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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) (IP6 kinase) (Inositol pyrophosphate synthase 1) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog) (hsVIP1)

 VIP1_HUMAN              Reviewed;        1433 AA.
Q6PFW1; O15082; Q5HYF8; Q7Z3A7; Q86TE7; Q86UV3; Q86UV4; Q86XW8;
Q8IZN0;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 125.
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=IP6 kinase;
AltName: Full=Inositol pyrophosphate synthase 1;
AltName: Full=InsP6 and PP-IP5 kinase 1;
AltName: Full=VIP1 homolog;
Short=hsVIP1;
Name=PPIP5K1; Synonyms=HISPPD2A, IP6K, IPS1, KIAA0377, VIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
TISSUE=Bone marrow, Testis, and Trachea;
PubMed=12825070; DOI=10.1038/sj.ejhg.5200991;
Avidan N., Tamary H., Dgany O., Cattan D., Pariente A., Thulliez M.,
Borot N., Moati L., Barthelme A., Shalmon L., Krasnov T.,
Ben-Asher E., Olender T., Khen M., Yaniv I., Zaizov R., Shalev H.,
Delaunay J., Fellous M., Lancet D., Beckmann J.S.;
"CATSPER2, a human autosomal nonsyndromic male infertility gene.";
Eur. J. Hum. Genet. 11:497-502(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[3]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Endometrial adenocarcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
TISSUE=Eye, and Uterus;
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
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).
[8]
FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
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).
[9]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=17412958; DOI=10.1126/science.1139099;
Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E.,
Haystead T.A., Ribeiro A.A., York J.D.;
"A conserved family of enzymes that phosphorylate inositol
hexakisphosphate.";
Science 316:106-109(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
CATALYTIC ACTIVITY.
PubMed=18981179; DOI=10.1074/jbc.M805686200;
Lin H., Fridy P.C., Ribeiro A.A., Choi J.H., Barma D.K., Vogel G.,
Falck J.R., Shears S.B., York J.D., Mayr G.W.;
"Structural analysis and detection of biological inositol
pyrophosphates reveal that the family of VIP/diphosphoinositol
pentakisphosphate kinases are 1/3-kinases.";
J. Biol. Chem. 284:1863-1872(2009).
[14]
BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, POLYPHOSPHOINOSITIDE-BINDING DOMAIN, AND MUTAGENESIS OF
ARG-399 AND ARG-417.
PubMed=21222653; DOI=10.1042/BJ20101437;
Gokhale N.A., Zaremba A., Shears S.B.;
"Receptor-dependent compartmentalization of PPIP5K1, a kinase with a
cryptic polyphosphoinositide binding domain.";
Biochem. J. 434:415-426(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-987; SER-1037;
SER-1073 AND SER-1152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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:0000269|PubMed:17412958, ECO:0000269|PubMed:17690096,
ECO:0000269|PubMed:17702752}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
-!- 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.
-!- 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.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.12 uM for InsP6 {ECO:0000269|PubMed:17690096,
ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653};
KM=0.10 uM for InsP7 {ECO:0000269|PubMed:17690096,
ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653};
Vmax=0.03 nmol/min/mg enzyme with InsP6 as substrate
{ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
ECO:0000269|PubMed:21222653};
Vmax=0.13 nmol/min/mg enzyme with InsP7 as substrate
{ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
ECO:0000269|PubMed:21222653};
Note=The catalytic efficiency is 80 folds higher for 5-PP-InsP5
(InsP7) compared to InsP6.;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752,
ECO:0000269|PubMed:21222653}. Cell membrane
{ECO:0000269|PubMed:21222653}. Note=Relocalizes to the plasma
membrane upon activation of the PtdIns 3-kinase pathway.
{ECO:0000269|PubMed:21222653}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=Q6PFW1-1; Sequence=Displayed;
Name=2;
IsoId=Q6PFW1-2; Sequence=VSP_030618, VSP_030622;
Name=3;
IsoId=Q6PFW1-3; Sequence=VSP_030618, VSP_030621;
Name=4;
IsoId=Q6PFW1-4; Sequence=VSP_030615, VSP_030618, VSP_030621;
Name=5;
IsoId=Q6PFW1-5; Sequence=VSP_030616, VSP_030619, VSP_030623;
Name=6;
IsoId=Q6PFW1-6; Sequence=VSP_030617;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q6PFW1-7; Sequence=VSP_030618, VSP_030620, VSP_030624;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in
skeletal muscle, heart and brain. {ECO:0000269|PubMed:17690096}.
-!- 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:0000269|PubMed:21222653}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA20831.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF502586; AAP30842.1; -; mRNA.
EMBL; AF502587; AAP30843.1; -; mRNA.
EMBL; AF502588; AAP30844.1; -; mRNA.
EMBL; AF502589; AAP30845.1; -; mRNA.
