VIP1_SCHPO
ID VIP1_SCHPO Reviewed; 920 AA.
AC O74429;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE EC=2.7.4.24 {ECO:0000250|UniProtKB:Q06685};
DE AltName: Full=Cortical actin cytoskeleton protein asp1;
DE AltName: Full=InsP6 and PP-IP5 kinase;
GN Name=asp1 {ECO:0000312|PomBase:SPCC1672.06c}; Synonyms=vip1;
GN ORFNames=SPCC1672.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-706 AND
RP SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-333 AND HIS-397.
RX PubMed=25254656; DOI=10.1371/journal.pgen.1004586;
RA Poehlmann J., Risse C., Seidel C., Pohlmann T., Jakopec V., Walla E.,
RA Ramrath P., Takeshita N., Baumann S., Feldbruegge M., Fischer R., Fleig U.;
RT "The Vip1 inositol polyphosphate kinase family regulates polarized growth
RT and modulates the microtubule cytoskeleton in fungi.";
RL PLoS Genet. 10:E1004586-E1004586(2014).
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. Phosphorylates
CC inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5
CC which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4.
CC Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks
CC from InsP6, to produce (PP)2-InsP4 (By similarity). Required for
CC maintaining cellular integrity, normal growth and interactions with the
CC ARP complex (PubMed:10388810). Acts as a regulator of the PHO80-PHO85
CC cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating
CC signaling of phosphate availability (By similarity). Required for the
CC function of the cortical actin cytoskeleton, possibly by participating
CC in correct F-actin localization and ensuring polarized growth
CC (PubMed:10388810). Regulates polarized growth and modulates interphase
CC microtubule cytoskeleton. Regulates microtubule dynamics without the
CC requirement of microtubule plus-end tracking protein Mal3. Required for
CC growth zone selection (PubMed:25254656). {ECO:0000250|UniProtKB:O43314,
CC ECO:0000250|UniProtKB:Q06685, ECO:0000269|PubMed:10388810,
CC ECO:0000269|PubMed:25254656}.
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:0000250|UniProtKB:Q06685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000250|UniProtKB:Q06685};
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:0000250|UniProtKB:Q06685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000250|UniProtKB:Q06685};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58.18 uM for inositol hexakisphosphate
CC {ECO:0000269|PubMed:25254656};
CC Vmax=450.5 nmol/min/ug enzyme {ECO:0000269|PubMed:25254656};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10388810,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10388810}.
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:0000269|PubMed:25254656}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to microtubule poison
CC thiabendazole (TBZ). Significantly increased number of interphase
CC microtubules that depolymerize at the lateral cortex/cytoplasm and not
CC at the cell tip. Microtubules touch the lateral cortex and become
CC depolymerized instead of being deflected as do the microtubules of
CC wild-type. {ECO:0000269|PubMed:25254656}.
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; CU329672; CAA20444.1; -; Genomic_DNA.
DR PIR; T41050; T41050.
DR RefSeq; NP_587877.1; NM_001022869.2.
DR AlphaFoldDB; O74429; -.
DR SMR; O74429; -.
DR BioGRID; 275814; 104.
DR STRING; 4896.SPCC1672.06c.1; -.
DR iPTMnet; O74429; -.
DR MaxQB; O74429; -.
DR PaxDb; O74429; -.
DR PRIDE; O74429; -.
DR EnsemblFungi; SPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
DR GeneID; 2539244; -.
DR KEGG; spo:SPCC1672.06c; -.
DR PomBase; SPCC1672.06c; asp1.
DR VEuPathDB; FungiDB:SPCC1672.06c; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_1_1; -.
DR InParanoid; O74429; -.
DR OMA; IQERWCC; -.
DR PhylomeDB; O74429; -.
DR BRENDA; 3.6.1.B18; 5613.
DR Reactome; R-SPO-1855167; Synthesis of pyrophosphates in the cytosol.
DR PRO; PR:O74429; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0101012; F:inositol 1,5-bisdiphosphate 2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IDA:PomBase.
DR GO; GO:0101011; F:inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate 1-diphosphatase activity; IDA:PomBase.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
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; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051516; P:regulation of bipolar cell growth; IMP:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0110162; P:regulation of mitotic spindle elongation (spindle phase three); IMP:PomBase.
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; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..920
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase"
FT /id="PRO_0000270923"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..445
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT REGION 709..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 248..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 258..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 333..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 338..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 333
FT /note="D->A: Loss of kinase activity and thus ATP-dependent
FT production of inositol pyrophosphates. Altered interphase
FT microtubule dynamics. Defective polarized growth."
FT /evidence="ECO:0000269|PubMed:25254656"
FT MUTAGEN 397
FT /note="H->A: Increased ATP-dependent production of inositol
FT pyrophosphates. Altered interphase microtubule dynamics."
FT /evidence="ECO:0000269|PubMed:25254656"
SQ SEQUENCE 920 AA; 105680 MW; 507872D240110C0A CRC64;
MIQNASHLTS IDTESSTRTA SPVSSIVTPT KRNVVGICAM DAKARSKPCR NILNRIIAEG
EFEAIVFGDN MILDEAVENW PACDYLICFY SSGFPLKKAE KYVELRKPFC VNDVVFQELL
WDRRLVLNIL DAIRVSTPQR LICSRDGGPK INKVLEEKLR RKFGIEITEV PTPEVKMLDE
DTLSVDGKII KKPYVEKPVY GEDHNIYIYF PKSVGGGGRK LFRKVANKSS DYDPDLCAPR
TEGSFIYEEF MNVDNAEDVK VYTVGPHYSH AETRKSPVVD GIVRRNPHGK EIRFITNLSE
EEKNMASKIS IAFEQPVCGF DLLRVSGQSY VIDVNGWSFV KDNNDYYDNA ARILKQMFHV
AERHRRNRVP SVQEVLNPPP RESEAWRLKS LVGVLRHADR TPKQKFKFSF TSDPFVKLLQ
GHTEEVILRN EQLNSVLAAT NLATELKCED INKLKQLRLA LETKKDLPGT KVQLKPAYSP
EGKLLKLQLI IKWGGEFTHS ARYQSKDLGE QFHKDLYIMN RDCLKDVEIY TSSERRVSAS
AEIFAMAFLE QETIPSDLLK VRKDLLDDSN AAKDTMDKVK KHLKSLLRVG DTARKEFTWP
ENMPKPCEVM QQVVQLMKYH RAVMRENFII LGPEVEQVQS RWCCNENPAL FRERWEKLFS
EFCDSEKADP SKVSELYDTL KYDALHNRQF LERIFTPYQY LKLPQSPSLI AKEPPQRTDS
NGNLVGMTGA NTNHTERPLE KLYELYDLAK VLFDFVSPQE YGIEPKEKLE IGLLTSVPLL
RQIIHDIKEA RDSDHASTRM YFTKESHIYT LLNCILESGL PMKLPRNQIP ELDYLTQICF
ELFERTNPSG NKEFSVRITL SPGCYAQCPL DMNLDAKHCI SVSPRRSLTR HLDLQQFITK
TEDLCNSVHL PKRFIPVNIN
