ID A0A3Q7T8Q9_VULVU Unreviewed; 1264 AA.
AC A0A3Q7T8Q9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma isoform X3 {ECO:0000313|RefSeq:XP_025851370.1};
GN Name=PIK3C2G {ECO:0000313|RefSeq:XP_025851370.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025851370.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025851370.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025851370.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025851370.1};
RG RefSeq;
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 RefSeq; XP_025851370.1; XM_025995585.1.
DR AlphaFoldDB; A0A3Q7T8Q9; -.
DR Proteomes; UP000286640; Unplaced.
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; 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 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:UP000286640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 63..149
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 299..447
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 462..638
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 707..985
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1018..1130
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1143..1264
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1264 AA; 145596 MW; 1E52C2AE1FAC6024 CRC64;
MAKEYRGCSS QLVEVPQGTN KDLASFCNKV KKIREMYHAA DINSNSGKIW STTTAFPYQL
FSNTKFNINI CIDNSTQLLH FMPNANYLVK DLIAEILHFC TNDQLFPKDH LLSVCGYEEF
LQNDYSLGSH KIFQKDKSVI QLNLQKNGEV PGKLSRKHED DHSQFYLKQL LEFMHIWKVS
RQCLSTVIKK YDFHLKCLLK TQQHVDNIIE DVKNICSVLG CVETKQITDA VNELNQILQR
KTENFHQNSE TSAKGLIERV TTALSRSIYQ LISVYCCSFY ADFQPLNVPN DISYVNPGLH
SHLSFTVYAV HNIPETWVHS YKAFSFSCCL TYAGKKLCQV RSYRNIPFKK LFFLLINWNE
TINFPLEIKS LPRESMLTIR LFGIVCATNN ANLLAWTCLP LFPKDKSILG SVLFSMTLQN
EPPIEMIVPG VWDISQPSSV ILQIDFPATE LEYMKFDSEE NRSNLEEPPK ECLKHIARLS
QKQSPLLLSE EKKRYLWFYR FYCNNENCSL PLVLGSAPGW DERTVSEIHI ILRRWQFSCP
LEALGLLTSS FPDQEIRKVA VRQLDNLLND ELLEYLPQLV QAVKFEWNLE SPLVQLLLHR
SLQSIQIAHR LYWLLKDAQN ETYFKSWYQK LLAALQFCSG KALSDEFSKE KKLIKILGDI
GEKVKSASDP QRQEVLKKEI GRLEEFFQCV KTCHLPLNPA LCIKGIDRDA CSYFTSHALP
LKITFINANP MGKNISIIFK AGDDLRQDML VLQIIQVMDN IWLQEGLDMQ MIIYRCLSTG
KGQGLVQMVP DAITLAKIHR HSGLIGPLKE NTIKKWFSQH NHLKADYEKA LRNFFYSCAG
WCVVTFILGV CDRHNDNIML TKSGHMFHID FGKFLGHAQT FGGIKRDRAP FIFTSEMEYF
ITEGGKNPQH FQDFVELCCQ AYNIVRRHSR LLLNLLEMML HAGLPELGGI QDLKYVYNNL
RPQDTDLEAT SHFTKKIKES LECFPVKLNN LIHTLAQMTS INPAKSASQN FSQEFCMLNA
TRSIQRATIL GFSKKTSHLY LIQVTHSNNE TSLTEKSFDQ FSKLHSELQK QFASLTLPEF
PHWWHLPFTN SNHKRFRDLN HYMEQILNGS YEVANSDYVL SFFLSEPVQQ TIEESSLLDL
GEKFPDKTPK VQLVISHEDA KLTILVKHMK NIHLPDGSAP SAHVEFYLLP YPSEVRRRKT
KSVPKCTDPT YNEIVVYNEV TELRGHVLML IVKSKTVFVG AINIQLYSVP LNEEKWYPLG
NCII
//
