VIP1_YEAST
ID VIP1_YEAST Reviewed; 1146 AA.
AC Q06685; D6VZ44;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE EC=2.7.4.24 {ECO:0000269|PubMed:17412958};
DE AltName: Full=InsP6 and PP-IP5 kinase;
GN Name=VIP1 {ECO:0000312|SGD:S000004402}; OrderedLocusNames=YLR410W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=10388810; DOI=10.1093/genetics/152.3.895;
RA Feoktistova A., McCollum D., Ohi R., Gould K.L.;
RT "Identification and characterization of Schizosaccharomyces pombe asp1(+),
RT a gene that interacts with mutations in the Arp2/3 complex and actin.";
RL Genetics 152:895-908(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-487 AND HIS-548.
RX PubMed=17412958; DOI=10.1126/science.1139099;
RA Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E.,
RA Haystead T.A., Ribeiro A.A., York J.D.;
RT "A conserved family of enzymes that phosphorylate inositol
RT hexakisphosphate.";
RL Science 316:106-109(2007).
RN [9]
RP FUNCTION.
RX PubMed=17412959; DOI=10.1126/science.1139080;
RA Lee Y.-S., Mulugu S., York J.D., O'Shea E.K.;
RT "Regulation of a cyclin-CDK-CDK inhibitor complex by inositol
RT pyrophosphates.";
RL Science 316:109-112(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-895 AND SER-1107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 (PubMed:17412958).
CC Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to
CC produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1,
CC produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity).
CC Required for maintaining cellular integrity, normal growth and
CC interactions with the ARP complex (PubMed:10388810). Acts as a
CC regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK)
CC complex, thereby regulating signaling of phosphate availability
CC (PubMed:17412959). Required for the function of the cortical actin
CC cytoskeleton, possibly by participating in correct F-actin localization
CC and ensuring polarized growth (PubMed:10388810). Regulates polarized
CC growth and modulates interphase microtubule cytoskeleton. Regulates
CC microtubule dynamics without the requirement of microtubule plus-end
CC tracking protein Mal3. Required for growth zone selection (By
CC similarity). {ECO:0000250|UniProtKB:O74429,
CC ECO:0000250|UniProtKB:Q6PFW1, ECO:0000269|PubMed:10388810,
CC ECO:0000269|PubMed:17412958, ECO:0000269|PubMed:17412959}.
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:17412958};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000305|PubMed:17412958};
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:17412958};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000305|PubMed:17412958};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The N-terminal kinase domain produces inositol polyphosphates.
CC The C-terminal acid phosphatase-like domain binds inositol
CC polyphosphates and negatively regulates their accumulation. The C-
CC terminal domain reduces the amount of inositol pyrophosphates in a
CC dose-dependent manner in vitro. {ECO:0000250|UniProtKB:O74429}.
CC -!- MISCELLANEOUS: Present with 8810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Although related to histidine acid phosphatase proteins, it
CC lacks the conserved active sites, suggesting that it has no phosphatase
CC activity. {ECO:0000305}.
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DR EMBL; U20162; AAB67497.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09710.1; -; Genomic_DNA.
DR PIR; S59376; S59376.
DR RefSeq; NP_013514.1; NM_001182298.1.
DR AlphaFoldDB; Q06685; -.
DR SMR; Q06685; -.
DR BioGRID; 31667; 551.
DR IntAct; Q06685; 31.
DR MINT; Q06685; -.
DR STRING; 4932.YLR410W; -.
DR iPTMnet; Q06685; -.
DR MaxQB; Q06685; -.
DR PaxDb; Q06685; -.
DR PRIDE; Q06685; -.
DR EnsemblFungi; YLR410W_mRNA; YLR410W; YLR410W.
DR GeneID; 851126; -.
DR KEGG; sce:YLR410W; -.
DR SGD; S000004402; VIP1.
DR VEuPathDB; FungiDB:YLR410W; -.
DR eggNOG; KOG1057; Eukaryota.
