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Inositol polyphosphate 5-phosphatase K (EC 3.1.3.56) (Skeletal muscle and kidney-enriched inositol phosphatase)

 INP5K_HUMAN             Reviewed;         448 AA.
Q9BT40; B2R6I2; B2R750; D3DTH8; Q15733; Q9NPJ5; Q9P2R5;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 146.
RecName: Full=Inositol polyphosphate 5-phosphatase K {ECO:0000305};
EC=3.1.3.56 {ECO:0000269|PubMed:10753883, ECO:0000269|PubMed:28190456, ECO:0000269|PubMed:28190459};
AltName: Full=Skeletal muscle and kidney-enriched inositol phosphatase {ECO:0000303|PubMed:10753883};
Name=INPP5K {ECO:0000312|HGNC:HGNC:33882};
Synonyms=PPS, SKIP {ECO:0000303|PubMed:10753883};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAH04362.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Testis {ECO:0000269|PubMed:10753883};
PubMed=10753883; DOI=10.1074/jbc.275.15.10870;
Ijuin T., Mochizuki Y., Fukami K., Funaki M., Asano T., Takenawa T.;
"Identification and characterization of a novel inositol polyphosphate
5-phosphatase.";
J. Biol. Chem. 275:10870-10875(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye {ECO:0000312|EMBL:AAH04362.1};
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] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 120-448.
TISSUE=Brain {ECO:0000312|EMBL:AAB03214.1};
Nussbaum R.L.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-349; ASP-361; TRP-362 AND
TYR-376.
PubMed=12536145; DOI=10.1074/jbc.M209991200;
Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D.,
Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.;
"Identification of a novel domain in two mammalian inositol-
polyphosphate 5-phosphatases that mediates membrane ruffle
localization. The inositol 5-phosphatase SKIP localizes to the
endoplasmic reticulum and translocates to membrane ruffles following
epidermal growth factor stimulation.";
J. Biol. Chem. 278:11376-11385(2003).
[7]
VARIANT [LARGE SCALE ANALYSIS] PHE-315.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[8]
INTERACTION WITH GPR78 AND PAK1, REGION, AND SUBCELLULAR LOCATION.
PubMed=26940976; DOI=10.1111/gtc.12353;
Ijuin T., Hatano N., Takenawa T.;
"Glucose-regulated protein 78 (GRP78) binds directly to PIP3
phosphatase SKIP and determines its localization.";
Genes Cells 21:457-465(2016).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN
MDCCAID, VARIANTS MDCCAID THR-50; SER-294 DEL; CYS-300 AND THR-363,
CHARACTERIZATION OF VARIANTS MDCCAID THR-50; SER-294 DEL; CYS-300 AND
THR-363, AND MUTAGENESIS OF ASP-310.
PubMed=28190456; DOI=10.1016/j.ajhg.2017.01.024;
Wiessner M., Roos A., Munn C.J., Viswanathan R., Whyte T., Cox D.,
Schoser B., Sewry C., Roper H., Phadke R., Marini Bettolo C.,
Barresi R., Charlton R., Boennemann C.G., Abath Neto O., Reed U.C.,
Zanoteli E., Araujo Martins Moreno C., Ertl-Wagner B., Stucka R.,
De Goede C., Borges da Silva T., Hathazi D., Dell'Aica M.,
Zahedi R.P., Thiele S., Mueller J., Kingston H., Mueller S.,
Curtis E., Walter M.C., Strom T.M., Straub V., Bushby K., Muntoni F.,
Swan L.E., Lochmueller H., Senderek J.;
"Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause
Congenital muscular dystrophy with cataracts and mild cognitive
impairment.";
Am. J. Hum. Genet. 100:523-536(2017).
[10]
FUNCTION, CATALYTIC ACTIVITY, VARIANTS MDCCAID MET-23; VAL-93; SER-140
AND ASN-269, CHARACTERIZATION OF VARIANTS MDCCAID MET-23; VAL-93;
SER-140 AND ASN-269, AND MUTAGENESIS OF ASP-310.
