INP4A_HUMAN
ID INP4A_HUMAN Reviewed; 977 AA.
AC Q96PE3; O15326; Q13187; Q53TD8; Q8TC02;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Inositol polyphosphate-4-phosphatase type I A {ECO:0000312|HGNC:HGNC:6074};
DE AltName: Full=Inositol polyphosphate 4-phosphatase type I {ECO:0000303|PubMed:30071275};
DE AltName: Full=Type I inositol 3,4-bisphosphate 4-phosphatase;
DE EC=3.1.3.66 {ECO:0000269|PubMed:15716355, ECO:0000269|PubMed:20463662, ECO:0000269|PubMed:30071275};
GN Name=INPP4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7608176; DOI=10.1074/jbc.270.27.16128;
RA Norris F.A., Auethavekiat V., Majerus P.W.;
RT "The isolation and characterization of cDNA encoding human and rat brain
RT inositol polyphosphate 4-phosphatase.";
RL J. Biol. Chem. 270:16128-16133(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=9295334; DOI=10.1074/jbc.272.38.23859;
RA Norris F.A., Atkins R.C., Majerus P.W.;
RT "The cDNA cloning and characterization of inositol polyphosphate 4-
RT phosphatase type II. Evidence for conserved alternative splicing in the 4-
RT phosphatase family.";
RL J. Biol. Chem. 272:23859-23864(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11485317; DOI=10.1006/bbrc.2001.5331;
RA Shearn C.T., Walker J., Norris F.A.;
RT "Identification of a novel spliceoform of inositol polyphosphate 4-
RT phosphatase type Ialpha expressed in human platelets: structure of human
RT inositol polyphosphate 4-phosphatase type I gene.";
RL Biochem. Biophys. Res. Commun. 286:119-125(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-731
RP AND CYS-895, AND ACTIVE SITE.
RX PubMed=15716355; DOI=10.1091/mbc.e04-09-0799;
RA Ivetac I., Munday A.D., Kisseleva M.V., Zhang X.M., Luff S., Tiganis T.,
RA Whisstock J.C., Rowe T., Majerus P.W., Mitchell C.A.;
RT "The type Ialpha inositol polyphosphate 4-phosphatase generates and
RT terminates phosphoinositide 3-kinase signals on endosomes and the plasma
RT membrane.";
RL Mol. Biol. Cell 16:2218-2233(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=20463662; DOI=10.1038/nature09023;
RA Sasaki J., Kofuji S., Itoh R., Momiyama T., Takayama K., Murakami H.,
RA Chida S., Tsuya Y., Takasuga S., Eguchi S., Asanuma K., Horie Y., Miura K.,
RA Davies E.M., Mitchell C., Yamazaki M., Hirai H., Takenawa T., Suzuki A.,
RA Sasaki T.;
RT "The PtdIns(3,4)P(2) phosphatase INPP4A is a suppressor of excitotoxic
RT neuronal death.";
RL Nature 465:497-501(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INTERACTION WITH INPP5F.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [13]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30071275; DOI=10.1016/j.bbamcr.2018.07.013;
RA Chaudhuri R., Khanna K., Koundinya D., Pattnaik B., Vatsa D., Agrawal A.,
RA Ghosh B.;
RT "Novel nuclear translocation of inositol polyphosphate 4-phosphatase is
RT associated with cell cycle, proliferation and survival.";
RL Biochim. Biophys. Acta 0:0-0(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) (PubMed:20463662,
CC PubMed:15716355). Catalyzes also inositol 1,3,4-trisphosphate and
CC inositol 1,4-bisphosphate (By similarity). Antagonizes the PI3K-AKT/PKB
CC signaling pathway by dephosphorylating phosphoinositides and thereby
CC modulating cell cycle progression and cell survival (PubMed:30071275)
CC (By similarity). May protect neurons from excitotoxic cell death by
CC regulating the synaptic localization of cell surface N-methyl-D-
CC aspartate-type glutamate receptors (NMDARs) and NMDAR-mediated
CC excitatory postsynaptic current (By similarity).
