ID A0A3B3ULG2_9TELE Unreviewed; 1600 AA.
AC A0A3B3ULG2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta {ECO:0000313|Ensembl:ENSPLAP00000014205.1};
GN Name=PIK3C2B {ECO:0000313|Ensembl:ENSPLAP00000014205.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000014205.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000014205.1}
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 RefSeq; XP_014873690.1; XM_015018204.1.
DR Ensembl; ENSPLAT00000022427.1; ENSPLAP00000014205.1; ENSPLAG00000017932.1.
DR GeneID; 106936945; -.
DR KEGG; plai:106936945; -.
DR CTD; 5287; -.
DR GeneTree; ENSGT00940000158263; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000261500; Unplaced.
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 Gene3D; 3.10.20.770; -; 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; 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; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 343..431
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 595..755
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 774..950
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1019..1297
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1332..1448
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1469..1589
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 47..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1600 AA; 178922 MW; 6C1F7EED09898224 CRC64;
MSAAQTQTQK EGSEAGWGAL EALGLSQREL VLAEALQMEY DALSRLKQDK TGTGTGSALP
EPGVPSQTGL KTPDPSMPGQ NRPTSSEELL LDLSGPDSSP NQPGGSHFPL PLPPRPAPPT
GVFMKETPYI LDGPELRKFS GSGSGDSVGP GLGFLSKGSA LPDDVPPAVP PRHPLPPPSG
SELPLLPPRP STRDVNLFQP GGDQLKVTSA ELNYDLINDS LARLNEGRPA PPARRTNGDQ
LGKPVARSKT LPPQVPPRTY TPAAKSNKNQ RRVSADPVRL GSRTNGFGYE LFQVSEERDE
EVAAFCHMLD VLRSAYPSTN RSRNAGFVWS PSVGHDELHQ ALGVAVKVTV ACEAFREPLT
FTCDGSSTVD LLIYQTLCYT QDQLDHLDVD DYLLKVCGHE EFLSNSQTLA GLEFVQQCLK
FDWDIRLFLT KRSAVNTNLA RTKEDDDTPS SMNHCILLQE RPIKQTVTRE ALTLLLDTFH
NEAESFLLSE VELLLHVERL VQSVKALCSS LAAVETPDVT AALNQLPACP CRLQPKVLKD
ASVLSLRENR ESVVEKLTAA ILDLVELYCS TFNANFHTAA QSRSATAPVQ EAGLVTNVLS
FNVYAAHRIP ITWATSYEGF FLSCSLTHGG KELCAPQHTS KQAVSKYLFH LVVWDQRVCF
PVEITQLPRE SQLTVTLYAS PLPPPGGAEE KGKQRRSTEP LGWVTMPLFN FRHVLTCGRK
LLGLWPSTPG RSGNARTSSP NFSQPDSVIL QVDFPTSSFE VIFSTPPPAD FCPQYDFSRL
DTISQIRLQD VLQKKAFHWL TADDKRLLWE KKAFCQSESA ALPLVLASAP CWQWACLPEI
YALLRQWACL GYLDALGLLH ASFPDQELRR TAVQWMDSIS DPELLDFLPQ LVQALKYECY
LDSSLVRFLL RRAIGDIRIA HYLFWLLKDN LQDSQFSARY QHLLAALLCC VGRALRDEFD
RQCWLVSILT KVAQKVRDAT PSSRQSVLRE SLDEMKQFFL VNSCCRLPLN PALLVSGINI
QSCSFFNSNA VPLKLSFQNL DPRGDNINVI FKSGDDLRQD MLTLQMIRIM NKIWIQEGLD
MRMVIFKCFS TGRGRGMVEM IPHADTLRKI QVEHGVTGSF KDRTLADWLQ KHNPTDEQYD
KAVENFIYSC AGCCVATYIL GICDRHNDNI MLKTSGHMFH IDFGKFLGHA QMFGNIKRDR
APFVFTSDMA YVINGGDKPS SRFHEFVDLC CDAYNLIRKH THLFLNLLGL MLSCGIPELS
DLDDLKYVYD ALRPHESEAD ATTYFTRLIE SSLGSVATKL NFFIHNLAQM KFASSEDRPA
LSFAPRIHTA RSDGVIKNLY ICRHIRFANK GYAFVVKVER EAQQEVQLVQ RTFEEFQELH
SKLRLVFPSS KLPSFPSRFV IGRSRSEATA DRRKDELNGY VWHLIHAAPE VAQCDLVYTF
FHPLSRDERT AGGSSKPAEV LWSPAAGTEL GEVKLSISYK NDKLFIMVIH IRGLQPLQDG
TDPDPYVKLY LLPDPQKTGK RKTKAARRTC NPTYNEMLVY DRIPRGDLDQ RVIHLRVLSD
GSFWENTLLG ETFITLTRLV PGQHWVDWHR LGPTGSDSAH
//