ID C3ZMJ4_BRAFL Unreviewed; 1288 AA.
AC C3ZMJ4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN46204.1};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_233446 {ECO:0000313|EMBL:EEN46204.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN46204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN46204.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN46204.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 EMBL; GG666646; EEN46204.1; -; Genomic_DNA.
DR RefSeq; XP_002590193.1; XM_002590147.1.
DR STRING; 7739.C3ZMJ4; -.
DR eggNOG; KOG0905; Eukaryota.
DR InParanoid; C3ZMJ4; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
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; cd05166; PI3Kc_II; 1.
DR CDD; cd06883; PX_PI3K_C2; 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; 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:SF14; LD28067P; 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; 2.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 31..120
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 289..441
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 460..636
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 703..981
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1019..1135
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1159..1277
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN46204.1"
SQ SEQUENCE 1288 AA; 145538 MW; B787472C6A13D899 CRC64;
RLRTEYKHDH ATTNPGHLVS PILRYQHCRE DSTLKVVIHT LQQGSEPVTF TCDVETSVSH
LVSQAVVSLL DDDTDVSVDD FALKICGREE FLANDTTLGD YEYVQDCEKF DLDVALVLYP
RDAIPHRLAR TAEDDAKDTK TSNLNHFIDN PVRTAVSKRG LGVLVDAFYN EADKLRSHAS
LVRQFNGVVQ AIKALCATLA GLETVEVSKS VARLKRAVPA PRQHSIAGPE GLMSSEISRA
SMQRQDEVNL ALEEVTAAIL ALVDMYSSAF DTDFTTNPQG TPTAGMWAGD AIVLVRLVSA
HRLPINSHQL FEKFRVSSGV FHGGHRMCDT KQTNIRSMEN GFFPRLVWDE WVEFSLPLCL
LPREARLCVA LYGVNSGADS NRPYGVTVLG WAAIPLFNYR GHMLHGPHLL GLWPESKVNP
IGTCSSNLLQ PDSIILQVEF PTHGGDVVFP PPEPHYEGRQ YSYNVLDDST REQIQEIVAK
ASISKLSEEE EELLWEKRHY CHTVPAALPR VLKHAPSWDW ASLADIYSLV HNWSPLTPVS
ALELLHPHFA DKEVRATAIS WMQHLPDDEL YDFLPQLVQA LRYECYHDSA LARFLLERSL
ASVRIAQQLY WHLKDNVGDQ QFGQRFQMVL AGLLSTCGRA LRTEFEKQVQ LIRLLHDVAV
KVKSAKDSAR QAMLQHAMEK INNKMAVPFR LPTNPALVCS GINFQSCSYF TSNATPLRLV
FRNADSFGEE IQAMYKVGDD LRQDMLTLQM IRIMNKLWLR EGLDLRMITF ACVATGKEAG
MVEIIPKSET LRKIQTEQGV TGSFKDKPLA DWLQKHNATE ADYEKAVENF MFSCAGYCVA
TYVLGIGDRH NDNIMIKTTG HMFHIDFGKF LGNAQMFGKI KRDRAPFVLT SDMAYVINDG
DRPSTRFQDF VDLCCEAFNI IRKNANLFIN LFGLMLSSGI PALSRTEDIQ YVHNALKPSA
SDAEATAHFT RLIEVSLGSR ATQINFFMHN LAQMRFSGNV GDESLFTFSP KVYSMETDGR
IKSLSVFGFQ KRYSGEKYYV YIIKVYRQDR EEPTFVFRTY DELFELHQRL TLAFPHNRLP
SFPTRTVIGR SNIKQVAERR QVDLNIYLKE VMSAPPQVSQ SDLVYTFFHP MLRDEKDAGA
ANMLKIGDSS NRPPTIGQVG GSVKLSIHYK KNGLFIMVMH AKDLQSQDGE YPNPYVKTYL
LPDPAKLTKQ KTKIAKKSLN PTYNEMLVYN MPLADVQRRT LQLTVWSSES VRENCFLGGT
SIRLGELDLK QEAVQWYRLG DMVGDELM
//
