VIP2L_ARATH
ID VIP2L_ARATH Reviewed; 1049 AA.
AC Q84WW3; F4K8B7; Q93YV1; Q9LFP8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP2 {ECO:0000303|PubMed:25231822};
DE EC=2.7.4.24 {ECO:0000269|PubMed:25231822};
DE AltName: Full=Protein VIP HOMOLOG 1 {ECO:0000303|PubMed:25901085};
DE AltName: Full=VIP1 homolog protein 2 {ECO:0000303|PubMed:25231822};
DE Short=Arabidopsis homolog protein of yeast VIP1 2 {ECO:0000303|PubMed:25231822};
DE Short=AtVIP2 {ECO:0000303|PubMed:25231822};
GN Name=VIP2 {ECO:0000303|PubMed:25231822};
GN Synonyms=VIH1 {ECO:0000303|PubMed:25901085};
GN OrderedLocusNames=At5g15070 {ECO:0000312|Araport:AT5G15070};
GN ORFNames=F2G14.190 {ECO:0000312|EMBL:CAC01826.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
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 FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25231822; DOI=10.1111/tpj.12669;
RA Desai M., Rangarajan P., Donahue J.L., Williams S.P., Land E.S.,
RA Mandal M.K., Phillippy B.Q., Perera I.Y., Raboy V., Gillaspy G.E.;
RT "Two inositol hexakisphosphate kinases drive inositol pyrophosphate
RT synthesis in plants.";
RL Plant J. 80:642-653(2014).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-218 AND ASP-291, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25901085; DOI=10.1105/tpc.114.135160;
RA Laha D., Johnen P., Azevedo C., Dynowski M., Weiss M., Capolicchio S.,
RA Mao H., Iven T., Steenbergen M., Freyer M., Gaugler P., de Campos M.K.,
RA Zheng N., Feussner I., Jessen H.J., Van Wees S.C., Saiardi A., Schaaf G.;
RT "VIH2 regulates the synthesis of inositol pyrophosphate InsP8 and
RT jasmonate-dependent defenses in Arabidopsis.";
RL Plant Cell 27:1082-1097(2015).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in
CC turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
CC phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to
CC produce (PP)2-InsP4 (PubMed:25231822). Probably involved in vitamin E
CC homeostasis via the regulation of gamma-tocopherol biosynthesis (By
CC similarity). {ECO:0000250|UniProtKB:F4J8C6,
CC ECO:0000269|PubMed:25231822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000269|PubMed:25231822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000305|PubMed:25231822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000269|PubMed:25231822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000305|PubMed:25231822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O43314}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84WW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84WW3-2; Sequence=VSP_058854;
CC -!- TISSUE SPECIFICITY: Mostly expressed at low levels in roots and
CC reproductive tissues (e.g. flowers and siliques), and, to a lower
CC extent, in vegetative tissues (e.g. roots, shoots, leaves and stems)
CC (PubMed:25231822). Also present in mature pollen (PubMed:25231822,
CC PubMed:25901085). {ECO:0000269|PubMed:25231822,
CC ECO:0000269|PubMed:25901085}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391146; CAC01826.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92112.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92113.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68985.1; -; Genomic_DNA.
DR EMBL; AY059756; AAL24104.1; -; mRNA.
DR EMBL; BT001922; AAN71921.1; -; mRNA.
DR PIR; T51452; T51452.
DR RefSeq; NP_001190313.1; NM_001203384.1. [Q84WW3-2]
DR RefSeq; NP_001330695.1; NM_001343385.1. [Q84WW3-1]
DR RefSeq; NP_568308.1; NM_121511.2. [Q84WW3-1]
DR AlphaFoldDB; Q84WW3; -.
DR SMR; Q84WW3; -.
DR STRING; 3702.AT5G15070.2; -.
DR iPTMnet; Q84WW3; -.
DR PRIDE; Q84WW3; -.
DR EnsemblPlants; AT5G15070.1; AT5G15070.1; AT5G15070. [Q84WW3-1]
DR EnsemblPlants; AT5G15070.2; AT5G15070.2; AT5G15070. [Q84WW3-2]
DR EnsemblPlants; AT5G15070.4; AT5G15070.4; AT5G15070. [Q84WW3-1]
DR GeneID; 831359; -.
DR Gramene; AT5G15070.1; AT5G15070.1; AT5G15070. [Q84WW3-1]
DR Gramene; AT5G15070.2; AT5G15070.2; AT5G15070. [Q84WW3-2]
DR Gramene; AT5G15070.4; AT5G15070.4; AT5G15070. [Q84WW3-1]
DR KEGG; ath:AT5G15070; -.
DR Araport; AT5G15070; -.
DR TAIR; locus:2147890; AT5G15070.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_0_1; -.
DR OMA; YLAHIVI; -.
DR OrthoDB; 93740at2759; -.
DR PhylomeDB; Q84WW3; -.
DR BioCyc; ARA:AT5G15070-MON; -.
DR PRO; PR:Q84WW3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84WW3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IMP:UniProtKB.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IMP:UniProtKB.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IMP:TAIR.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006020; P:inositol metabolic process; IMP:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1904966; P:positive regulation of vitamin E biosynthetic process; ISS:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; PTHR12750; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1049
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase VIP2"
FT /id="PRO_0000439499"
FT REGION 354..428
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT REGION 835..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22..23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 207..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 216..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 291..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 296..299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:F4J8C6"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4J8C6"
FT VAR_SEQ 937
FT /note="E -> ETLKHKNYCLQ (in isoform 2)"
FT /id="VSP_058854"
FT MUTAGEN 218
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25901085"
FT MUTAGEN 291
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25901085"
FT CONFLICT 290
FT /note="C -> F (in Ref. 3; AAL24104)"
FT /evidence="ECO:0000305"
SQ 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
