ID F6VGH6_CALJA Unreviewed; 1481 AA.
AC F6VGH6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma {ECO:0000313|Ensembl:ENSCJAP00000013467.3};
GN Name=PIK3C2G {ECO:0000313|Ensembl:ENSCJAP00000013467.3};
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:ENSCJAP00000013467.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000013467.3}
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:ENSCJAP00000013467.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; 9483.ENSCJAP00000013467; -.
DR Ensembl; ENSCJAT00000014186.3; ENSCJAP00000013467.3; ENSCJAG00000007208.4.
DR eggNOG; KOG0905; Eukaryota.
DR GeneTree; ENSGT00940000159982; -.
DR HOGENOM; CLU_002191_2_0_1; -.
DR InParanoid; F6VGH6; -.
DR OMA; FTPGRKM; -.
DR TreeFam; TF102031; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
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 4-PHOSPHATE 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; 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; 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 519..667
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 682..858
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 927..1205
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1235..1347
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1364..1481
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1481 AA; 169796 MW; 9D3660565F712A82 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 HNIPETWVHS
YKAFSFTCWL TYAGKKLCQV RNCRNIPVKK LFFFLVNWNE TINFPLEIES LPRESMLTVK
LFGIACATNS ASLLAWSCLP LFPKEKSILG SMLFSMTFQS EPPMEMIAPG VWDVSQPSPV
TLQIDFPATG WEFMKPDSEE NRSNLEEPPK EHLNHIARLS KKQTPLLLSE EKKRYLWFYR
FYCNNENCSL ALVLGSAPGW DERTVSEIHT ILRSWTFSQP LEALGLLTSS FPDQEIRKVA
VQQLDNLLND ELLDYLPQLV QAVKFEWNLE SPLVQLLLHR SLQSIQVAHR LYWLLRDAEN
EAYFKSWYQK LLAALQVCAG KALSEEFSKE QKLIKILGDI AEKVKSASDH QRQEVLKKEM
GRLEEFFQDV TTCHLPLNPA LCIKGIDHDA CSYFTSNALP LKITFINANP MGKNISTIFK
AGDDLRQDML VLQIIQVMDN IWLQEGLDMQ MIIYRCLSTG KDQGMVQMVP DAVTLAKIHR
HSGLIGPLKE NTIKKWFSQH NHLKADYEKA LRNFFYSCAG WCVVTFILGV CDRHNDNIML
TKSGHMFHID FGKFLGHAQT FGGIKRDRAP FIFTSEMEYF ITEGGKNPQR FQDFVELCCR
AYNIIRKHSQ LLLNLLEMML YAGLPELSGI QDLKYVYNNL RPQDTDLEAT SHFTKKIKES
LECFPVKLNN LIHTLAQMTA MSPGKSTFPQ ESCLLSTTRS IQRAEILGFS KKSSNLYVIQ
VTHSSNETSL TEKSFDQFLK LHSQLQKQFA SLTLPEFPHW WHLHFTNSDH KRVRDLNHYM
EQILNGSYEV ANSDCVVSFF LSEAVQPTAE ESSLVYLGET FPDKKPKVQL VISYEGVKLT
ILVKHMKNIH LPDGSAPSAH VEFYLLPYPS EVRRRKTKSV PKCTDPTYNE IVVYDEVTEL
QGHVLMLIVK SKTVFVGAIN IQLCSVPLSE EKWYPLGNSI I
//