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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP2 (EC 2.7.4.21) (EC 2.7.4.24) (Protein VIP HOMOLOG 1) (VIP1 homolog protein 2) (Arabidopsis homolog protein of yeast VIP1 2) (AtVIP2)

 VIP2L_ARATH             Reviewed;        1049 AA.
Q84WW3; F4K8B7; Q93YV1; Q9LFP8;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 99.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP2 {ECO:0000303|PubMed:25231822};
EC=2.7.4.21 {ECO:0000269|PubMed:25231822};
EC=2.7.4.24 {ECO:0000269|PubMed:25231822};
AltName: Full=Protein VIP HOMOLOG 1 {ECO:0000303|PubMed:25901085};
AltName: Full=VIP1 homolog protein 2 {ECO:0000303|PubMed:25231822};
Short=Arabidopsis homolog protein of yeast VIP1 2 {ECO:0000303|PubMed:25231822};
Short=AtVIP2 {ECO:0000303|PubMed:25231822};
Name=VIP2 {ECO:0000303|PubMed:25231822};
Synonyms=VIH1 {ECO:0000303|PubMed:25901085};
OrderedLocusNames=At5g15070 {ECO:0000312|Araport:AT5G15070};
ORFNames=F2G14.190 {ECO:0000312|EMBL:CAC01826.1};
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=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(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] (ISOFORM 1).
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]
FUNCTION, 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).
[5]
FUNCTION, MUTAGENESIS OF LYS-218 AND ASP-291, 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 (By similarity). {ECO:0000250|UniProtKB:F4J8C6,
ECO:0000269|PubMed:25231822}.
-!- 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=2;
Name=1;
IsoId=Q84WW3-1; Sequence=Displayed;
Name=2;
IsoId=Q84WW3-2; Sequence=VSP_058854;
Note=Derived from EST data. No experimental confirmation
available. {ECO:0000312|EMBL:AED92113.1};
-!- TISSUE SPECIFICITY: Mostly expressed at low levels in roots and
reproductive tissues (e.g. flowers and siliques), and, to a lower
extent, in vegetative tissues (e.g. roots, shoots, leaves and
stems) (PubMed:25231822). Also present in mature pollen
(PubMed:25231822, PubMed:25901085). {ECO:0000269|PubMed:25231822,
ECO:0000269|PubMed:25901085}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAC01826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL391146; CAC01826.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED92112.1; -; Genomic_DNA.
EMBL; CP002688; AED92113.1; -; Genomic_DNA.
EMBL; CP002688; ANM68985.1; -; Genomic_DNA.
EMBL; AY059756; AAL24104.1; -; mRNA.
EMBL; BT001922; AAN71921.1; -; mRNA.
PIR; T51452; T51452.
RefSeq; NP_001190313.1; NM_001203384.1. [Q84WW3-2]
RefSeq; NP_001330695.1; NM_001343385.1. [Q84WW3-1]
RefSeq; NP_568308.1; NM_121511.2. [Q84WW3-1]
UniGene; At.23566; -.
ProteinModelPortal; Q84WW3; -.
SMR; Q84WW3; -.
STRING; 3702.AT5G15070.2; -.
iPTMnet; Q84WW3; -.
PaxDb; Q84WW3; -.
EnsemblPlants; AT5G15070.1; AT5G15070.1; AT5G15070. [Q84WW3-1]
EnsemblPlants; AT5G15070.2; AT5G15070.2; AT5G15070. [Q84WW3-2]
EnsemblPlants; AT5G15070.4; AT5G15070.4; AT5G15070. [Q84WW3-1]
GeneID; 831359; -.
Gramene; AT5G15070.1; AT5G15070.1; AT5G15070.
Gramene; AT5G15070.2; AT5G15070.2; AT5G15070.
Gramene; AT5G15070.4; AT5G15070.4; AT5G15070.
KEGG; ath:AT5G15070; -.
Araport; AT5G15070; -.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
HOGENOM; HOG000177917; -.
KO; K13024; -.