PubMed=28190459; DOI=10.1016/j.ajhg.2017.01.019;
Osborn D.P., Pond H.L., Mazaheri N., Dejardin J., Munn C.J.,
Mushref K., Cauley E.S., Moroni I., Pasanisi M.B., Sellars E.A.,
Hill R.S., Partlow J.N., Willaert R.K., Bharj J., Malamiri R.A.,
Galehdari H., Shariati G., Maroofian R., Mora M., Swan L.E., Voit T.,
Conti F.J., Jamshidi Y., Manzini M.C.;
"Mutations in INPP5K cause a form of Congenital Muscular Dystrophy
overlapping Marinesco-Sjoegren Syndrome and dystroglycanopathy.";
Am. J. Hum. Genet. 100:537-545(2017).
-!- FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-
trisphosphate, inositol 1,3,4,5-tetrakisphosphate,
phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol
3,4,5-trisphosphate. Has 6-fold higher affinity for
phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-
trisphosphate (PubMed:10753883). Negatively regulates assembly of
the actin cytoskeleton. Controls insulin-dependent glucose uptake
among inositol 3,4,5-trisphosphate phosphatases; therefore, is the
specific regulator for insulin signaling in skeletal muscle (By
similarity). {ECO:0000250|UniProtKB:Q8C5L6,
ECO:0000269|PubMed:10753883, ECO:0000269|PubMed:28190456,
ECO:0000269|PubMed:28190459}.
-!- CATALYTIC ACTIVITY: D-myo-inositol 1,4,5-trisphosphate + H(2)O =
myo-inositol 1,4-bisphosphate + phosphate.
{ECO:0000269|PubMed:10753883, ECO:0000269|PubMed:28190456,
ECO:0000269|PubMed:28190459}.
-!- SUBUNIT: Interacts with GPR78; necessary for INPP5K localization
at the endoplasmic reticulum. Interacts with PAK1; competes with
GPR78. {ECO:0000269|PubMed:26940976}.
-!- INTERACTION:
Q15041:ARL6IP1; NbExp=3; IntAct=EBI-749162, EBI-714543;
Q969F0:FATE1; NbExp=5; IntAct=EBI-749162, EBI-743099;
Q15323:KRT31; NbExp=5; IntAct=EBI-749162, EBI-948001;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-749162, EBI-739832;
Q15013:MAD2L1BP; NbExp=5; IntAct=EBI-749162, EBI-712181;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:12536145, ECO:0000269|PubMed:26940976,
ECO:0000269|PubMed:28190456}. Note=Following stimulation with EGF,
translocates to membrane ruffles. {ECO:0000269|PubMed:12536145,
ECO:0000269|PubMed:26940976}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:10753883};
IsoId=Q9BT40-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:10753883};
IsoId=Q9BT40-2; Sequence=VSP_050612;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
skeletal muscle, heart and kidney. {ECO:0000269|PubMed:10753883}.
-!- DISEASE: Muscular dystrophy, congenital, with cataracts and
intellectual disability (MDCCAID) [MIM:617404]: An autosomal
recessive form of muscular dystrophy with onset in early childhood
and characterized by progressive muscle weakness. Almost all
patients also have early-onset cataracts and intellectual
disability of varying severity. Some patients have seizures.
{ECO:0000269|PubMed:28190456, ECO:0000269|PubMed:28190459}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase type II family. {ECO:0000305}.
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EMBL; AB036829; BAA92340.1; -; mRNA.
EMBL; AB036830; BAA92341.1; -; mRNA.
EMBL; AB036831; BAA92342.1; -; Genomic_DNA.
EMBL; AK312585; BAG35479.1; -; mRNA.
EMBL; AK312844; BAG35697.1; -; mRNA.
EMBL; CH471108; EAW90614.1; -; Genomic_DNA.
EMBL; CH471108; EAW90615.1; -; Genomic_DNA.
EMBL; CH471108; EAW90618.1; -; Genomic_DNA.
EMBL; BC004362; AAH04362.1; -; mRNA.
EMBL; U45973; AAB03214.1; -; mRNA.
CCDS; CCDS11004.1; -. [Q9BT40-1]
CCDS; CCDS11005.1; -. [Q9BT40-2]
RefSeq; NP_001129114.1; NM_001135642.1. [Q9BT40-2]
RefSeq; NP_057616.2; NM_016532.3. [Q9BT40-1]
RefSeq; NP_570122.1; NM_130766.2. [Q9BT40-2]
RefSeq; XP_005256740.1; XM_005256683.2. [Q9BT40-2]
RefSeq; XP_011522236.1; XM_011523934.1. [Q9BT40-2]
RefSeq; XP_016880244.1; XM_017024755.1. [Q9BT40-2]
RefSeq; XP_016880245.1; XM_017024756.1. [Q9BT40-2]
UniGene; Hs.632238; -.