CC {ECO:0000250|UniProtKB:Q62784, ECO:0000250|UniProtKB:Q9EPW0,
CC ECO:0000269|PubMed:15716355, ECO:0000269|PubMed:20463662,
CC ECO:0000269|PubMed:30071275}.
CC -!- FUNCTION: [Isoform 4]: Displays no 4-phosphatase activity for
CC PtdIns(3,4)P2, Ins(3,4)P2, or Ins(1,3,4)P3.
CC {ECO:0000269|PubMed:9295334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:17193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58088; EC=3.1.3.66;
CC Evidence={ECO:0000269|PubMed:15716355, ECO:0000269|PubMed:20463662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17194;
CC Evidence={ECO:0000305|PubMed:15716355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4-bisphosphate + H2O = 1D-myo-inositol 3-
CC phosphate + phosphate; Xref=Rhea:RHEA:43388, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58401, ChEBI:CHEBI:83241;
CC Evidence={ECO:0000250|UniProtKB:Q62784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43389;
CC Evidence={ECO:0000250|UniProtKB:Q62784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol
CC 1,3-bisphosphate + phosphate; Xref=Rhea:RHEA:43392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414,
CC ChEBI:CHEBI:83242; Evidence={ECO:0000250|UniProtKB:Q62784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43393;
CC Evidence={ECO:0000250|UniProtKB:Q62784};
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC {ECO:0000269|PubMed:15716355, ECO:0000269|PubMed:20463662}.
CC -!- SUBUNIT: Interacts with INPP5F. {ECO:0000269|PubMed:25869668}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:15716355}. Recycling endosome membrane
CC {ECO:0000269|PubMed:15716355}. Cell membrane
CC {ECO:0000269|PubMed:15716355}. Nucleus {ECO:0000269|PubMed:30071275}.
CC Cytoplasm {ECO:0000269|PubMed:30071275}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9EPW0}. Note=Translocates to the plasma
CC membrane upon EGF stimulation (PubMed:15716355). Shuttles between the
CC cytoplasm and the nucleus, depending on the cell cycle stage, with
CC highest amounts detected in the nucleus during the G0/G1phase
CC (PubMed:30071275). {ECO:0000269|PubMed:15716355,
CC ECO:0000269|PubMed:30071275}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha-3;
CC IsoId=Q96PE3-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-1;
CC IsoId=Q96PE3-2; Sequence=VSP_015241;
CC Name=3;
CC IsoId=Q96PE3-3; Sequence=VSP_015240;
CC Name=4; Synonyms=Beta;
CC IsoId=Q96PE3-4; Sequence=VSP_015241, VSP_015242;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the platelets, MEG-01
CC megakaryocytes and Jurkat T-cells. Isoform 2 is expressed in the brain.
CC {ECO:0000269|PubMed:11485317}.
CC -!- MISCELLANEOUS: [Isoform 4]: Inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the inositol 3,4-bisphosphate 4-phosphatase
CC family. {ECO:0000305}.
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DR EMBL; U26398; AAB01068.1; -; mRNA.
DR EMBL; U96919; AAB72150.1; -; mRNA.
DR EMBL; AF368319; AAK58870.1; -; mRNA.
DR EMBL; AC010134; AAX93230.1; -; Genomic_DNA.
DR EMBL; BC028361; AAH28361.1; -; mRNA.
DR CCDS; CCDS46369.1; -. [Q96PE3-1]
DR CCDS; CCDS46370.1; -. [Q96PE3-2]
DR CCDS; CCDS46371.1; -. [Q96PE3-3]
DR CCDS; CCDS46372.1; -. [Q96PE3-4]
DR PIR; B57487; B57487.
DR RefSeq; NP_001127696.1; NM_001134224.1. [Q96PE3-1]
DR RefSeq; NP_001127697.1; NM_001134225.1. [Q96PE3-3]
DR RefSeq; NP_001557.1; NM_001566.2. [Q96PE3-4]
DR RefSeq; NP_004018.1; NM_004027.2. [Q96PE3-2]
DR RefSeq; XP_016859487.1; XM_017003998.1.
DR AlphaFoldDB; Q96PE3; -.
