMVKDDGQL FHIDFGHFLD HKKKKFGYKR ERVPFVLTQD
     FLIVISKGAQ ECTKTREFER FQEMCYKAYL AIRQHANLFI NLFSMMLGSG MPELQSFDDI
     AYIRKTLALD KTEQEALEYF MKQMNDAHHG GWTTKMDWIF HTIKQHALN
//
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