VIP1_RAT
ID VIP1_RAT Reviewed; 1434 AA.
AC P0C644;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 {ECO:0000305};
DE EC=2.7.4.24 {ECO:0000269|PubMed:17702752};
DE AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
DE AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
DE AltName: Full=InsP6 and PP-IP5 kinase 1;
DE AltName: Full=VIP1 homolog;
GN Name=Ppip5k1 {ECO:0000312|RGD:1311552}; Synonyms=Hisppd2a, Vip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17702752; DOI=10.1074/jbc.m704655200;
RA Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.;
RT "Purification, sequencing, and molecular identification of a mammalian PP-
RT InsP5 kinase that is activated when cells are exposed to hyperosmotic
RT stress.";
RL J. Biol. Chem. 282:30763-30775(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC group-containing inositol pyrophosphates diphosphoinositol
CC pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC respectively called InsP7 and InsP8, regulate a variety of cellular
CC processes, including apoptosis, vesicle trafficking, cytoskeletal
CC dynamics, exocytosis, insulin signaling and neutrophil activation.
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. Activated when
CC cells are exposed to hyperosmotic stress.
CC {ECO:0000250|UniProtKB:Q6PFW1, ECO:0000269|PubMed:17702752}.
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:Q6PFW1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000250|UniProtKB:Q6PFW1};
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:17702752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000269|PubMed:17702752};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane
CC upon activation of the PtdIns 3-kinase pathway.
CC {ECO:0000250|UniProtKB:Q6PFW1}.
CC -!- DOMAIN: The C-terminal acid phosphatase-like domain binds
CC PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase
CC domain of histidine acid phosphatases, it has no phosphatase activity.
CC {ECO:0000250|UniProtKB:Q6PFW1}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000305}.
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DR EMBL; AC116071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C644; -.
DR SMR; P0C644; -.
DR IntAct; P0C644; 2.
DR STRING; 10116.ENSRNOP00000059430; -.
DR iPTMnet; P0C644; -.
DR PaxDb; P0C644; -.
DR PRIDE; P0C644; -.
DR UCSC; RGD:1311552; rat.
DR RGD; 1311552; Ppip5k1.
DR eggNOG; KOG1057; Eukaryota.
DR InParanoid; P0C644; -.
DR PhylomeDB; P0C644; -.
DR BRENDA; 2.7.4.24; 5301.
DR Reactome; R-RNO-1855167; Synthesis of pyrophosphates in the cytosol.
DR PRO; PR:P0C644; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1434
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase 1"
FT /id="PRO_0000315691"
FT REGION 384..455
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT REGION 916..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1434
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 226..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 250..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 259..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 334..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 339..342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ARP1"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1434 AA; 159619 MW; A3C2C9C28B4EAB47 CRC64;
MWSLTANEDE DESATAHFFL GAGDEGLGTC GIGMRTGESD SELLEDEEDE VPPEPQIIVG
ICAMTKKSKS KPMTQILERL CRFDYLTVVI LGEDVILNEP VENWPPCHCL ISFHSKGFPL
DKAVAYSKLR NPFLINDLTM QYYIQDRREV YRILQEEGID LPRYAVLNRD PACPEECNLI
EGEDQVEVNG AVFPKPFVEK PVSAEDHNVY IYYPSSAGGG SQRLFRKIGS RSSVYSPESS
VRKTGSYIYE EFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG KEVRYPVMLT
AMEKLVARKV CVAFKQTVCG FDLLRANGHS FVCDVNGFSF VKNSMKYYDD CAKILGNTIM
RELAPQFQIP WSIPTEAEDI PIVPTTSGTM MELRCVIAII RHGDRTPKQK MKMEVTHPRF
FALFEKHGGY KTGKLKLKRP EQLQEVLDIT RLLLAELEKE PGAEIEEKTG KLEQLKSVLE
MYGHFSGINR KVQLTYYPHG VKASSEGQDL QREPPAPSLL LVLKWGGELT PDGRVQAEEL
GRAFRCMYPG GQGDYAGFPG CGLLRLHSTF RHDLKIYASD EGRVQMTAAA FAKGLLALEG
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHHI LQQDAPFGPE DYDQLAPTGS
TSLLNSMSVI QNPVKVCDQV FALIENLTHQ IRERMQDPSS VDLQLYHSET LELMLQRWSK
LERDFRQKSG RYDISKIPDI YDCVKYDVQH NGSLGLQGTA ELLRLSKALA DVVIPQEYGI
SREEKVEIAV GFCLPLLRKI LLDLQRTHED ESVNKLHPLY SRGVLSPGRH VRTRLYFTSE
SHVHSLLSVF RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER
FHVELHFSPG VKGVEEGSAP AGCGFRPASS ENEEMKTDPG SIENLCPAKP SDEPDRALQT
SPQPVEGTGL PRRSPLIRNR KAGSMEVLSE TSSSRPGGYR LFSSSRPPTE MKQSGLGSQC
TGLFSTTVLG GSSSAPNLQD YARTHGKKLP PAGLKHRDEL LFVPAVKRFS VSFAKHPTNG
FEGCSMVPTI YPLETLHNAL SLRQVSEFLT KVCQRHTDAH AQASAALFDS MHNHQASDNP
FSPPRTLHSP PLQLRHRSEK PPWYSSGPSS TVSSAGPSSP TTVDGNSHFG FSDQSSVNTQ
MIEEKQGLGL LQETPGDGTP EFHIELAEST QSPQEPPVEI SPPGSQDDTE VNQTCQEVPD
TIQPCHDILE EIGQPNQEVP DISQLLLKNH DTATNTCQPC QASQLSKKVY EEICQLCQDN
PEESNQLCQE VSVELGRMVH RFPVSIGSTT QETLMEIGRP TQEIPEEPCQ EFSEKVGMLT
QKASAISELS QDILETDNPS QELSEETDLQ AQEVSEEIDQ EPEVVDELSN EDIS
