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Database: UniProt
Entry: A0A3Q2FHU9_CYPVA
LinkDB: A0A3Q2FHU9_CYPVA
Original site: A0A3Q2FHU9_CYPVA 
ID   A0A3Q2FHU9_CYPVA        Unreviewed;       984 AA.
AC   A0A3Q2FHU9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma {ECO:0000313|Ensembl:ENSCVAP00000003615.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000003615.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000003615.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   AlphaFoldDB; A0A3Q2FHU9; -.
DR   STRING; 28743.ENSCVAP00000003615; -.
DR   Ensembl; ENSCVAT00000009730.1; ENSCVAP00000003615.1; ENSCVAG00000004821.1.
DR   GeneTree; ENSGT00940000159982; -.
DR   OMA; FTPGRKM; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR015433; PI_Kinase.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
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; PF00613; PI3Ka; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 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   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..206
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          202..378
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          447..725
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          864..979
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   984 AA;  112626 MW;  EAC0ADFB2D25146F CRC64;
     MIMLNGALLK VLQIYFDNFQ SDFRSQSLIG RPETRDVDDN EEILQFSIVS LYKLNPSWMN
     YESFSVSCDL TYGETKICET GVSENISTAL SHGNNISCNR LMVFPVRVNE LPYECMLTFH
     LKGTKRGKIS ESLSWAVLPL YNNRTLVGGT VLLSMSTLAE LPFPPSPALS DSHRQPTGVI
     LQLEFEEQYE WEYQRPIALP ESITFTQPCD EVQSKMLNVS KKHCICFLKE TERSFLWSKR
     DCADKTNTFL HLLLSGVPRW QPEDLTEIYT VVDKWLIHLP EEALFLLTPS FPDETVRKAA
     VNYFGEIPDG EFEMFLPQLV QALKSEWKLD GPLVMLLLER SLKNIRIAQQ LYWLLEETNT
     DCYFHSWFNK VKAALLHCCG QALRKELDYE ARLVQVLVQV AQKVRFADKS QRKNVLNREK
     ERIHEFFRGG ITCRLPLDPA FSVKGVDLDA CKFYSANSSP LGVTFVCEDS LAKKTSVICK
     VGDNLRQDML VLQIVRVMDW VWLQEGLDLQ MITYRCLSTG KDQGLVEVVP EAVTLGKIHQ
     EWGLSGTLRE DTLEKWFHML NKTKEGYEKA VTNFIQSCAG WCVVTFILGI CDRHNDNIML
     KHSGHMFHID FGRIMGNAQK FGTFRRDRKP FVFTSEMQHL ITGGGKKPQR LHRFVELCCE
     AYNIIRSRSA LILGMLELML SAGMPELKDI SDLEFVQNKL KPHDTDLEAT SYFTKKIKEC
     MDCFAVKFNF FTHTLAQPKK QQSITQNNIP AANSNIQGAV IEGFNVKGRV VTYSLKITID
     DGILTSQKTF RQFEMIHNSL QTYFIESKLP QFPGWYKMSF TPQRRKALLN TYLKELFKGP
     CKGDEYVCSL FLDGPKVEKN VTGGAPQIQL HISYSNAKLS VLVKHLQNIK LPNGSNPDAY
     VVTRLRPDPQ QTSKRKTKVV SNNDHPTFNE LLEYNHVPVL YGMVLEVTVK SRKAKKTFVA
     ATNIKLEDEV LDKEVWFPLG NCVI
//
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