EMBL; AF543190; AAN40768.1; -; mRNA.
EMBL; AB002375; BAA20831.2; ALT_INIT; mRNA.
EMBL; BX538022; CAD97968.1; -; mRNA.
EMBL; BX647814; CAI46011.1; -; mRNA.
EMBL; BC050263; AAH50263.1; -; mRNA.
EMBL; BC057395; AAH57395.1; -; mRNA.
CCDS; CCDS32215.1; -. [Q6PFW1-3]
CCDS; CCDS45252.1; -. [Q6PFW1-1]
CCDS; CCDS53937.1; -. [Q6PFW1-7]
RefSeq; NP_001124330.1; NM_001130858.2. [Q6PFW1-1]
RefSeq; NP_001124331.1; NM_001130859.2. [Q6PFW1-3]
RefSeq; NP_001177143.1; NM_001190214.1. [Q6PFW1-7]
RefSeq; NP_055474.3; NM_014659.5. [Q6PFW1-3]
RefSeq; XP_005254861.1; XM_005254804.1. [Q6PFW1-3]
RefSeq; XP_016878237.1; XM_017022748.1. [Q6PFW1-3]
RefSeq; XP_016878238.1; XM_017022749.1. [Q6PFW1-3]
RefSeq; XP_016878239.1; XM_017022750.1. [Q6PFW1-3]
RefSeq; XP_016878240.1; XM_017022751.1. [Q6PFW1-3]
RefSeq; XP_016878248.1; XM_017022759.1. [Q6PFW1-6]
UniGene; Hs.156814; -.
UniGene; Hs.679105; -.
UniGene; Hs.679911; -.
ProteinModelPortal; Q6PFW1; -.
SMR; Q6PFW1; -.
BioGrid; 115031; 10.
STRING; 9606.ENSP00000380129; -.
ChEMBL; CHEMBL5046; -.
iPTMnet; Q6PFW1; -.
PhosphoSitePlus; Q6PFW1; -.
BioMuta; PPIP5K1; -.
DMDM; 74758334; -.
EPD; Q6PFW1; -.
MaxQB; Q6PFW1; -.
PaxDb; Q6PFW1; -.
PeptideAtlas; Q6PFW1; -.
PRIDE; Q6PFW1; -.
Ensembl; ENST00000334933; ENSP00000334779; ENSG00000168781. [Q6PFW1-3]
Ensembl; ENST00000348806; ENSP00000308773; ENSG00000168781. [Q6PFW1-7]
Ensembl; ENST00000360135; ENSP00000353253; ENSG00000168781. [Q6PFW1-7]
Ensembl; ENST00000360301; ENSP00000353446; ENSG00000168781. [Q6PFW1-3]
Ensembl; ENST00000396923; ENSP00000380129; ENSG00000168781. [Q6PFW1-1]
Ensembl; ENST00000420765; ENSP00000400887; ENSG00000168781. [Q6PFW1-1]
GeneID; 9677; -.
KEGG; hsa:9677; -.
UCSC; uc001zrw.3; human. [Q6PFW1-1]
CTD; 9677; -.
DisGeNET; 9677; -.
EuPathDB; HostDB:ENSG00000168781.21; -.
GeneCards; PPIP5K1; -.
H-InvDB; HIX0012186; -.
HGNC; HGNC:29023; PPIP5K1.
HPA; HPA039380; -.
MIM; 610979; gene.
neXtProt; NX_Q6PFW1; -.
OpenTargets; ENSG00000168781; -.
PharmGKB; PA165479401; -.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
GeneTree; ENSGT00390000009048; -.
HOVERGEN; HBG108657; -.
InParanoid; Q6PFW1; -.
KO; K13024; -.
OMA; MHSNQAS; -.
OrthoDB; EOG091G00ZU; -.
PhylomeDB; Q6PFW1; -.
TreeFam; TF313594; -.
BioCyc; MetaCyc:HS09822-MONOMER; -.
BRENDA; 2.7.4.24; 2681.
Reactome; R-HSA-1855167; Synthesis of pyrophosphates in the cytosol.
SABIO-RK; Q6PFW1; -.
GenomeRNAi; 9677; -.
PRO; PR:Q6PFW1; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000168781; -.
ExpressionAtlas; Q6PFW1; baseline and differential.
Genevisible; Q6PFW1; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA: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; IDA:UniProtKB.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:MGI.
GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IDA:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; IDA:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
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; Cell membrane; Complete proteome;
Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 1433 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 1.
/FTId=PRO_0000315688.
NP_BIND 248 251 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 257 259 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 332 334 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 64 65 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 224 225 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 337 340 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 382 453 Polyphosphoinositide-binding domain.
{ECO:0000269|PubMed:21222653}.