OMA; DEHENLA; -.
OrthoDB; EOG093600TK; -.
BioCyc; ARA:AT5G15070-MONOMER; -.
Reactome; R-ATH-1855167; Synthesis of pyrophosphates in the cytosol.
PRO; PR:Q84WW3; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q84WW3; baseline and differential.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS: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; IGI:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; IMP:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:UniProtKB.
GO; GO:1904966; P:positive regulation of vitamin E biosynthetic process; ISS: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; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 1049 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase VIP2.
/FTId=PRO_0000439499.
NP_BIND 207 210 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 216 218 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 291 293 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 22 23 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 182 183 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 296 299 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 354 428 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:O43314}.
BINDING 103 103 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 156 156 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 163 163 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 182 182 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 218 218 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 232 232 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 234 234 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 279 279 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:F4J8C6}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000250|UniProtKB:F4J8C6}.
VAR_SEQ 937 937 E -> ETLKHKNYCLQ (in isoform 2).
/FTId=VSP_058854.
MUTAGEN 218 218 K->A: Loss of activity.
{ECO:0000269|PubMed:25901085}.
MUTAGEN 291 291 D->A: Loss of activity.
{ECO:0000269|PubMed:25901085}.
CONFLICT 290 290 C -> F (in Ref. 3; AAL24104).
{ECO:0000305}.
SEQUENCE 1049 AA; 118783 MW; 8F63A6291B137509 CRC64;
MGVEEGAGVD KKITIGVCVM EKKVFSAPMG QIMDRIHAFG EFEIIHFGDK VILEDPVESW
PICDCLIAFY SSGYPLEKVQ AYSSLRKPFL VNELDPQYLL HDRRKVYEHL EMYGIPVPRY
ACVNRKVPDE DLDYFVEEED FVEVKGERFW KPFVEKPVNG DDHSIMIYYP SSAGGGMKEL
FRKVGNRSSE FHPDVRRVRR EGSYIYEEFM PTGGTDVKVY TVGPEYAHAE ARKSPVVDGV
VMRNPDGKEV RYPVLLTPAE KQMAREVCIA FRQAVCGFDL LRSEGSSYVC DVNGWSFVKN
SYKYYDDAAC VLRKMFLDAK APHLSSTIPP ILPWKINEPV QSNEGLTRQG SGIIGTFGQS
EELRCVIAIV RHGDRTPKQK VKLKVTEEKL LNLMLKYNGG KPRAETKLKT AVQLQDLLDA
TRMLIPRARS GESDSDAEDL EHADKLRQVK AVLEEGGHFS GIYRKVQLKP LKWVNVPKSD
GEGEEERPVE ALMVLKYGGV LTHAGRKQAE ELGRYFRNNM YPGEGTGLLR LHSTYRHDLK
IYSSDEGRVQ MSAAAFAKGL LDLEGQLTPI LVSLVSKDSS MLDGLDNASS EMEAAKAQLN
EIITAGSKMV HDHVSSELPW MTDGAGLPPH ADEHLPELVK LAKKVTEQVR LLAQDEHENL
AEPSAYDVVP PYDQAKALGK SNIDVGRIAA GLPCGSEGFL LMFARWRKLE RDLYNERRER
FDITQIPDVY DSCKYDLLHN SHLDLKGLDE LFKVAQLLAD GVIPNEYGIN PQQKLKIGSK
IARRLLGKIL IDLRNTREEA MSVAELKNSQ DQVSVSLYSS RKEDRYSQPK LFVKSDELRR
PSTGENKEED DDKETKYRLD PKYANVMTPE RHVRTRLYFT SESHIHSLMN VLRYCNLDES
LQGEESLVCQ SALDRLCKTK ELDYMSYVVL RLFENTEISL DDPKRFRIEL TFSRGADLSP
LEKKDEEAES LLREHTLPIM GPERLQEVGS CLTLETMEKM IRPFAMPAED FPPPCTPAGF
SGYFSKSAAV LERLVKLWPF HKNTSNGKS


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