PLPP4_HUMAN
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 03-AUG-2022, entry version 136.
DE RecName: Full=Phospholipid phosphatase 4 {ECO:0000312|HGNC:HGNC:23531};
DE EC=3.1.3.4 {ECO:0000269|PubMed:17590538};
DE EC=3.1.3.81 {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},
GN PPAPDC1 {ECO:0000312|HGNC:HGNC:23531},
GN 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=3.1.3.81;
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 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate/lysophosphatidate {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; Q5VZY2; -.
DR PeptideAtlas; Q5VZY2; -.
DR PRIDE; Q5VZY2; -.
DR ProteomicsDB; 65736; -. [Q5VZY2-3]
DR Antibodypedia; 46311; 82 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 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; 1621899at2759; -.
DR PhylomeDB; Q5VZY2; -.
DR TreeFam; TF323722; -.
DR BioCyc; MetaCyc:G66-31698-MON; -.
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; 15 hits in 1029 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 125 other tissues.
DR Genevisible; Q5VZY2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR InterPro; IPR028668; PLPP4/5.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF90; PTHR10165:SF90; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
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
