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ITPK6_ORYSJ
ID   ITPK6_ORYSJ             Reviewed;         547 AA.
AC   Q0J0B2; A0A0P0XQ65; Q69IU4;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Inositol-tetrakisphosphate 1-kinase 6 {ECO:0000305};
DE            EC=2.7.1.134 {ECO:0000305};
DE   AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 6 {ECO:0000305};
DE            Short=Inositol-triphosphate 5/6-kinase 6 {ECO:0000305};
DE            Short=Ins(1,3,4)P(3) 5/6-kinase 6 {ECO:0000305};
DE            Short=OsITP5/6K-6 {ECO:0000303|PubMed:17961936};
DE            Short=OsITPK6 {ECO:0000303|PubMed:22038091};
DE            EC=2.7.1.159 {ECO:0000305};
GN   Name=ITPK6;
GN   OrderedLocusNames=Os09g0518700 {ECO:0000312|EMBL:BAF25603.1},
GN   LOC_Os09g34300 {ECO:0000305};
GN   ORFNames=OSJNOa211K08.2 {ECO:0000312|EMBL:BAD54694.1},
GN   P0498F03.7 {ECO:0000312|EMBL:BAD34407.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17961936; DOI=10.1016/j.gene.2007.09.006;
RA   Suzuki M., Tanaka K., Kuwano M., Yoshida K.T.;
RT   "Expression pattern of inositol phosphate-related enzymes in rice (Oryza
RT   sativa L.): implications for the phytic acid biosynthetic pathway.";
RL   Gene 405:55-64(2007).
RN   [6]
RP   INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=22038091; DOI=10.1007/s11103-011-9830-9;
RA   Du H., Liu L., You L., Yang M., He Y., Li X., Xiong L.;
RT   "Characterization of an inositol 1,3,4-trisphosphate 5/6-kinase gene that
RT   is essential for drought and salt stress responses in rice.";
RL   Plant Mol. Biol. 77:547-563(2011).
CC   -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate
CC       such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and participates in phytic acid
CC       biosynthesis in developing seeds. Phytic acid is the primary storage
CC       form of phosphorus in cereal grains and other plant seeds.
CC       {ECO:0000250|UniProtKB:Q84Y01}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC         inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC         EC=2.7.1.134; Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC         1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC         ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC         1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660,
CC         ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q13572};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000250|UniProtKB:Q13572};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q13572}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in embryos and at lower levels in
CC       roots, leaves, flowers and anthers. {ECO:0000269|PubMed:17961936}.
CC   -!- INDUCTION: By drought stress. {ECO:0000269|PubMed:22038091}.
CC   -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD34407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD54694.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP006525; BAD34407.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP007254; BAD54694.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008215; BAF25603.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT08993.1; -; Genomic_DNA.
DR   EMBL; AK102571; BAG95621.1; -; mRNA.
DR   AlphaFoldDB; Q0J0B2; -.
DR   SMR; Q0J0B2; -.
DR   STRING; 4530.OS09T0518700-01; -.
DR   PaxDb; Q0J0B2; -.
DR   PRIDE; Q0J0B2; -.
DR   EnsemblPlants; Os09t0518700-01; Os09t0518700-01; Os09g0518700.
DR   Gramene; Os09t0518700-01; Os09t0518700-01; Os09g0518700.
DR   eggNOG; ENOG502QQ6B; Eukaryota.
DR   InParanoid; Q0J0B2; -.
DR   OMA; KMAIVFR; -.
DR   BRENDA; 2.7.1.134; 8948.
DR   BRENDA; 2.7.1.159; 8948.
DR   PlantReactome; R-OSA-1119434; Phytic acid biosynthesis (lipid-independent).
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   ExpressionAtlas; Q0J0B2; baseline and differential.
DR   Genevisible; Q0J0B2; OS.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IBA:GO_Central.
DR   GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IBA:GO_Central.
DR   GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IEA:EnsemblPlants.
DR   InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR   InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR   PANTHER; PTHR14217; PTHR14217; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   PIRSF; PIRSF038163; ITPK_uncN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..547
FT                   /note="Inositol-tetrakisphosphate 1-kinase 6"
FT                   /id="PRO_0000431879"
FT   DOMAIN          327..539
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         263
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         317
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         381
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         404..415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         415
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         450
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         511
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         511
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         513
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         513
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         517
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
SQ   SEQUENCE   547 AA;  60800 MW;  4A40E1D4E0847C94 CRC64;
     MPSMRVTTDT WPRRAAQEPL LLLLLRSSLM KSASLQALNP NRAMAAMGRS VRVVLDSSVL
     LDPSGVTAEE EEVVVALRPG AEALLRRLRY SNLRVAICHP EGLPTNESGF LEKTAKLYSF
     GYMPLTSPSG SNLLNELMLE WSGTNFCFYV TSGVHEGLLS ELQNHNWEVI AMGNEDVIKN
     SGVIHISMLQ ELLITLATSI KKEIGNSSAF VVGYVMKQSR EEDFAKRGAF PIYPSKNDLI
     FVPLSFELPL ASQLQEVDLV LHKITDEIIN IDPNSSISFP KGISFSPGMS EIIRFVEEHC
     DFCVIDPFKN IYPLLDRIQI QEILIRLEGL SAEGRPKLRA PCFLKIESFC GSELQKQLAE
     AKLSFPLIVK PQVACGVADA HNMALIFKIE EFSNLSVPLP AILQEYIDHG SKIFKFYAIG
     DKIFHAIKNS MPNASHLKSS SGGKPLTFNS LKTLPVATKE QLLQNEVQDS KLLDINLVEE
     AAKLLKELLG LTIFGFDVVV QESSGDHVIV DLNYLPSFKE VPDNVAMPAF WDAIKQSYES
     RKQMTQT
 
 
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