ID A0A3P9C1S7_9CICH Unreviewed; 1727 AA.
AC A0A3P9C1S7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha {ECO:0000313|Ensembl:ENSMZEP00005016059.1};
GN Name=PIK3C2A {ECO:0000313|Ensembl:ENSMZEP00005016059.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005016059.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005016059.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005016059.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; 106582.ENSMZEP00005016059; -.
DR Ensembl; ENSMZET00005016572.1; ENSMZEP00005016059.1; ENSMZEG00005012057.1.
DR GeneTree; ENSGT00940000157813; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000265160; LG7.
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; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd05176; PI3Kc_C2_alpha; 1.
DR Gene3D; 3.10.20.770; -; 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; IPR037705; PI3K-C2-alpha_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:SF28; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT ALPHA; 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; SM00144; PI3K_rbd; 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:UP000265160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 450..540
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 719..895
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 899..1076
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1144..1422
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1461..1577
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1600..1719
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 192519 MW; 4C95A7D218384440 CRC64;
MAQISSGNGF KLDVPQPKGV VGKEEALRME EEALAKLQRE KKHTLTATAS SSSSGAASSS
SSKPKPSKST TTVPQPSTYT NRPDKDLIVF PETKKQAEQD TFRDIDVEKL TNEELEKLLL
DENFGANSSK VSRPSSLLGF NLSASYPGGH ACSSSPFQSS QWTPALSNPS SSGVSTPTLQ
PTPMFPSAPF PKPGTFQNGF TPAMTPFMAL PTMAFTPIQP AAAMVFPQPT VDPEMAKLFD
KIASTSEYLK NGRLASTDVN SSQAGIASLA PNPPPQQPAV MESSSISRFE WLDLDPLTKR
KSENEEAPLE SVDSSQTVSG ASAGDPWDAV LETKGNSSNS SSSPKLEGRV SHTGRSQHRR
ASTGAPVARS HSLNIPETSS QHKTINQEKG KGNALVKNDA LEEQDAQNLE IVAFCEDIAS
LRSKFPHDDI ATNPGFVLSP VITQRNGGGD NSCSVKVSIE ISDSQQPVTF TCDVSSPVEL
LISQTLCWVH DDLDKVDFSS YLLKVCGREE VLQNKHSLGS HEYVQNCRKW ENEITLQLLS
HSTMRRDLAR TAEDDKSTIN LEKHLGLVER PFKENVTRQG LADYLEGYHN QVNICLQNES
TQYKTVDRLV QTVKNMCCAL DEVETQAITE AVKRLRHSVN LPRTRSPMMG LTSSGQSSNG
LTSPVEESMA LLTQAIYDLA KLYLRSFSSP SSSFHSPPLP QVTDGDAVEV KRSKEASGTT
DHLQFTLFAL HGIPANWVSS YEKYFLVCSL THNGKNLFKP VQSKRVGTYK SFFYHIKWDE
LINFPIAVAV LPLESILSLA LFGVLNQNAS GSPDSNKQRK APELLGKVSM PLFDFRRVLA
RGTRLLCLWT SAQGAAAAAS SAGSRKRVPT ERIVLQVNFP NSPVDVLYVG PKEAPSPEPH
TLEELDPDLR RKLEKICSRA SNFGLKRADH QLLWDHRLHC RRDHPSSLPK VLASAPSWDW
ASMAHIHSLL HHWPTLPPVT ALELLDSKFA DTEVRSVAVS WIEKSSDDQL ADYLPQLVQA
IKFECHLKNA LVMFLLSRAQ GNINIAHYLY WLLKDAVQDS TWGPRYERVL GVLLCLCGAR
LRAELEKQTH LVTLLGAVAE RVRQAGGSTR QVALQEGLEN IQNFFQRNSC RLPLSPSLVA
KELNIKACSF FNSNAVPLKL ALVNADPLGE EINVMFKVGD DLRQDMLTLQ MIRIMDRIWL
QEGLDLRIVN FKCISTGKDK GMVELVPSSD TLRKIQVEYG VTGSFKDKPL AEWLRKYNPA
EDEYEKASEN FIYSCAGCCV ATYVLGICDR HNDNIMLRST GHMFHIDFGK FLGHAQMFGS
FKRDRAPFVL TSDMAYVING GERPTSRFQL FVDLCCQAYN LIRKNSGLFL NLLSLMMSSG
LPELTGSQDL KYVFDALQPH NTDAEATIFF TRLIESSLGS VATKFNFFIH NLAQLRFSGL
PANDEPILSF SPKTYTLKQE GRIVHASIFS FQKRYNPDKH YIYVVRLLRE GQNEPQFVFR
TFDEFQELHN KLTILFPLWK LPSFPSKMVL GRSQIKEVAA KRKLELNNYV HNLMRSSTEV
TQCDLIYTFF HPIARDDKTE GVDAMAKAPE PPLSPTSGRV EGEVKLSISY RNSTLFIMVM
HIRDLVSEDG TDPNPYVKTY LLPDPHKTSK RKTKISRKTR NPTFNEMLVY SGYSKETLGL
RELQLSVLSA ESLRENYFLG GITLRLKDFD LSNETVKWYK LTAVPYF
//