DR GeneTree; ENSGT00390000009048; -.
DR HOGENOM; CLU_000914_3_1_1; -.
DR InParanoid; Q06685; -.
DR OMA; IQERWCC; -.
DR BioCyc; YEAST:MON3O-224; -.
DR Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
DR PRO; PR:Q06685; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06685; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0101011; F:inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate 1-diphosphatase activity; IDA:SGD.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IDA:SGD.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IDA:SGD.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IDA:SGD.
DR GO; GO:0000830; F:inositol hexakisphosphate 4-kinase activity; IDA:SGD.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IDA:SGD.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IDA:SGD.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051516; P:regulation of bipolar cell growth; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
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 Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1146
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase"
FT /id="PRO_0000270924"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..597
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT REGION 1106..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 377..378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 402..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 412..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 487..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 492..495
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 487
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:17412958"
FT MUTAGEN 548
FT /note="H->A: Does not affect enzyme activity."
FT /evidence="ECO:0000269|PubMed:17412958"
SQ SEQUENCE 1146 AA; 129755 MW; D69E44EAD16490F9 CRC64;
MSGIKKEPIE SDEVPQQETK NNLPSAPSEM SPLFLNKNTQ KAMQSIAPIL EGFSPKTSAS
ENMSLKLPPP GIQDDHSEEN LTVHDTLQRT ISTALGNGNN TNTVTTSGLK KADSESKSEA
DPEGLSNSNI VNDADNINSI SKTGSPHLPQ GTMDAEQTNM GTNSVPTSSA SSRKSSTSHP
KPRLPKVGKI GVCAMDAKVL SKPMRHILNR LIEHGEFETV IFGDKVILDE RIENWPTCDF
LISFFSSGFP LDKAIKYVKL RKPFIINDLI MQKILWDRRL CLQVLEAYNV PTPPRLEISR
DGGPRANEEL RAKLREHGVE VKPVEEPEWK MVDDDTLEVD GKTMTKPFVE KPVDGEDHNI
YIYYHSKNGG GGRRLFRKVG NKSSEFDPTL VHPRTEGSYI YEQFMDTDNF EDVKAYTIGE
NFCHAETRKS PVVDGIVRRN THGKEVRYIT ELSDEEKTIA GKVSKAFSQM ICGFDLLRVS
GKSYVIDVNG FSFVKDNKAY YDSCANILRS TFIEAKKKMD MEKKNLPIIR EEKEQKWVFK
GLAIIIRHAD RTPKQKFKHS FTSPIFISLL KGHKEEVVIR NVNDLKIVLQ ALRIALDEKA
GNPAKIKVLA NALEKKLNFP GTKIQLKPVL NKENEVEKVQ FILKWGGEPT HSAKYQATEL
GEQMRQDFDL LNKSILQNIK IFSSSERRVL HTAQYWTRAL FGADELGSDE ISIRKDLLDD
SNAAKDLMDK VKKKLKPLLR EGKEAPPQFA WPSKMPEPYL VIKRVVELMN YHKKIMDNNF
AKKDVNSMQT RWCTSEDPSL FKERWDKLFK EFNNAEKVDP SKISELYDTM KYDALHNRQF
LENIFDPGLP NEAIADELGS HSLVDRYPIN VLAKNNFKII DSHSMNNSGK NSSNSVGSLG
WVLESGKTST ARNPKSSSQF DEPRFMQLRE LYKLAKVLFD FICPKEYGIS DAEKLDIGLL
TSLPLAKQIL NDIGDMKNRE TPACVAYFTK ESHIYTLLNI IYESGIPMRI ARNALPELDY
LSQITFELYE STDASGQKSH SIRLKMSPGC HTQDPLDVQL DDRHYISCIP KISLTKHLDM
DYVQQKLRNK FTRVIMPPKF TPVNITSPNL SFQKRKTRRK SVSVEKLKRP ASSGSSSSTS
VNKTLD
