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Database: UniProt
Entry: F6VGH6_CALJA
LinkDB: F6VGH6_CALJA
Original site: F6VGH6_CALJA 
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
//
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