BINDING 145 145 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 198 198 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 205 205 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 224 224 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 259 259 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 273 273 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 275 275 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 320 320 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 944 944 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1037 1037 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1073 1073 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1145 1145 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARP1}.
MOD_RES 1152 1152 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 653 653 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_030615.
VAR_SEQ 810 821 Missing (in isoform 5).
{ECO:0000303|PubMed:12825070}.
/FTId=VSP_030616.
VAR_SEQ 818 1433 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030617.
VAR_SEQ 818 821 Missing (in isoform 2, isoform 3, isoform
4 and isoform 7).
{ECO:0000303|PubMed:12825070,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9205841}.
/FTId=VSP_030618.
VAR_SEQ 865 957 Missing (in isoform 5).
{ECO:0000303|PubMed:12825070}.
/FTId=VSP_030619.
VAR_SEQ 1020 1082 Missing (in isoform 7).
{ECO:0000303|PubMed:9205841}.
/FTId=VSP_030620.
VAR_SEQ 1062 1082 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12825070,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_030621.
VAR_SEQ 1082 1082 N -> NG (in isoform 2).
{ECO:0000303|PubMed:12825070}.
/FTId=VSP_030622.
VAR_SEQ 1107 1240 Missing (in isoform 5).
{ECO:0000303|PubMed:12825070}.
/FTId=VSP_030623.
VAR_SEQ 1167 1167 Y -> LETRFCHVGQAGLELLTSSDLPASASQSAGITGVSH
RTQPD (in isoform 7).
{ECO:0000303|PubMed:9205841}.
/FTId=VSP_030624.
MUTAGEN 399 399 R->A: Decreases 8-fold the affinity for
PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:21222653}.
MUTAGEN 417 417 R->A: Decreases 16-fold the affinity for
PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:21222653}.
CONFLICT 44 44 D -> G (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 304 304 V -> M (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 374 374 E -> V (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 423 423 E -> Q (in Ref. 1; AAP30843/AAP30845/
AAN40768). {ECO:0000305}.
CONFLICT 473 473 L -> P (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 483 483 F -> S (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 490 490 V -> E (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 548 548 G -> V (in Ref. 4; CAD97968).
{ECO:0000305}.
CONFLICT 738 738 I -> L (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 788 788 V -> A (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 936 936 E -> G (in Ref. 4; CAI46011).
{ECO:0000305}.
CONFLICT 985 985 A -> V (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 1020 1020 G -> A (in Ref. 1; AAP30843).
{ECO:0000305}.
CONFLICT 1041 1041 L -> P (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 1066 1066 V -> L (in Ref. 1; AAP30842).
{ECO:0000305}.
CONFLICT 1126 1126 A -> T (in Ref. 4; CAI46011).
{ECO:0000305}.
CONFLICT 1134 1134 M -> V (in Ref. 4; CAI46011).
{ECO:0000305}.
CONFLICT 1198 1198 P -> R (in Ref. 4; CAI46011).
{ECO:0000305}.
CONFLICT 1293 1293 H -> M (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
CONFLICT 1294 1294 D -> T (in Ref. 1; AAP30845/AAN40768).
{ECO:0000305}.
SEQUENCE 1433 AA; 159521 MW; BA0DEFB2A71B1467 CRC64;
MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC
AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY
GHFSGINRKV QLTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTRSTS
LLNSMTIIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLCYL RYSRGVLSPG RHVRTRLYFT
SESHVHSLLS VFRYGGLLDE TQDAQWQRAL DYLSAISELN YMTQIVIMLY EDNTQDPLSE
ERFHVELHFS PGVKGVEEEG SAPAGCGFRP ASSENEEMKT NQGSMENLCP GKASDEPDRA
LQTSPQPPEG PGLPRRSPLI RNRKAGSMEV LSETSSSRPG GYRLFSSSRP PTEMKQSGLG
SQCTGLFSTT VLGGSSSAPN LQDYARSHGK KLPPASLKHR DELLFVPAVK RFSVSFAKHP
TNGFEGCSMV PTIYPLETLH NALSLRQVSE FLSRVCQRHT DAQAQASAAL FDSMHSSQAS
DNPFSPPRTL HSPPLQLQQR SEKPPWYSSG PSSTVSSAGP SSPTTVDGNS QFGFSDQPSL
NSHVAEEHQG LGLLQETPGS GAQELSIEGE QELFEPNQSP QVPPMETSQP YEEVSQPCQE
VPDISQPCQD ISEALSQPCQ KVPDISQQCQ ENHDNGNHTC QEVPHISQPC QKSSQLCQKV
SEEVCQLCLE NSEEVSQPCQ GVSVEVGKLV HKFHVGVGSL VQETLVEVGS PAEEIPEEVI
QPYQEFSVEV GRLAQETSAI NLLSQGIPEI DKPSQEFPEE IDLQAQEVPE EIN


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