ID A0A452FLT1_CAPHI Unreviewed; 1634 AA.
AC A0A452FLT1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta {ECO:0000313|Ensembl:ENSCHIP00000025102.1};
GN Name=PIK3C2B {ECO:0000313|Ensembl:ENSCHIP00000025102.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000025102.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000025102.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000025102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; LWLT01000016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000032963.1; ENSCHIP00000025102.1; ENSCHIG00000021981.1.
DR GeneTree; ENSGT00940000158263; -.
DR Proteomes; UP000291000; Chromosome 16.
DR Bgee; ENSCHIG00000021981; Expressed in ileum and 16 other cell types or tissues.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR CDD; cd00895; PI3Kc_C2_beta; 1.
DR CDD; cd07290; PX_PI3K_C2_beta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042134; PX_PI3K_C2_beta.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..463
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 627..786
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 805..981
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1050..1328
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1365..1481
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1504..1624
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 76..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 184123 MW; 007CB566560A5C85 CRC64;
MSSTQGSGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEESRAK QNADPSLISW
DEPVLDVYSK PAARRKDLKL LRGLSGSDPT LNYNSVSPQE GLPNHSTSRG SQPGPDPWPK
GSLAEDYLYI FDGSDGGLSL SPGPRHREDS SKKLSPPPLP PRVSIWDTPP LPPRKGSPSS
SKVSQPSDIN TFSLVEQPPG KLLGPRILEE EEELGGGSPG RPLGSMDYDG INDAITRLNL
KSTYDAEMLR DATRGWKEGR GPLDFAKDTP GKPVARSKTM PPQVPPRTYA SRCANRKNAT
PGKNRRISAA PVGSRPHAVA NGHELFEVSE ERDEEVAAFC HMLDVLRSGS DVRDYSLTGY
VWSAVTPSPE HLGDEVNLKV TVLCDSLREP LTFTCNCSST VDLLIYQTLC YTRDELRDVD
VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC RKFGVDIRLQ LMEQKAVRGD LARTVNDDQS
PSTLNYLVHL QERPVKQTIS RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC
NALAAVETPE ITSALNQLPP CPSRMKPKIQ KVTGLARETR WREKVVEALT AAILDLVELY
CNTFNADFQT AAPGSRKHAL VQEACHLSGP LAFTVYATHR IPIVWATSYE EFYLSCSLSH
GGKELCSPLQ TRRVHFSKYL FHLVIWDQQI CFPVQLNRLP RETLLCATLY ALPVPPPGSS
SEANKQRRVP EALGWVTAPL FNFRQVLTCG RKLLGLWPAT QESPSARWSA PNFHQPDSVI
LQIDFPTSAF DIKFTSPAGD KFSPRYEFGS LREEDQHVLK SIVQKESLYW LTDADKKRLW
EKRYYCHAEV SALPLVLASA PSWEWACLPD TYALLAQWTP MSHQDALGLL HATFPDQEVR
RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV THYFFWLLKD
GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNTL AKLAQQVREA APSARQGILR
AGLEEVEQFF ALNGSCRLPL SPSLLVKGVV PRDCSYFNSN AVPLKLSFQN VDPLGENIRV
IFKCGDDLRQ DMLTLQMIRI MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNSETLRK
IQVEHGVTGS FKDRPLADWL QKHNPGEDAY EKAVENFIYS CAGCCVATYV LGICDRHNDN
IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP SSRFHDFVDL
CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY DALRPQDTEA NATTYFTRLI
ESSLGSVATK LNFFIHNLAQ MKFLGSDDRL TLSFAPRTHT LKSSGRISGV FLCRHEKVFH
PNKGYIYVVK VMRENAHEAT YIQRTFEEFQ ELHNKLRLLF PSSLLPSFPS RFVIGRSRGE
AGAERRREEL NGYIWHLVHA APEVAECDLV YTFFHPLPRD EKTAGSSLAP KSSEGTWARP
VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP QKTTKKKTKV
ARKTCNPTYN EMLVYDGIPK GDLRQRELQL SVLSEQGFWE NVLLGEVHIR LRELDLAQEK
TGWFALGSRS PETL
//
