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ITPK4_ORYSJ
ID   ITPK4_ORYSJ             Reviewed;         355 AA.
AC   Q6K7B8; Q0E1B2;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Inositol-tetrakisphosphate 1-kinase 4 {ECO:0000305};
DE            EC=2.7.1.134 {ECO:0000305};
DE   AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 4 {ECO:0000305};
DE            Short=Inositol-triphosphate 5/6-kinase 4 {ECO:0000305};
DE            Short=Ins(1,3,4)P(3) 5/6-kinase 4 {ECO:0000305};
DE            Short=OsITP5/6K-4 {ECO:0000303|PubMed:17961936};
DE            Short=OsITPK4 {ECO:0000303|PubMed:22038091};
DE            EC=2.7.1.159 {ECO:0000305};
GN   Name=ITPK4;
GN   OrderedLocusNames=Os02g0466400 {ECO:0000312|EMBL:BAF08726.1},
GN   LOC_Os02g26720 {ECO:0000305};
GN   ORFNames=OJ1342_D02.13 {ECO:0000312|EMBL:BAD19564.1},
GN   OsJ_06663 {ECO:0000312|EMBL:EAZ22973.1};
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
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   [6]
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   [7]
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=BAF08726.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP004850; BAD19564.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08726.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000139; EAZ22973.1; -; Genomic_DNA.
DR   EMBL; AK071209; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q6K7B8; -.
DR   SMR; Q6K7B8; -.
DR   STRING; 4530.OS02T0466400-01; -.
DR   PaxDb; Q6K7B8; -.
DR   PRIDE; Q6K7B8; -.
DR   eggNOG; ENOG502QQS1; Eukaryota.
DR   HOGENOM; CLU_041857_0_0_1; -.
DR   InParanoid; Q6K7B8; -.
DR   PlantReactome; R-OSA-1119434; Phytic acid biosynthesis (lipid-independent).
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6K7B8; 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   InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR   InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR   InterPro; IPR041429; ITPK1_N.
DR   PANTHER; PTHR14217; PTHR14217; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   Pfam; PF17927; Ins134_P3_kin_N; 1.
DR   PIRSF; PIRSF038186; ITPK; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..355
FT                   /note="Inositol-tetrakisphosphate 1-kinase 4"
FT                   /id="PRO_0000431875"
FT   DOMAIN          107..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          225..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         157
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         179..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         190
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         291
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   CONFLICT        72
FT                   /note="R -> H (in Ref. 5; AK071209)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   355 AA;  38497 MW;  2C2E4E7F30632DC7 CRC64;
     MAPELSSPSS SPRYTVGYAL LPEKVSSVVR PSLVALAADR GVRLVAVDVS RPLAEQGPFD
     LLVHKMYDRG WRAQLEELAA RHPGVTVVVD SPGAIDRLLD RATMLDVVSG LRTPVSVPPQ
     VVVSDAAADA DELLARAALR FPLIAKPLAV DGSAESHDMR LVYRRDGVLP LLRAPLVLQE
     FVNHGGVLFK VYVVGDRATC VRRSSLPDVP ARRLLDLDAE PSVPFANISN QPLPPPDDDG
     GAADDDTPAA GFVDEVARGL RRGLGLHLFN FDMIRERSEE HGDRYFIIDI NYFPGYAKMP
     GYEAALTDFF LEMLRGTRPV PEQLGPGSGL DMEARKLEPG LGIGLRELES GRAQA
 
 
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