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P4KG6_ARATH
ID   P4KG6_ARATH             Reviewed;         622 AA.
AC   Q8W4R8; Q9LMY3;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Phosphatidylinositol 4-kinase gamma 6;
DE            Short=AtPI4Kgamma6;
DE            Short=PI-4Kgamma6;
DE            Short=PI4K gamma 6;
DE            EC=2.7.1.67;
GN   Name=PI4KG6; Synonyms=PI4KGAMMA6; OrderedLocusNames=At1g13640;
GN   ORFNames=F21F23.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12226484; DOI=10.1104/pp.004770;
RA   Mueller-Roeber B., Pical C.;
RT   "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT   putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT   specific phospholipase C.";
RL   Plant Physiol. 130:22-46(2002).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=17880284; DOI=10.1042/bj20070959;
RA   Galvao R.M., Kota U., Soderblom E.J., Goshe M.B., Boss W.F.;
RT   "Characterization of a new family of protein kinases from Arabidopsis
RT   containing phosphoinositide 3/4-kinase and ubiquitin-like domains.";
RL   Biochem. J. 409:117-127(2008).
CC   -!- FUNCTION: The phosphorylation of phosphatidylinositol (PI) to PI4P is
CC       the first committed step in the generation of phosphatidylinositol 4,5-
CC       bisphosphate (PIP2), a precursor of the second messenger inositol
CC       1,4,5-trisphosphate (InsP3). {ECO:0000250}.
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 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67;
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF81291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC027656; AAF81291.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE29053.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59920.1; -; Genomic_DNA.
DR   EMBL; AY060574; AAL31202.1; -; mRNA.
DR   EMBL; AY149944; AAN31098.1; -; mRNA.
DR   PIR; F86269; F86269.
DR   RefSeq; NP_001322238.1; NM_001332079.1.
DR   RefSeq; NP_563930.1; NM_101234.4.
DR   AlphaFoldDB; Q8W4R8; -.
DR   SMR; Q8W4R8; -.
DR   STRING; 3702.AT1G13640.1; -.
DR   iPTMnet; Q8W4R8; -.
DR   PaxDb; Q8W4R8; -.
DR   PRIDE; Q8W4R8; -.
DR   ProteomicsDB; 250814; -.
DR   EnsemblPlants; AT1G13640.1; AT1G13640.1; AT1G13640.
DR   EnsemblPlants; AT1G13640.2; AT1G13640.2; AT1G13640.
DR   GeneID; 837925; -.
DR   Gramene; AT1G13640.1; AT1G13640.1; AT1G13640.
DR   Gramene; AT1G13640.2; AT1G13640.2; AT1G13640.
DR   KEGG; ath:AT1G13640; -.
DR   Araport; AT1G13640; -.
DR   TAIR; locus:2023865; AT1G13640.
DR   eggNOG; KOG2381; Eukaryota.
DR   HOGENOM; CLU_027241_1_1_1; -.
DR   InParanoid; Q8W4R8; -.
DR   OMA; DNDGFTQ; -.
DR   OrthoDB; 1273723at2759; -.
DR   PhylomeDB; Q8W4R8; -.
DR   PRO; PR:Q8W4R8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8W4R8; baseline and differential.
DR   Genevisible; Q8W4R8; AT.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR044571; P4KG1-8.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45800; PTHR45800; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..622
FT                   /note="Phosphatidylinositol 4-kinase gamma 6"
FT                   /id="PRO_0000423363"
FT   DOMAIN          38..95
FT                   /note="Ubiquitin-like; degenerate"
FT   DOMAIN          158..459
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          164..170
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          310..318
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          339..365
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   BINDING         165..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   BINDING         277..280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   BINDING         341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT   MOD_RES         565
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C671"
SQ   SEQUENCE   622 AA;  69572 MW;  E62960FD1881256A CRC64;
     MAMAVFKAPL KGEFHGARKM EGKQYKHHLL QQQSTGRRRV FVQTDTGCVL GVELDRNDNV
     HTVKKRLQIA FNFPTEESSL TFGDMVLKND LSAVRNDSPL LLKRNLMHRS SSTPCLSPTG
     NDLQRKDRSG PIEILSHSPC FLSLKQTAND IVKAMKMGVE PIPVNGGLGG AYYFRDEKGQ
     SVAIVKPTDE EPFAPNNPKG FVGKALGQPG LKPSVRVGET GFREVAAYLL DYDHFANVPP
     TALVKITHSV FNVNDGMDGN KSREKKKLVS SKIASFQKFV PHDFDASDHG TSSFPVASVH
     RIGILDIRIL NTDRHGGNLL VKKLDDGGVG RFGQVELIPI DHGLCLPETL EDPYFEWIHW
     PQASIPFSEE ELDYIQSLDP VKDCEMLRRE LPMIREACLR VLVLCTVFLK EAAVFGLCLA
     EIGEMMTREF RAGEEEPSEL EMLCIEAKRL TTEQDVLSPK SDGEGETEFQ FDIDYNELDS
     VYGSETETDE FFAKNPFSNG RSSLGELKES IAEEEEDDEE EAKLTLSLSK LSTSMKNNLS
     NTMGSGYLKP PKDNQTDKAL VSHKSANVQL PLSVNFVKLA DMKEVEWVVF LERFQELLYS
     AFAERKTMTL RNTQRLGTSC KF
 
 
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