ID   PLPP4_HUMAN             Reviewed;         271 AA.
AC   Q5VZY2; A2RU82; Q08EQ2; Q0IIP2; Q495B4; Q5VZY1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Phospholipid phosphatase 4 {ECO:0000312|HGNC:HGNC:23531};
DE            EC=3.1.3.4 {ECO:0000269|PubMed:17590538};
DE            EC=3.6.1.75 {ECO:0000269|PubMed:17590538};
DE   AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 1A {ECO:0000312|HGNC:HGNC:23531};
GN   Name=PLPP4 {ECO:0000312|HGNC:HGNC:23531};
GN   Synonyms=DPPL2 {ECO:0000303|PubMed:17590538}, PPAPDC1
GN   {ECO:0000312|HGNC:HGNC:23531}, PPAPDC1A {ECO:0000312|HGNC:HGNC:23531};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, REGION, AND MUTAGENESIS
RP   OF ARG-109; HIS-146 AND HIS-202.
RX   PubMed=17590538; DOI=10.1016/j.gene.2007.05.009;
RA   Takeuchi M., Harigai M., Momohara S., Ball E., Abe J., Furuichi K.,
RA   Kamatani N.;
RT   "Cloning and characterization of DPPL1 and DPPL2, representatives of a
RT   novel type of mammalian phosphatidate phosphatase.";
RL   Gene 399:174-180(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Brain;
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   [4]
RP   FUNCTION.
RX   PubMed=28851360; DOI=10.1186/s12943-017-0717-5;
RA   Zhang X., Zhang L., Lin B., Chai X., Li R., Liao Y., Deng X., Liu Q.,
RA   Yang W., Cai Y., Zhou W., Lin Z., Huang W., Zhong M., Lei F., Wu J., Yu S.,
RA   Li X., Li S., Li Y., Zeng J., Long W., Ren D., Huang Y.;
RT   "Phospholipid Phosphatase 4 promotes proliferation and tumorigenesis, and
RT   activates Ca2+-permeable Cationic Channel in lung carcinoma cells.";
RL   Mol. Cancer 16:147-147(2017).
CC   -!- FUNCTION: Magnesium-independent phospholipid phosphatase with broad
CC       substrate specificity (PubMed:17590538). Preferentially catalyzes the
CC       conversion of diacylglycerol pyrophosphate into phosphatidate but can
CC       also act on phosphatidate and lysophosphatidate (PubMed:17590538).
CC       Phospholipid phosphatases are involved in both the synthesis of lipids
CC       and the degradation or generation of lipid-signaling molecules like
CC       diacylglycerol (PubMed:28851360). {ECO:0000269|PubMed:17590538,
CC       ECO:0000269|PubMed:28851360}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75;
CC         Evidence={ECO:0000269|PubMed:17590538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC         Evidence={ECO:0000305|PubMed:17590538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC         glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC         Evidence={ECO:0000269|PubMed:17590538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000305|PubMed:17590538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O = 1,2-
CC         dioctanoyl-sn-glycero-3-phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:42856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78229, ChEBI:CHEBI:82765;
CC         Evidence={ECO:0000269|PubMed:17590538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42857;
CC         Evidence={ECO:0000305|PubMed:17590538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-phosphate + H2O = 1,2-dioctanoyl-
CC         sn-glycerol + phosphate; Xref=Rhea:RHEA:42860, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:76979, ChEBI:CHEBI:78229;
CC         Evidence={ECO:0000269|PubMed:17590538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42861;
CC         Evidence={ECO:0000305|PubMed:17590538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC         octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:75757; Evidence={ECO:0000269|PubMed:17590538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000305|PubMed:17590538};
CC   -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase
CC       (PubMed:17590538). Inhibited by N-ethylmaleimide (PubMed:17590538).
CC       {ECO:0000269|PubMed:17590538}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=104 uM for 1,2-dioctanoyl-sn-glycero-3-diphosphate/diacylglycerol
CC         pyrophosphate {ECO:0000269|PubMed:17590538};
CC         KM=506 uM for 1,2-dioctanoyl-sn-glycero-3-phosphate/phosphatidate
CC         {ECO:0000269|PubMed:17590538};
CC         KM=580 uM for
CC         1-(9Z-octadecenoyl)-sn-glycero-3-phosphate/lysophosphatidate
CC         {ECO:0000269|PubMed:17590538};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000269|PubMed:17590538}.
