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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog)

 VIP1_RAT                Reviewed;        1434 AA.
P0C644;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
25-OCT-2017, entry version 75.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1;
EC=2.7.4.21;
EC=2.7.4.24;
AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
AltName: Full=InsP6 and PP-IP5 kinase 1;
AltName: Full=VIP1 homolog;
Name=Ppip5k1; Synonyms=Hisppd2a, Vip1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17702752; DOI=10.1074/jbc.M704655200;
Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.;
"Purification, sequencing, and molecular identification of a mammalian
PP-InsP5 kinase that is activated when cells are exposed to
hyperosmotic stress.";
J. Biol. Chem. 282:30763-30775(2007).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases IP6K1, IP6K2 and IP6K3 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, regulate a
variety of cellular processes, including apoptosis, vesicle
trafficking, cytoskeletal dynamics, exocytosis, insulin signaling
and neutrophil activation. 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. Activated
when cells are exposed to hyperosmotic stress.
{ECO:0000250|UniProtKB:Q6PFW1, ECO:0000269|PubMed:17702752}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
{ECO:0000269|PubMed:17702752}.
-!- 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:17702752}.
-!- 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:17702752}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
{ECO:0000269|PubMed:17702752}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane
{ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma
membrane upon activation of the PtdIns 3-kinase pathway.
{ECO:0000250|UniProtKB:Q6PFW1}.
-!- DOMAIN: The C-terminal acid phosphatase-like domain binds
PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the
phosphatase domain of histidine acid phosphatases, it has no
phosphatase activity. {ECO:0000250|UniProtKB:Q6PFW1}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC116071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Rn.46305; -.
ProteinModelPortal; P0C644; -.
SMR; P0C644; -.
STRING; 10116.ENSRNOP00000059430; -.
iPTMnet; P0C644; -.
PaxDb; P0C644; -.
PRIDE; P0C644; -.
UCSC; RGD:1311552; rat.
RGD; 1311552; Ppip5k1.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
HOGENOM; HOG000177917; -.
HOVERGEN; HBG108657; -.
InParanoid; P0C644; -.
PhylomeDB; P0C644; -.
BRENDA; 2.7.4.24; 5301.
PRO; PR:P0C644; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
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; ISS:UniProtKB.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
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; 3.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 1434 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 1.
/FTId=PRO_0000315691.
NP_BIND 250 253 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 259 261 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 334 336 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 66 67 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 226 227 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 339 342 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 384 455 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:Q6PFW1}.
BINDING 147 147 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 200 200 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 207 207 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 226 226 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 261 261 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 275 275 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 277 277 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 322 322 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 984 984 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1034 1034 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1070 1070 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARP1}.
MOD_RES 1149 1149 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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


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