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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP1 (EC 2.7.4.21) (EC 2.7.4.24) (Probable protein QUANTITATIVE VITAMIN E-7) (Protein VIP HOMOLOG 2) (VIP1 homolog protein 1) (Arabidopsis homolog protein of yeast VIP1 1) (AtVIP1)

 VIP1L_ARATH             Reviewed;        1050 AA.
F4J8C6; Q0WSV1; Q9MAD6; Q9SRH8;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 55.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP1 {ECO:0000303|PubMed:25231822};
EC=2.7.4.21 {ECO:0000269|PubMed:25231822};
EC=2.7.4.24 {ECO:0000269|PubMed:25231822};
AltName: Full=Probable protein QUANTITATIVE VITAMIN E-7 {ECO:0000303|PubMed:17077148};
AltName: Full=Protein VIP HOMOLOG 2 {ECO:0000303|PubMed:25901085};
AltName: Full=VIP1 homolog protein 1 {ECO:0000303|PubMed:25231822};
Short=Arabidopsis homolog protein of yeast VIP1 1 {ECO:0000303|PubMed:25231822};
Short=AtVIP1 {ECO:0000303|PubMed:25231822};
Name=VIP1 {ECO:0000303|PubMed:25231822};
Synonyms=QVE7 {ECO:0000303|PubMed:17077148},
VIH2 {ECO:0000303|PubMed:25901085};
OrderedLocusNames=At3g01310 {ECO:0000312|Araport:AT3G01310};
ORFNames=T22N4.6 {ECO:0000312|EMBL:AAF03495.1},
T4P13.1 {ECO:0000312|EMBL:AAF26144.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-1050.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-1050.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
STRAIN=cv. Columbia, cv. Cvi-0, and cv. Landsberg erecta;
PubMed=17077148; DOI=10.1073/pnas.0606221103;
Gilliland L.U., Magallanes-Lundback M., Hemming C., Supplee A.,
Koornneef M., Bentsink L., Dellapenna D.;
"Genetic basis for natural variation in seed vitamin E levels in
Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 103:18834-18841(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[8]
FUNCTION, MUTAGENESIS OF ASP-292, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=25231822; DOI=10.1111/tpj.12669;
Desai M., Rangarajan P., Donahue J.L., Williams S.P., Land E.S.,
Mandal M.K., Phillippy B.Q., Perera I.Y., Raboy V., Gillaspy G.E.;
"Two inositol hexakisphosphate kinases drive inositol pyrophosphate
synthesis in plants.";
Plant J. 80:642-653(2014).
[9]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-219 AND ASP-292,
AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=25901085; DOI=10.1105/tpc.114.135160;
Laha D., Johnen P., Azevedo C., Dynowski M., Weiss M., Capolicchio S.,
Mao H., Iven T., Steenbergen M., Freyer M., Gaugler P.,
de Campos M.K., Zheng N., Feussner I., Jessen H.J., Van Wees S.C.,
Saiardi A., Schaaf G.;
"VIH2 regulates the synthesis of inositol pyrophosphate InsP8 and
jasmonate-dependent defenses in Arabidopsis.";
Plant Cell 27:1082-1097(2015).
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases to synthesize the diphosphate group-containing
inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-
InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4.
PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and
InsP8, may regulate a variety of cellular processes, including
apoptosis, vesicle trafficking, cytoskeletal dynamics, and
exocytosis. Phosphorylates inositol hexakisphosphate (InsP6) at
positions 1 or 3 to produce PP-InsP5 which is in turn
phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from
InsP6, to produce (PP)2-InsP4 (PubMed:25231822). Probably involved
in vitamin E homeostasis via the regulation of gamma-tocopherol
biosynthesis (PubMed:17077148). Catalyzes the conversion of InsP7
to InsP8. Regulates jasmonic acid (JA) perception and plant
defenses against herbivorous insects (e.g. P.rapae) and
necrotrophic fungi (e.g. M.brassicae, B.cinerea and
A.brassicicola) by triggering the production of jasmonate-induced
pools of InsP8 and subsequent activation of SCF(COI1) E3 ubiquitin
ligase complexes with JAZ proteins (e.g. TIFY10A/JAZ1)
(PubMed:25901085). {ECO:0000269|PubMed:17077148,
ECO:0000269|PubMed:25231822, ECO:0000269|PubMed:25901085}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
{ECO:0000269|PubMed:25231822}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:25231822}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:25231822}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
{ECO:0000269|PubMed:25231822}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O43314}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=Additional isoforms seem to exist.
{ECO:0000312|Araport:AT3G01310};
Name=1;
IsoId=F4J8C6-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Mostly expressed in vegetative tissues (e.g.
leaves and stems), and, to a lower extent, in roots, shoots and
reproductive tissues (e.g. flowers and siliques) (PubMed:25231822,
PubMed:25901085). Also present in mature pollen (PubMed:25901085).
{ECO:0000269|PubMed:25231822, ECO:0000269|PubMed:25901085}.
-!- DISRUPTION PHENOTYPE: Abnormal accumulation of InsP7 and reduced
levels of InsP8. Increased weight increase of P.rapae and
M.brassicae larvae feeded on mutant plants thus leading to a
reduced resistance. Increased susceptibility to the necrotrophic
fungi B.cinerea and A.brassicicola. Increased levels of jasmonic
acid (JA) and bioactive conjugates such as JA-Leu/Ile and JA-Val
upon mechanical wounding, but reduced induction of JA-responsive
