ID Q4SWM8_TETNG Unreviewed; 1239 AA.
AC Q4SWM8;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=(spotted green pufferfish) hypothetical protein {ECO:0000313|EMBL:CAF94954.1};
DE Flags: Fragment;
GN ORFNames=GSTENG00011408001 {ECO:0000313|EMBL:CAF94954.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF94954.1};
RN [1] {ECO:0000313|EMBL:CAF94954.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAF94954.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAF94954.1}.
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DR EMBL; CAAE01013606; CAF94954.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4SWM8; -.
DR KEGG; tng:GSTEN00011408G001; -.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; 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:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 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 SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..69
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 401..577
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 661..939
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 972..1087
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1109..1230
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 245..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAF94954.1"
FT NON_TER 1239
FT /evidence="ECO:0000313|EMBL:CAF94954.1"
SQ SEQUENCE 1239 AA; 138637 MW; EB99F49B613B515E CRC64;
CTGSSTVDLL IYQTLCYALD DLDHLDVQEY LLKVCGYDEF LDHSQTLAAL ELVQQSLKFD
WNIRLFLIKK SKINTELART EEDDQTMSTM NHNILLQERP IKQTVTREAL SLLLDTFHIE
AESFLLSEAE LLLHVERLVQ SVKALCSSLA AVESPEVTAA LSQLPACPCR LQPRVLKDAS
VLAVRSNRER VVEKLTAAIL DLLELYCSTF NANFHTAQQS RRTTRPSRRR GSWPAWCPSI
FTLLTASPSP GQRDQPATQG VTADRDPLCQ RSAAPWWRGG EGEAAPQRGG SGLGDHAPLQ
LPTVGPPPPH RGSATAGATA ASSAVRHSHH SHVTCVCVCS VLTCGRKLLG LWPPTPGKTG
GARTSSPNFS QPDSVILQLD FPSSSFDVVF STPPPADFCP RYDFAALDTI SQIQLQDVLH
KKAVFWLTAD DRRLLWEKKS FCQSESSALP LVLASAPCWQ WSCLPEIYAL LRQWSCPRHL
DNLGLLHASF PDQEVRRMAV QWMDPMSHTE LLDVLPQLVQ ALKYECYLDS SLVRFLLRRA
MRDIRIAHYL FWLLKDNLQH SQFTARYHHL LAALLCCVGR GLREEFDRQC WLVSILANVA
HRVRDAAPSS RQVGPLTTLN RALKHSNCVL REALEEMSQF FSVNSSCRLP LNPALHVKGI
NIQLCSFFNS NAVPLKLSFQ NLDPLGDHIN VIFKSGDDLR QDMLTLQVIR IMNKIWIQEG
LDMRMVIFKC FSTGRGRGMV EMIPHADTLR KIQVEHGVTG SFRDRPLADW LQKHNPTEEQ
YDKAVENFIY SCAGCCVATY VLGICDRHND NIMLKSSGHM FHIDFGKFLG HAQMFGNIKR
DRAPFVFTSD MAYVINGGDK PSSRFHDFVD LCCEAYNLIR KHTHLFLNLL GLMLSCGIPE
LSDQEDLKYV YDALRPHESE ADATMYFTRR GPGGGGGGGR RGGGRCGGGG GGGGGARPSL
SFAPRLLAKS GGVISNLYVC RHISTANSSK GHAFVVKVQK DGHKEALFVQ RTFEEFNELH
SKLRLLFPAS KLPRFPNRLV IGRSSDATAD RRKDELNAYL WHLINSPPEV AQSDLVSTFF
HPLPRDERAA SSNSSKPPEV LWSAASGKEL GQVKLSISYK NDKLFIMVMH IRGLPSMQDG
TDPDPYVKLY LLPDPQKTSK RKTKAARRTC NPTYNEMLVY ERIPQGDLDQ RVIHLRVLGD
GAFWENTLLL GETFIPLKKL VPDQHWVDWH QLRAAGSGS
//
