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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (mmVIP2)

 VIP2_MOUSE              Reviewed;        1129 AA.
Q6ZQB6; E9PVE9; Q3TM75; Q3UUA3; Q7TPU4;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
30-AUG-2017, entry version 97.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2;
EC=2.7.4.21 {ECO:0000269|PubMed:17690096};
EC=2.7.4.24 {ECO:0000269|PubMed:17690096};
AltName: Full=Diphosphoinositol pentakisphosphate kinase 2;
AltName: Full=Histidine acid phosphatase domain-containing protein 1;
AltName: Full=InsP6 and PP-IP5 kinase 2;
AltName: Full=VIP1 homolog 2;
Short=mmVIP2;
Name=Ppip5k2; Synonyms=Hisppd1, Kiaa0433, Vip2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Lung, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Egg;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17690096; DOI=10.1074/jbc.M704656200;
Fridy P.C., Otto J.C., Dollins D.E., York J.D.;
"Cloning and characterization of two human VIP1-like inositol
hexakisphosphate and diphosphoinositol pentakisphosphate kinases.";
J. Biol. Chem. 282:30754-30762(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-1066, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
{ECO:0000269|PubMed:17690096}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
{ECO:0000269|PubMed:17690096}.
-!- 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:17690096}.
-!- 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:17690096}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
{ECO:0000269|PubMed:17690096}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.23 uM for InsP6 {ECO:0000269|PubMed:17690096};
KM=0.54 uM for InsP7 {ECO:0000269|PubMed:17690096};
Vmax=1.70 nmol/min/mg enzyme with InsP6 as substrate
{ECO:0000269|PubMed:17690096};
Vmax=5.23 nmol/min/mg enzyme with InsP7 as substrate
{ECO:0000269|PubMed:17690096};
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O43314}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6ZQB6-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZQB6-2; Sequence=VSP_030637, VSP_030638;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6ZQB6-3; Sequence=VSP_041618;
-!- 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:O43314}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC97950.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK129140; BAC97950.1; ALT_INIT; mRNA.
EMBL; AK138622; BAE23724.1; -; mRNA.
EMBL; AK166095; BAE38567.1; -; mRNA.
EMBL; AC099860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC162298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053396; AAH53396.1; -; mRNA.
CCDS; CCDS35678.2; -. [Q6ZQB6-1]
RefSeq; NP_776121.4; NM_173760.5. [Q6ZQB6-1]
UniGene; Mm.220817; -.
UniGene; Mm.417682; -.
ProteinModelPortal; Q6ZQB6; -.
SMR; Q6ZQB6; -.
STRING; 10090.ENSMUSP00000043401; -.
iPTMnet; Q6ZQB6; -.
PhosphoSitePlus; Q6ZQB6; -.
PaxDb; Q6ZQB6; -.
PeptideAtlas; Q6ZQB6; -.
PRIDE; Q6ZQB6; -.
Ensembl; ENSMUST00000042509; ENSMUSP00000043401; ENSMUSG00000040648. [Q6ZQB6-1]
Ensembl; ENSMUST00000171129; ENSMUSP00000132889; ENSMUSG00000040648. [Q6ZQB6-3]
GeneID; 227399; -.
KEGG; mmu:227399; -.
UCSC; uc007cfk.4; mouse. [Q6ZQB6-1]
UCSC; uc007cfl.1; mouse. [Q6ZQB6-2]
CTD; 23262; -.
MGI; MGI:2142810; Ppip5k2.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
GeneTree; ENSGT00390000009048; -.
HOGENOM; HOG000177917; -.
HOVERGEN; HBG108657; -.
InParanoid; Q6ZQB6; -.
KO; K13024; -.
Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
SABIO-RK; Q6ZQB6; -.
PRO; PR:Q6ZQB6; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000040648; -.
CleanEx; MM_HISPPD1; -.
ExpressionAtlas; Q6ZQB6; baseline and differential.
Genevisible; Q6ZQB6; MM.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; IDA:MGI.
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; IDA:MGI.
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;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 1129 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 2.
/FTId=PRO_0000315693.
NP_BIND 243 246 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 252 254 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 327 329 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 59 60 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 219 220 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 332 335 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 377 448 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:O43314}.
BINDING 140 140 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 193 193 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 200 200 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 219 219 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 254 254 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 268 268 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 270 270 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 315 315 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:O43314}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000250|UniProtKB:O43314}.
MOD_RES 1058 1058 Phosphoserine.
{ECO:0000250|UniProtKB:O43314}.
MOD_RES 1066 1066 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1106 1106 Phosphoserine.
{ECO:0000250|UniProtKB:O43314}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000250|UniProtKB:O43314}.
VAR_SEQ 1 6 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041618.
VAR_SEQ 545 545 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030637.
VAR_SEQ 1051 1129 SSMATRSSPGMRRKISLNTYTPTKILPTPPAALKSSKASSK
AAAGGPSQAMAPHTSSRKKSINSKTEGHEPKKSTGKKR ->
CMEFTFIVT (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030638.
CONFLICT 197 197 A -> V (in Ref. 1; BAE38567).
{ECO:0000305}.
CONFLICT 582 582 A -> T (in Ref. 4; AAH53396).
{ECO:0000305}.
CONFLICT 729 729 I -> V (in Ref. 4; AAH53396).
{ECO:0000305}.
CONFLICT 1035 1035 S -> P (in Ref. 4; AAH53396).
{ECO:0000305}.
CONFLICT 1109 1109 K -> M (in Ref. 1; BAC97950).
{ECO:0000305}.
SEQUENCE 1129 AA; 128427 MW; A563826CC0085E3C CRC64;
MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI VVGICSMAKK
SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC DCLISFHSKG FPLDKAVAYA
KLRNPFVIND LNMQYLIQDR RDVYSILQAE GILLPRYAIL NRDPNNPKEC NLIEGEDHVE
VNGEVFQKPF VEKPVSAEDH NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY
IYEEFMPTDG TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA
WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN IVMRELAPQF
HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP KQKMKMEVRH QKFFDLFEKC
DGYKSGKLKL KKPKQLQEVL DIARQLLMEL GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG
INRKVQLTYL PHGCPKTSSE EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY
PGGQGDYAGF PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ
MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS GSISVIKSMH
LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS ETLELMLRRW SKLEKDFKTK
NGRYDISKIP DIYDCIKYDV QHNGSLKLEN TMELYRLSKA LADIVIPQEY GITKAEKLEI
AKGYCTPLVR KIRSDLQRTQ DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS
ILRYGALCDD SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS
PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV MLFKPLVSEP
IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN PTVGFELYSM VPSICPLETL
HNALFLKQVD DFLASIASPS TEVLRKVPEM SSMATRSSPG MRRKISLNTY TPTKILPTPP
AALKSSKASS KAAAGGPSQA MAPHTSSRKK SINSKTEGHE PKKSTGKKR


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