ID F6W0K3_CALJA Unreviewed; 1440 AA.
AC F6W0K3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma {ECO:0000313|Ensembl:ENSCJAP00000013459.4};
GN Name=PIK3C2G {ECO:0000313|Ensembl:ENSCJAP00000013459.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000013459.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000013459.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000013459.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSCJAT00000014178.4; ENSCJAP00000013459.4; ENSCJAG00000007208.4.
DR GeneTree; ENSGT00940000159982; -.
DR Proteomes; UP000008225; Chromosome 9.
DR Bgee; ENSCJAG00000007208; Expressed in liver and 1 other cell type or tissue.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
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; cd05177; PI3Kc_C2_gamma; 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; IPR037707; PI3K-C2-gamma_dom.
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:SF29; PHOSPHATIDYLINOSITOL 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT GAMMA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 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:UP000008225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 284..370
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 480..626
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 641..817
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 886..1164
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1194..1306
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1323..1440
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1440 AA; 164904 MW; 198ECB5AC45FE8A6 CRC64;
MAYSWQTDPN PNESHEKQYE HQEFLSVNQP HSSCQVSLGF DQIIDEISDK IPHKNEIDEN
TFSLPSVPEW DSRGHSLNKA HQISLNEFTS KSPEVSWHQL RRAPEIGFSP SVLPNPQNMN
KECPWGNPIG KHHGADDSRF NVLAPSFTSL DKINLQKELG SENHNYHIGF ESSISPTNST
FLTDFMRKEG NKRSGHMNIV EPSLMLSKGS LQPRMWESTW QENIESIGCS IQLVEVPQGS
NLSLASFCNK VKKIRERYHA ADINFNSGKI WSTTTAFPYQ LFSKTKFTIR IFTDNSTQPL
HLMPYANYLV KDLITEILHF CTNDQLLPKD HILNICGSEE FLQNDHCLGS HKMFQKDTSV
IQLHLQKSRE APGKLSRKRE DDHSQFYLNQ LLEFMHIWKV SRQCLLTLLR KYDFHLKNLL
KTQENVDIIE EVKKICSVLG CVETKQITDA ANELSLILQR KAENFYQSSE TSVKGLLEKA
TTELSTSIYQ LINVYCNSFY ADFQPVNVSR CISYLNPGLP SHLSFTVYAA HNIPETWVHR
INFPLEIESL PRESMLTVKL FGIACATNSA SLLAWSCLPL FPKEKSILGS MLFSMTFQSE
PPMEMIAPGV WDVSQPSPVT LQIDFPATGW EFMKPDSEEN RSNLEEPPKE HLNHIARLSK
KQTPLLLSEE KKRYLWFYRF YCNNENCSLA LVLGSAPGWD ERTVSEIHTI LRSWTFSQPL
EALGLLTSSF PDQEIRKVAV QQLDNLLNDE LLDYLPQLVQ AVKFEWNLES PLVQLLLHRS
LQSIQVAHRL YWLLRDAENE AYFKSWYQKL LAALQVCAGK ALSEEFSKEQ KLIKILGDIA
EKVKSASDHQ RQEVLKKEMG RLEEFFQDVT TCHLPLNPAL CIKGIDHDAC SYFTSNALPL
KITFINANPM GKNISTIFKA GDDLRQDMLV LQIIQVMDNI WLQEGLDMQM IIYRCLSTGK
DQGMVQMVPD AVTLAKIHRH SGLIGPLKEN TIKKWFSQHN HLKADYEKAL RNFFYSCAGW
CVVTFILGVC DRHNDNIMLT KSGHMFHIDF GKFLGHAQTF GGIKRDRAPF IFTSEMEYFI
TEGGKNPQRF QDFVELCCRA YNIIRKHSQL LLNLLEMMLY AGLPELSGIQ DLKYVYNNLR
PQDTDLEATS HFTKKIKESL ECFPVKLNNL IHTLAQMTAM SPGKSTFPQE SCLLSTTRSI
QRAEILGFSK KSSNLYVIQV THSSNETSLT EKSFDQFLKL HSQLQKQFAS LTLPEFPHWW
HLHFTNSDHK RVRDLNHYME QILNGSYEVA NSDCVVSFFL SEAVQPTAEE SSLVYLGETF
PDKKPKVQLV ISYEGVKLTI LVKHMKNIHL PDGSAPSAHV EFYLLPYPSE VRRRKTKSVP
KCTDPTYNEI VVYDEVTELQ GHVLMLIVKS KTVFVGAINI QLCSVPLSEE KWYPLGNSII
//