ProteinModelPortal; Q9BT40; -.
SMR; Q9BT40; -.
BioGrid; 119720; 34.
CORUM; Q9BT40; -.
IntAct; Q9BT40; 22.
MINT; MINT-1445023; -.
STRING; 9606.ENSP00000413937; -.
SwissLipids; SLP:000000957; -.
DEPOD; Q9BT40; -.
iPTMnet; Q9BT40; -.
PhosphoSitePlus; Q9BT40; -.
BioMuta; INPP5K; -.
DMDM; 116242791; -.
EPD; Q9BT40; -.
MaxQB; Q9BT40; -.
PaxDb; Q9BT40; -.
PeptideAtlas; Q9BT40; -.
PRIDE; Q9BT40; -.
Ensembl; ENST00000320345; ENSP00000318476; ENSG00000132376. [Q9BT40-2]
Ensembl; ENST00000406424; ENSP00000385177; ENSG00000132376. [Q9BT40-2]
Ensembl; ENST00000421807; ENSP00000413937; ENSG00000132376. [Q9BT40-1]
GeneID; 51763; -.
KEGG; hsa:51763; -.
UCSC; uc002fsr.4; human. [Q9BT40-1]
CTD; 51763; -.
DisGeNET; 51763; -.
EuPathDB; HostDB:ENSG00000132376.19; -.
GeneCards; INPP5K; -.
HGNC; HGNC:33882; INPP5K.
HPA; HPA031044; -.
MIM; 607875; gene.
MIM; 617404; phenotype.
neXtProt; NX_Q9BT40; -.
OpenTargets; ENSG00000132376; -.
PharmGKB; PA164720951; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000046051; -.
HOVERGEN; HBG082135; -.
InParanoid; Q9BT40; -.
KO; K01106; -.
OMA; PEGLWTM; -.
OrthoDB; EOG091G055L; -.
PhylomeDB; Q9BT40; -.
TreeFam; TF317034; -.
BioCyc; MetaCyc:HS05626-MONOMER; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
ChiTaRS; INPP5K; human.
GeneWiki; SKIP; -.
GenomeRNAi; 51763; -.
PRO; PR:Q9BT40; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132376; -.
CleanEx; HS_INPP5K; -.
ExpressionAtlas; Q9BT40; baseline and differential.
Genevisible; Q9BT40; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IDA:MGI.
GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IDA:MGI.
GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0042577; F:lipid phosphatase activity; NAS:UniProtKB.
GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; IMP:UniProtKB.
GO; GO:0034594; F:phosphatidylinositol trisphosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IMP:UniProtKB.
GO; GO:0005000; F:vasopressin receptor activity; ISS:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:MGI.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:0035305; P:negative regulation of dephosphorylation; ISS:UniProtKB.
GO; GO:0010829; P:negative regulation of glucose transport; IDA:UniProtKB.
GO; GO:2000466; P:negative regulation of glycogen (starch) synthase activity; ISS:UniProtKB.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:UniProtKB.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:2001153; P:positive regulation of renal water transport; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISS:UniProtKB.
GO; GO:0097178; P:ruffle assembly; IDA:UniProtKB.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
Pfam; PF03372; Exo_endo_phos; 1.
SMART; SM00128; IPPc; 1.
SUPFAM; SSF56219; SSF56219; 1.
1: Evidence at protein level;
Alternative splicing; Cataract; Complete proteome;
Congenital muscular dystrophy; Disease mutation;
Endoplasmic reticulum; Hydrolase; Mental retardation; Polymorphism;
Reference proteome.
CHAIN 1 448 Inositol polyphosphate 5-phosphatase K.
/FTId=PRO_0000209727.
REGION 16 318 Catalytic. {ECO:0000255}.
REGION 318 448 Required for interaction with GPR78 and
PAK1. {ECO:0000269|PubMed:26940976}.
REGION 321 448 Required for ruffle localization.
