UniProt: A0A9L0S1U1

Database: UniProt
Entry: A0A9L0S1U1_HORSE

LinkDB:  A0A9L0S1U1_HORSE 
Original site:  A0A9L0S1U1_HORSE

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (31)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (7)   
   SMART (5)   
Literature (1)   
   PubMed (1)   
All databases (40)   

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ID   A0A9L0S1U1_HORSE        Unreviewed;      1053 AA.
AC   A0A9L0S1U1;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   18-JUN-2025, entry version 11.
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=PIK3CB {ECO:0000313|Ensembl:ENSECAP00000068852.1,
GN   ECO:0000313|VGNC:VGNC:21447};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000068852.1, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000068852.1, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000068852.1,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000068852.1}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000068852.1};
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC         3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2-
CC         (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC         inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137,
CC         ChEBI:CHEBI:83243, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00051347};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397;
CC         Evidence={ECO:0000256|ARBA:ARBA00051347};
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: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004805}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   Ensembl; ENSECAT00000082953.1; ENSECAP00000068852.1; ENSECAG00000023941.4.
DR   VGNC; VGNC:21447; PIK3CB.
DR   GeneTree; ENSGT00940000157522; -.
DR   Proteomes; UP000002281; Chromosome 16.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro.
DR   CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR   CDD; cd00872; PI3Ka_I; 1.
DR   CDD; cd05173; PI3Kc_IA_beta; 1.
DR   FunFam; 1.10.1070.11:FF:000001; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR   FunFam; 2.60.40.150:FF:000046; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR   FunFam; 3.30.1010.10:FF:000005; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta; 1.
DR   FunFam; 3.10.20.770:FF:000003; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform; 1.
DR   Gene3D; 3.10.20.770; -; 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; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR037702; PI3Kbeta_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF33; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT BETA 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..115
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          194..285
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          327..496
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          507..684
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          755..1036
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1053 AA;  121186 MW;  E51BF3BE19E6480A CRC64;
     MCFNFMMPPA MADSLDIWSV DSQIVSDGSI RVDFLLPTGI YIQLDVPREA PISYIKQMLW
     KQVCDYPMFN LLMEIDSYMF ACVNQTAVYE ELEDETRRLC DVRPFLPVLK LVTRSCDPGE
     KLDSKIGVLI GKGLHEFDAL KDPEVNEFRV KMRKFSEEKI QSLVGLSWMD WLQQTYPPEH
     EPSNLENLED KLYGGKLIVA VHFENCQDVF SFQVSPNMNP IKINELAIQK RLTIRGKEDE
     VSPCDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRTLPH FILVECCKIK KMYEQEMIAI
     EAAINRNSSN LPLPLPPKKT RVISHIWENN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG
     TELLCKTIVS SEISGKNDHI WNEPLEFDIN TCDLPRMARL CFAVYAVLDK VKTKKSTKTI
     NPSKYQTIRK SGKVHYPVAW VNTMVFDFKG QLRSGDVILH SWSSFPDELE EMLNPMGTVQ
     TNPYTENATA LHIKFPENKK QPYYYPPFDK SRGGKKFLAV LKEILDRDPL SQLCENEMDL
     IWTLRQDCRE NFPQSLPKLL LSIKWNKLED VAQLQALLQI WPKLPPREAL ELLDFNYPDQ
     YVREYAVNCL RQMSDEELSQ YLLQLVQVLK YEPFLDCALS RFLLERALAN RRIGQFLFWH
     LRSEVHIPAV SVQFGVILEA YCRGSVGHMK VLSKQVEALN KLKTLNSLIK LNAVKLNRAK
     GKEAMHTCLK QNAYREALSD LQSPLNPCVI LSELYVEKCK YMDSKMKPLW LVYTNKVFGE
     DSVGVIFKNG DDLRQDMLTL QMLRLMDLLW KEAGLDLRML PYGCLATGDR SGLIEVVSTS
     ETIADIQLNS SNVAAAAAFN KDALLNWLKE YNSGDDLDRA IEEFTLSCAG YCVASYVLGI
     GDRHSDNIMV KKTGQLFHID FGHILGNFKS KFGIKRERVP FILTYDFIHV IQQGKTGNTE
     KFGRFRQCCE DAYLILRRHG NLFITLFALM LTAGLPELTS VKDIQYLKDS LALGKSEEEA
     LKQFKQKFDE ALRESWTTKV NWMAHTVRKD YRS
//

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