ID A0A452SJU4_URSAM Unreviewed; 1638 AA.
AC A0A452SJU4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta {ECO:0000313|Ensembl:ENSUAMP00000032812.1};
GN Name=PIK3C2B {ECO:0000313|Ensembl:ENSUAMP00000032812.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000032812.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000032812.1}
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 STRING; 9643.ENSUAMP00000032812; -.
DR Ensembl; ENSUAMT00000036555.1; ENSUAMP00000032812.1; ENSUAMG00000024988.1.
DR GeneTree; ENSGT00940000158263; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:Ensembl.
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: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:UP000291022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 379..467
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 631..790
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 809..985
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1054..1332
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1369..1485
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1508..1628
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 87..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1638 AA; 185207 MW; 3571E6E0008A3DEB CRC64;
MSSTQGSGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEESRAK QNTDSSLISW
DEPVLDFYNK PAGRQKDLKL LRGLSGSDPT LNYNSLSPQE GLSNHSTSQG SQPGPDPWPK
GSLARDYLYI FDGSDEGLSL SPGDLGSGDI DSSSKKLSPP PLPPRVSIWD TPPLPPRKGS
PSSSKISQPN DVNTFSLVEH PPGKLLGRRI LEEEEELGGG GPGRLLGPVD YDGINDAITR
LNLKSTYDAE MLRDTTRGWK EGRGPLDFGG KDTPGKPVAR SKTMPPQVPP RTYASRYAHG
KNTTPGKNRR ISAAPVDLRR RAVANGHELF EVSEERDEEV AAFCHMLDVL RSGSDIQDYS
LTGYVWSAVT ASPEHLGDEV NLKVTVLCDS IQEPLTFTCN CSSTVDLLIH QTLCYTHDEL
RDVDVGNFVL KPCGLEEFLQ NKHALGSHEY IQYCRKFDID IRLQLMEQKA VRSDLARTVN
DDQSPSTLNY LVHLQERPVK QTISRQALDL LFDTYHNEVD AFLLADGDFP LKADRVVQSV
KAICNALAAV ETPEITSALN QLPPCPSRMQ PKIQKDPTVL AVRENREKVV EALTAAILDL
VELYGSTFDA DFQTAVHGSR KHDLVQEACQ FSGPLAFTVY ATHRIPITWA TSYEDFYLSC
SLSHGGKELC SPLYTRKAHF SKYLFHLIIW DQQICFPVQV NRLPRETLLC ATLYALPIPL
PGSSSEANKQ RRLPEALGWV TTPLFNFRQV LTCGRKLLGL WPATQENPSA RWSAPNFHQP
DSVILQIDFP TSAFDIKFTS PPGDKFSPRY VFGSLREEDQ RVLKNIMQKE SLYWLTDADK
KRLWEKRYYC HLEVSSLPLV LASAPSWEWA CLPDIYALLK QWTHMNHQDA LGLLHATFPD
QEVRRMAVQW IGSLSDAELL DYLPQLVQAL KYECYLDSPL VRFLLKRAVS DLRVTHYFFW
LLKDGLKDSQ FSIRYQYLLA ALLCCCGKGL REEFNRQCWL VNTLAKLAQQ VREAAPSARQ
GILRTGLEEV RQFFALIGSC RLPLSPSLLV KGIVPRDCSY FNSNAVPLKL SFQNVDPLGE
NIRVIFKCGD DLRQDMLTLQ MIRIMSKIWV QEGLDMRMVI FRCFATGRGR GMVEMIPNAE
TLRKIQVEHG VTGSFKDRPL ADWLQKHNPG EDEYEKAVEN FIYSCAGCCV ATYVLGICDR
HNDNIMLKTT GHMFHIDFGR FLGHAQMFGN IKRDRAPFVF TSDMAYVING GDKPSSRFHD
FVDLCCQAYN LIRKHTHLFL NLLGLMLSCG IPELSDLEDL KYVYDALRPQ DTEANATTYF
TRLIESSLGS VATKLNFFIH NLAQMKFTGS DDRLTLSFAP RTHTLKSSGR ISDVFLCRHE
KIFHPNKGYV YVVKVMRENA HEATYIQRTF EEFQELHNKL RLLFPSSQLP SFPSRFVIGR
SRGEAVAERR REELNRYIRH LTHDAPEVAE CDLVYTFFHP LPRDEKAAGA SPAPKSSDGS
WARPVGKVGG EVKLSISYKN NKLFIMVMHI RGLQLLQDGN DPDPYVKIYL LPDPQKTTKK
KTKVARKTCN PTYNEMLVYD GIPKGDLQQR ELQLSVLSEQ GFWENVLLGE VHIRLRELDL
AQEKTGWFAL GSRSHETL
//