VAR_SEQ 1 76 Missing (in isoform 2).
{ECO:0000303|PubMed:10753883,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_050612.
VARIANT 23 23 V -> M (in MDCCAID; decreased
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; dbSNP:rs750781027).
{ECO:0000269|PubMed:28190459}.
/FTId=VAR_078998.
VARIANT 50 50 I -> T (in MDCCAID; decreased
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; shows normal
localization indistinguishable from the
wild-type).
{ECO:0000269|PubMed:28190456}.
/FTId=VAR_078999.
VARIANT 93 93 M -> V (in MDCCAID; decreased
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity).
{ECO:0000269|PubMed:28190459}.
/FTId=VAR_079000.
VARIANT 140 140 G -> S (in MDCCAID; no
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; dbSNP:rs749383757).
{ECO:0000269|PubMed:28190459}.
/FTId=VAR_079001.
VARIANT 269 269 D -> N (in MDCCAID; no
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; dbSNP:rs761612652).
{ECO:0000269|PubMed:28190459}.
/FTId=VAR_079002.
VARIANT 294 294 Missing (in MDCCAID; decreased
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; shows normal
localization indistinguishable from the
wild-type).
{ECO:0000269|PubMed:28190456}.
/FTId=VAR_079003.
VARIANT 300 300 Y -> C (in MDCCAID; no
phosphatidylinositol-4,5-bisphosphate 5-
phosphatase activity; shows normal
localization indistinguishable from the
wild-type; dbSNP:rs766046008).
{ECO:0000269|PubMed:28190456}.
/FTId=VAR_079004.
VARIANT 315 315 S -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036497.
VARIANT 363 363 I -> T (in MDCCAID; shows a diffuse
perinuclear mislocalization).
{ECO:0000269|PubMed:28190456}.
/FTId=VAR_079005.
MUTAGEN 310 310 D->G: No phosphatidylinositol-4,5-
bisphosphate 5-phosphatase activity.
{ECO:0000269|PubMed:28190456,
ECO:0000269|PubMed:28190459}.
MUTAGEN 349 349 Y->A,F: No effect on EGF-induced ruffle
localization.
{ECO:0000269|PubMed:12536145}.
MUTAGEN 361 361 D->A: Significant decrease in EGF-induced
ruffle localization.
{ECO:0000269|PubMed:12536145}.
MUTAGEN 362 362 W->A: Significant decrease in EGF-induced
ruffle localization.
{ECO:0000269|PubMed:12536145}.
MUTAGEN 376 376 Y->A,F: No effect on EGF-induced ruffle
localization.
{ECO:0000269|PubMed:12536145}.
CONFLICT 120 120 T -> A (in Ref. 5; AAB03214).
{ECO:0000305}.
CONFLICT 416 416 S -> R (in Ref. 1; BAA92340/BAA92341/
BAA92342 and 5; AAB03214). {ECO:0000305}.
CONFLICT 426 426 S -> R (in Ref. 1; BAA92340/BAA92341/
BAA92342 and 5; AAB03214). {ECO:0000305}.
SEQUENCE 448 AA; 51090 MW; 46FAA48C6E2EEAD4 CRC64;
MSSRKLSGPK GRRLSIHVVT WNVASAAPPL DLSDLLQLNN RNLNLDIYVI GLQELNSGII
SLLSDAAFND SWSSFLMDVL SPLSFIKVSH VRMQGILLLV FAKYQHLPYI QILSTKSTPT
GLFGYWGNKG GVNICLKLYG YYVSIINCHL PPHISNNYQR LEHFDRILEM QNCEGRDIPN
ILDHDLIIWF GDMNFRIEDF GLHFVRESIK NRCYGGLWEK DQLSIAKKHD PLLREFQEGR
LLFPPTYKFD RNSNDYDTSE KKRKPAWTDR ILWRLKRQPC AGPDTPIPPA SHFSLSLRGY
SSHMTYGISD HKPVSGTFDL ELKPLVSAPL IVLMPEDLWT VENDMMVSYS STSDFPSSPW
DWIGLYKVGL RDVNDYVSYA WVGDSKVSCS DNLNQVYIDI SNIPTTEDEF LLCYYSNSLR
SVVGISRPFQ IPPGSLREDP LGEAQPQI


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