DR SMR; Q96PE3; -.
DR BioGRID; 109843; 15.
DR IntAct; Q96PE3; 4.
DR MINT; Q96PE3; -.
DR STRING; 9606.ENSP00000074304; -.
DR SwissLipids; SLP:000000900; -.
DR DEPOD; INPP4A; -.
DR GlyGen; Q96PE3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96PE3; -.
DR MetOSite; Q96PE3; -.
DR PhosphoSitePlus; Q96PE3; -.
DR BioMuta; INPP4A; -.
DR DMDM; 73920059; -.
DR EPD; Q96PE3; -.
DR jPOST; Q96PE3; -.
DR MassIVE; Q96PE3; -.
DR MaxQB; Q96PE3; -.
DR PaxDb; Q96PE3; -.
DR PeptideAtlas; Q96PE3; -.
DR PRIDE; Q96PE3; -.
DR ProteomicsDB; 77678; -. [Q96PE3-1]
DR ProteomicsDB; 77679; -. [Q96PE3-2]
DR ProteomicsDB; 77680; -. [Q96PE3-3]
DR ProteomicsDB; 77681; -. [Q96PE3-4]
DR Antibodypedia; 41266; 108 antibodies from 22 providers.
DR DNASU; 3631; -.
DR Ensembl; ENST00000074304.9; ENSP00000074304.5; ENSG00000040933.16. [Q96PE3-1]
DR Ensembl; ENST00000409016.8; ENSP00000386704.3; ENSG00000040933.16. [Q96PE3-2]
DR Ensembl; ENST00000409540.7; ENSP00000387294.3; ENSG00000040933.16. [Q96PE3-4]
DR Ensembl; ENST00000409851.8; ENSP00000386777.4; ENSG00000040933.16. [Q96PE3-3]
DR Ensembl; ENST00000523221.1; ENSP00000427722.1; ENSG00000040933.16. [Q96PE3-1]
DR GeneID; 3631; -.
DR KEGG; hsa:3631; -.
DR MANE-Select; ENST00000409851.8; ENSP00000386777.4; NM_001134225.2; NP_001127697.1. [Q96PE3-3]
DR UCSC; uc002syx.4; human. [Q96PE3-1]
DR CTD; 3631; -.
DR DisGeNET; 3631; -.
DR GeneCards; INPP4A; -.
DR HGNC; HGNC:6074; INPP4A.
DR HPA; ENSG00000040933; Low tissue specificity.
DR MalaCards; INPP4A; -.
DR MIM; 600916; gene.
DR neXtProt; NX_Q96PE3; -.
DR OpenTargets; ENSG00000040933; -.
DR PharmGKB; PA29882; -.
DR VEuPathDB; HostDB:ENSG00000040933; -.
DR eggNOG; KOG4428; Eukaryota.
DR GeneTree; ENSGT00940000157360; -.
DR HOGENOM; CLU_007802_0_0_1; -.
DR InParanoid; Q96PE3; -.
DR OMA; CRRENTY; -.
DR OrthoDB; 129165at2759; -.
DR PhylomeDB; Q96PE3; -.
DR TreeFam; TF325637; -.
DR BioCyc; MetaCyc:HS00551-MON; -.
DR BRENDA; 3.1.3.66; 2681.
DR PathwayCommons; Q96PE3; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SignaLink; Q96PE3; -.
DR UniPathway; UPA00944; -.
DR BioGRID-ORCS; 3631; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; INPP4A; human.
DR GeneWiki; INPP4A; -.
DR GenomeRNAi; 3631; -.
DR Pharos; Q96PE3; Tbio.
DR PRO; PR:Q96PE3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96PE3; protein.
DR Bgee; ENSG00000040933; Expressed in Brodmann (1909) area 23 and 190 other tissues.
DR ExpressionAtlas; Q96PE3; baseline and differential.
DR Genevisible; Q96PE3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017161; F:inositol-1,3,4-trisphosphate 4-phosphatase activity; TAS:Reactome.
DR GO; GO:0052828; F:inositol-3,4-bisphosphate 4-phosphatase activity; TAS:Reactome.