CC   -!- INTERACTION:
CC       Q5VZY2; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-10485931, EBI-12109402;
CC       Q5VZY2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10485931, EBI-11343438;
CC       Q5VZY2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-10485931, EBI-747430;
CC       Q5VZY2; Q13323: BIK; NbExp=3; IntAct=EBI-10485931, EBI-700794;
CC       Q5VZY2; O95393: BMP10; NbExp=3; IntAct=EBI-10485931, EBI-3922513;
CC       Q5VZY2; P04233-2: CD74; NbExp=3; IntAct=EBI-10485931, EBI-12222807;
CC       Q5VZY2; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-10485931, EBI-1045797;
CC       Q5VZY2; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10485931, EBI-18013275;
CC       Q5VZY2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10485931, EBI-6942903;
CC       Q5VZY2; O43169: CYB5B; NbExp=3; IntAct=EBI-10485931, EBI-1058710;
CC       Q5VZY2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10485931, EBI-781551;
CC       Q5VZY2; P22794: EVI2A; NbExp=3; IntAct=EBI-10485931, EBI-2870359;
CC       Q5VZY2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10485931, EBI-18304435;
CC       Q5VZY2; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-10485931, EBI-6911547;
CC       Q5VZY2; O00258: GET1; NbExp=3; IntAct=EBI-10485931, EBI-18908258;
CC       Q5VZY2; P17302: GJA1; NbExp=3; IntAct=EBI-10485931, EBI-1103439;
CC       Q5VZY2; O95377: GJB5; NbExp=3; IntAct=EBI-10485931, EBI-3909454;
CC       Q5VZY2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10485931, EBI-11721746;
CC       Q5VZY2; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-10485931, EBI-358888;
CC       Q5VZY2; O14880: MGST3; NbExp=3; IntAct=EBI-10485931, EBI-724754;
CC       Q5VZY2; O75459: PAGE1; NbExp=3; IntAct=EBI-10485931, EBI-2559100;
CC       Q5VZY2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-10485931, EBI-716063;
CC       Q5VZY2; Q5VZY2: PLPP4; NbExp=6; IntAct=EBI-10485931, EBI-10485931;
CC       Q5VZY2; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10485931, EBI-3920694;
CC       Q5VZY2; O95470: SGPL1; NbExp=3; IntAct=EBI-10485931, EBI-1046170;
CC       Q5VZY2; P78382: SLC35A1; NbExp=3; IntAct=EBI-10485931, EBI-12870360;
CC       Q5VZY2; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10485931, EBI-17280858;
CC       Q5VZY2; Q16623: STX1A; NbExp=3; IntAct=EBI-10485931, EBI-712466;
CC       Q5VZY2; P32856-2: STX2; NbExp=3; IntAct=EBI-10485931, EBI-11956649;
CC       Q5VZY2; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-10485931, EBI-8032987;
CC       Q5VZY2; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-10485931, EBI-7238458;
CC       Q5VZY2; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-10485931, EBI-3923061;
CC       Q5VZY2; O75841: UPK1B; NbExp=3; IntAct=EBI-10485931, EBI-12237619;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:17590538}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5VZY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5VZY2-2; Sequence=VSP_025238;
CC       Name=3;
CC         IsoId=Q5VZY2-3; Sequence=VSP_025237;
CC       Name=4;
CC         IsoId=Q5VZY2-4; Sequence=VSP_025239, VSP_025240;
CC   -!- TISSUE SPECIFICITY: Expressed mainly to the brain, kidney and testis,
CC       and to a lesser extent the bone marrow, thymus, prostate, liver and
CC       uterus. {ECO:0000269|PubMed:17590538}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; BD418666; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC023282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC101267; AAI01268.1; -; mRNA.
DR   EMBL; BC101268; AAI01269.1; -; mRNA.
DR   EMBL; BC101269; AAI01270.1; -; mRNA.
DR   EMBL; BC122535; AAI22536.1; -; mRNA.
DR   EMBL; BC132787; AAI32788.1; -; mRNA.
DR   CCDS; CCDS41573.1; -. [Q5VZY2-1]
DR   RefSeq; NP_001025230.1; NM_001030059.2. [Q5VZY2-1]
DR   RefSeq; NP_001305095.1; NM_001318166.1.
DR   RefSeq; NP_001305096.1; NM_001318167.1. [Q5VZY2-2]
DR   RefSeq; NP_001305097.1; NM_001318168.1.
DR   RefSeq; NP_001305098.1; NM_001318169.1. [Q5VZY2-4]
DR   AlphaFoldDB; Q5VZY2; -.
DR   BioGRID; 128189; 54.
DR   IntAct; Q5VZY2; 32.
DR   STRING; 9606.ENSP00000381302; -.
DR   SwissLipids; SLP:000000605; -.
DR   DEPOD; PLPP4; -.
DR   iPTMnet; Q5VZY2; -.
DR   PhosphoSitePlus; Q5VZY2; -.
DR   BioMuta; PLPP4; -.
DR   DMDM; 147721098; -.
DR   MassIVE; Q5VZY2; -.
DR   PaxDb; 9606-ENSP00000381302; -.
DR   PeptideAtlas; Q5VZY2; -.
DR   ProteomicsDB; 65736; -. [Q5VZY2-3]
DR   Antibodypedia; 46311; 93 antibodies from 19 providers.
