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   24-JAN-2024, entry version 150.
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; 18.
DR   IntAct; Q96PE3; 4.
DR   MINT; Q96PE3; -.
DR   STRING; 9606.ENSP00000074304; -.
DR   SwissLipids; SLP:000000900; -.
DR   DEPOD; INPP4A; -.
DR   GlyCosmos; Q96PE3; 1 site, 1 glycan.
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; 9606-ENSP00000074304; -.
DR   PeptideAtlas; Q96PE3; -.
DR   ProteomicsDB; 77678; -. [Q96PE3-1]
DR   ProteomicsDB; 77679; -. [Q96PE3-2]
DR   ProteomicsDB; 77680; -. [Q96PE3-3]
DR   ProteomicsDB; 77681; -. [Q96PE3-4]
DR   Pumba; Q96PE3; -.
DR   Antibodypedia; 41266; 128 antibodies from 22 providers.
DR   DNASU; 3631; -.
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   AGR; HGNC:6074; -.
DR   CTD; 3631; -.
DR   DisGeNET; 3631; -.
DR   GeneCards; INPP4A; -.
DR   HGNC; HGNC:6074; INPP4A.
DR   HPA; ENSG00000040933; Low tissue specificity.
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; HQVTYRF; -.
DR   OrthoDB; 5490552at2759; -.
DR   PhylomeDB; Q96PE3; -.
DR   TreeFam; TF325637; -.
DR   BioCyc; MetaCyc:HS00551-MONOMER; -.
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; 16 hits in 1164 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 192 other cell types or tissues.
DR   ExpressionAtlas; Q96PE3; baseline and differential.
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: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   CDD; cd04048; C2A_Copine; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR039034; INPP4.
DR   PANTHER; PTHR12187; AGAP000124-PA; 1.
DR   PANTHER; PTHR12187:SF4; INOSITOL POLYPHOSPHATE-4-PHOSPHATASE TYPE I A; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 1.
DR   Genevisible; Q96PE3; HS.
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
//