DR GO; GO:0016316; F:phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity; IBA:GO_Central.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039034; INPP4.
DR PANTHER; PTHR12187; PTHR12187; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Endosome; Hydrolase;
KW Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..977
FT /note="Inositol polyphosphate-4-phosphatase type I A"
FT /id="PRO_0000190232"
FT DOMAIN 26..153
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ACT_SITE 895
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305|PubMed:15716355"
FT MOD_RES 355
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 389..393
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015240"
FT VAR_SEQ 574..613
FT /note="GNPDSHAYWIRPEDPFCDVPSSPCPSTMPSTACHPHLTTH -> D (in
FT isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7608176,
FT ECO:0000303|PubMed:9295334"
FT /id="VSP_015241"
FT VAR_SEQ 935..977
FT /note="EGCRRENTMKNVGSRKYAFNSLQLKAFPKHYRPPEGTYGKVET -> IGTRE
FT VVTQKNLSGLVPIRDLRLDPSLLCSIPLLALSPNLLIVWLFLSIAYLVTKLRCK (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:9295334"
FT /id="VSP_015242"
FT VARIANT 604
FT /note="T -> A (in dbSNP:rs2278206)"
FT /id="VAR_059359"
FT MUTAGEN 731
FT /note="D->N: Complete loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15716355"
FT MUTAGEN 895
FT /note="C->S: Does not rescue the wortmannin-induced
FT dilation of endosomes due to accumulation of
FT (PtdIns(3,4)P2)."
FT /evidence="ECO:0000269|PubMed:15716355"
FT CONFLICT 767
FT /note="G -> E (in Ref. 5; AAH28361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 109956 MW; 14087B24256B2D05 CRC64;
MTAREHSPRH GARARAMQRA STIDVAADML GLSLAGNIQD PDEPILEFSL ACSELHTPSL
DRKPNSFVAV SVTTPPQAFW TKHAQTEIIE GTNNPIFLSS IAFFQDSLIN QMTQVKLSVY
DVKDRSQGTM YLLGSGTFIV KDLLQDRHHR LHLTLRSAES DRVGNITVIG WQMEEKSDQR
PPVTRSVDTV NGRMVLPVDE SLTEALGIRS KYASLRKDTL LKSVFGGAIC RMYRFPTTDG
NHLRILEQMA ESVLSLHVPR QFVKLLLEED AARVCELEEL GELSPCWESL RRQIVTQYQT
IILTYQENLT DLHQYRGPSF KASSLKADKK LEFVPTNLHI QRMRVQDDGG SDQNYDIVTI
GAPAAHCQGF KSGGLRKKLH KFEETKKHFE ECCTSSGCQS IIYIPQDVVR AKEIIAQINT
LKTQVSYYAE RLSRAAKDRS ATGLERTLAI LADKTRQLVT VCDCKLLANS IHGLNAARPD
YIASKASPTS TEEEQVMLRN DQDTLMARWT GRNSRSSLQV DWHEEEWEKV WLNVDKSLEC
IIQRVDKLLQ KERLHGEGCE DVFPCAGSCT SKKGNPDSHA YWIRPEDPFC DVPSSPCPST
MPSTACHPHL TTHCSPPPEE SSPGEWSEAL YPLLTTLTDC VAMMSDKAKK AMVFLLMQDS
APTIATYLSL QYRRDVVFCQ TLTALICGFI IKLRNCLHDD GFLRQLYTIG LLAQFESLLS
TYGEELAMLE DMSLGIMDLR NVTFKVTQAT SSASADMLPV ITGNRDGFNV RVPLPGPLFD
ALPREIQSGM LLRVQPVLFN VGINEQQTLA ERFGDTSLQE VINVESLVRL NSYFEQFKEV
LPEDCLPRSR SQTCLPELLR FLGQNVHARK NKNVDILWQA AEICRRLNGV RFTSCKSAKD
RTAMSVTLEQ CLILQHEHGM APQVFTQALE CMRSEGCRRE NTMKNVGSRK YAFNSLQLKA
FPKHYRPPEG TYGKVET