genes in challenged mutant plants. {ECO:0000269|PubMed:25901085}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF03495.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAF26144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AC008261; AAF26144.1; ALT_SEQ; Genomic_DNA.
EMBL; AC010676; AAF03495.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE73636.1; -; Genomic_DNA.
EMBL; BT010149; AAQ22618.1; -; mRNA.
EMBL; AK227817; BAE99797.1; -; mRNA.
RefSeq; NP_001030614.1; NM_001035537.3. [F4J8C6-1]
UniGene; At.47813; -.
ProteinModelPortal; F4J8C6; -.
SMR; F4J8C6; -.
iPTMnet; F4J8C6; -.
PaxDb; F4J8C6; -.
EnsemblPlants; AT3G01310.2; AT3G01310.2; AT3G01310. [F4J8C6-1]
GeneID; 821297; -.
Gramene; AT3G01310.2; AT3G01310.2; AT3G01310.
KEGG; ath:AT3G01310; -.
Araport; AT3G01310; -.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
HOGENOM; HOG000177917; -.
KO; K13024; -.
Reactome; R-ATH-1855167; Synthesis of pyrophosphates in the cytosol.
PRO; PR:F4J8C6; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; F4J8C6; baseline and differential.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IMP:UniProtKB.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IMP:UniProtKB.
GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IMP:UniProtKB.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IMP:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; IMP:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:UniProtKB.
GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:UniProtKB.
GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:UniProtKB.
GO; GO:1900367; P:positive regulation of defense response to insect; IMP:UniProtKB.
GO; GO:1904966; P:positive regulation of vitamin E biosynthetic process; IMP:UniProtKB.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 4.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Jasmonic acid signaling pathway; Kinase;
Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
Transferase.
CHAIN 1 1050 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase VIP1.
/FTId=PRO_0000439498.
NP_BIND 208 211 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 217 219 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 292 294 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 23 24 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 183 184 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 297 300 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 355 429 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:O43314}.
BINDING 104 104 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 157 157 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 164 164 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 183 183 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 219 219 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 233 233 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 235 235 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 280 280 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MUTAGEN 219 219 K->A: Loss of activity.
{ECO:0000269|PubMed:25901085}.
MUTAGEN 292 292 D->A: Loss of activity.
{ECO:0000269|PubMed:25231822,
ECO:0000269|PubMed:25901085}.
CONFLICT 505 505 H -> F (in Ref. 4; BAE99797).
{ECO:0000305}.
SEQUENCE 1050 AA; 118924 MW; B45949B7E7053BA5 CRC64;
MEMEEGASGV GEKIKIGVCV MEKKVFSAPM GEILDRLQSF GEFEILHFGD KVILEDPIES
WPICDCLIAF HSSGYPLEKA QAYAALRKPF LVNELDPQYL LHDRRKVYEH LEMYGIPVPR
YACVNRKVPN QDLHYFVEEE DFVEVHGERF WKPFVEKPVN GDDHSIMIYY PSSAGGGMKE
LFRKIGNRSS EFHPDVRRVR REGSYIYEEF MATGGTDVKV YTVGPEYAHA EARKSPVVDG
VVMRNTDGKE VRYPVLLTPA EKQMAREVCI AFRQAVCGFD LLRSEGCSYV CDVNGWSFVK
NSYKYYDDAA CVLRKMCLDA KAPHLSSTLP PTLPWKVNEP VQSNEGLTRQ GSGIIGTFGQ
SEELRCVIAV VRHGDRTPKQ KVKLKVTEEK LLNLMLKYNG GKPRAETKLK SAVQLQDLLD
ATRMLVPRTR PGRESDSDAE DLEHAEKLRQ VKAVLEEGGH FSGIYRKVQL KPLKWVKIPK
SDGDGEEERP VEALMVLKYG GVLTHAGRKQ AEELGRYFRN NMYPGEGTGL LRLHSTYRHD
LKIYSSDEGR VQMSAAAFAK GLLDLEGQLT PILVSLVSKD SSMLDGLDNA SIEMEAAKAR
LNEIVTSGTK MIDDDQVSSE DFPWMTDGAG LPPNAHELLR ELVKLTKNVT EQVRLLAMDE
DENLTEPYDI IPPYDQAKAL GKTNIDSDRI ASGLPCGSEG FLLMFARWIK LARDLYNERK
DRFDITQIPD VYDSCKYDLL HNSHLDLKGL DELFKVAQLL ADGVIPNEYG INPQQKLKIG
SKIARRLMGK ILIDLRNTRE EALSVAELKE SQEQVLSLSA SQREDRNSQP KLFINSDELR
RPGTGDKDED DDKETKYRLD PKYANVKTPE RHVRTRLYFT SESHIHSLMN VLRYCNLDES
LLGEESLICQ NALERLCKTK ELDYMSYIVL RLFENTEVSL EDPKRFRIEL TFSRGADLSP
LRNNDDEAET LLREHTLPIM GPERLQEVGS CLSLETMEKM VRPFAMPAED FPPASTPVGF
SGYFSKSAAV LERLVNLFHN YKNSSSNGRS


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EIAAB45359 hGMH1,Homo sapiens,HSD23,HSD-23,Human,PDLs22,Periodontal ligament-specific protein 22,Protein GMH1 homolog,Protein unc-50 homolog,UNC50,UNCL,Uncoordinated-like protein
E1707m Mouse ELISA Kit FOR Probable protein kinase-like protein SgK071 homolog 96T
26-947 VPS4A is a member of the AAA protein family (ATPases associated with diverse cellular activities), and is the homolog of the yeast Vps4 protein. In humans, two paralogs of the yeast protein have been 0.05 mg
EIAAB11547 DnaJ homolog subfamily B member 4,DNAJB4,DNAJW,Heat shock 40 kDa protein 1 homolog,Heat shock protein 40 homolog,HLJ1,Homo sapiens,HSP40 homolog,Human,Human liver DnaJ-like protein


 

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