DR   DNASU; 196051; -.
DR   Ensembl; ENST00000398250.6; ENSP00000381302.1; ENSG00000203805.11. [Q5VZY2-1]
DR   GeneID; 196051; -.
DR   KEGG; hsa:196051; -.
DR   MANE-Select; ENST00000398250.6; ENSP00000381302.1; NM_001030059.3; NP_001025230.1.
DR   UCSC; uc001lev.1; human. [Q5VZY2-1]
DR   AGR; HGNC:23531; -.
DR   CTD; 196051; -.
DR   DisGeNET; 196051; -.
DR   GeneCards; PLPP4; -.
DR   HGNC; HGNC:23531; PLPP4.
DR   HPA; ENSG00000203805; Tissue enriched (brain).
DR   neXtProt; NX_Q5VZY2; -.
DR   OpenTargets; ENSG00000203805; -.
DR   PharmGKB; PA134907381; -.
DR   VEuPathDB; HostDB:ENSG00000203805; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000158288; -.
DR   InParanoid; Q5VZY2; -.
DR   OMA; WFSYRRY; -.
DR   OrthoDB; 25293at2759; -.
DR   PhylomeDB; Q5VZY2; -.
DR   TreeFam; TF323722; -.
DR   BioCyc; MetaCyc:G66-31698-MONOMER; -.
DR   BRENDA; 3.1.3.4; 2681.
DR   BRENDA; 3.1.3.81; 2681.
DR   PathwayCommons; Q5VZY2; -.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   SABIO-RK; Q5VZY2; -.
DR   SignaLink; Q5VZY2; -.
DR   UniPathway; UPA00085; -.
DR   BioGRID-ORCS; 196051; 16 hits in 1113 CRISPR screens.
DR   ChiTaRS; PLPP4; human.
DR   GeneWiki; PPAPDC1A; -.
DR   GenomeRNAi; 196051; -.
DR   Pharos; Q5VZY2; Tbio.
DR   PRO; PR:Q5VZY2; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q5VZY2; Protein.
DR   Bgee; ENSG00000203805; Expressed in oocyte and 127 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0090279; P:regulation of calcium ion import; IMP:UniProtKB.
DR   CDD; cd03390; PAP2_containing_1_like; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF90; PHOSPHOLIPID PHOSPHATASE 4; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   Genevisible; Q5VZY2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Phospholipid phosphatase 4"
FT                   /id="PRO_0000286943"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          102..110
FT                   /note="Phosphatase sequence motif I"
FT                   /evidence="ECO:0000269|PubMed:17590538"
FT   REGION          143..146
FT                   /note="Phosphatase sequence motif II"
FT                   /evidence="ECO:0000269|PubMed:17590538"
FT   REGION          195..205
FT                   /note="Phosphatase sequence motif III"
FT                   /evidence="ECO:0000269|PubMed:17590538"
FT   REGION          250..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Proton donors"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   ACT_SITE        202
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   SITE            206
FT                   /note="Stabilizes the active site histidine for
FT                   nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   VAR_SEQ         1..189
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025237"
FT   VAR_SEQ         56..96
FT                   /note="AISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGV -> IPLWVES
FT                   SASFLHTFATDSTILLWPTQLAINPTLVCESQPH (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025239"
FT   VAR_SEQ         86..149
FT                   /note="AVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVMNSEMHCTGDPDLVSE
FT                   GRKSFPSIHSSF -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025238"
FT   VAR_SEQ         97..271
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025240"
FT   MUTAGEN         109
FT                   /note="R->A: Loss of phosphatase activity; when associated
FT                   with A-146 and with A-202."
FT                   /evidence="ECO:0000269|PubMed:17590538"
FT   MUTAGEN         146
FT                   /note="H->A: Loss of phosphatase activity; when associated
FT                   with A-109 and with A-202."
FT                   /evidence="ECO:0000269|PubMed:17590538"
FT   MUTAGEN         202
FT                   /note="H->A: Loss of phosphatase activity; when associated
FT                   with A-109 and with A-146."
FT                   /evidence="ECO:0000269|PubMed:17590538"
SQ   SEQUENCE   271 AA;  30395 MW;  C534549E44DDB9A1 CRC64;
     MRELAIEIGV RALLFGVFVF TEFLDPFQRV IQPEEIWLYK NPLVQSDNIP TRLMFAISFL
     TPLAVICVVK IIRRTDKTEI KEAFLAVSLA LALNGVCTNT IKLIVGRPRP DFFYRCFPDG
     VMNSEMHCTG DPDLVSEGRK SFPSIHSSFA FSGLGFTTFY LAGKLHCFTE SGRGKSWRLC
     AAILPLYCAM MIALSRMCDY KHHWQDSFVG GVIGLIFAYI CYRQHYPPLA NTACHKPYVS
     LRVPASLKKE ERPTADSAPS LPLEGITEGP V
//