ID   PPAP_RAT                Reviewed;         381 AA.
AC   P20646; A0A0G2JSL5; A6XJQ5;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Prostatic acid phosphatase;
DE            EC=3.1.3.2 {ECO:0000269|PubMed:8077215};
DE   AltName: Full=5'-nucleotidase;
DE            Short=5'-NT;
DE            EC=3.1.3.5 {ECO:0000250|UniProtKB:P15309};
DE   AltName: Full=Acid phosphatase 3;
DE   AltName: Full=Ecto-5'-nucleotidase;
DE   AltName: Full=Fluoride-resistant acid phosphatase {ECO:0000303|PubMed:2421214};
DE            Short=FRAP {ECO:0000303|PubMed:2421214};
DE   AltName: Full=Protein tyrosine phosphatase ACP3;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P15309};
DE   AltName: Full=Thiamine monophosphatase;
DE            Short=TMPase;
DE   Flags: Precursor;
GN   Name=Acp3; Synonyms=Acpp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=2373368; DOI=10.1016/0378-1119(90)90009-g;
RA   Roiko K., Jaenne O.A., Vihko P.;
RT   "Primary structure of rat secretory acid phosphatase and comparison to
RT   other acid phosphatases.";
RL   Gene 89:223-229(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Sprague-Dawley;
RX   PubMed=17638863; DOI=10.1158/0008-5472.can-07-1651;
RA   Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M.,
RA   Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J.,
RA   Hirvikoski P.P., Vihko P.T.;
RT   "Prostatic acid phosphatase is not a prostate specific target.";
RL   Cancer Res. 67:6549-6554(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=2421214; DOI=10.1016/0304-3940(86)90346-0;
RA   McMahon S.B.;
RT   "The localization of fluoride-resistant acid phosphatase (FRAP) in the
RT   pelvic nerves and sacral spinal cord of rats.";
RL   Neurosci. Lett. 64:305-310(1986).
RN   [5]
RP   CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, SUBUNIT, ACTIVITY REGULATION,
RP   SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF TRP-137; HIS-143; TYR-154;
RP   ARG-158 AND ASP-289.
RX   PubMed=8077215; DOI=10.1016/s0021-9258(17)31694-0;
RA   Porvari K.S., Herrala A.M., Kurkela R.M., Taavitsainen P.A., Lindqvist Y.,
RA   Schneider G., Vihko P.T.;
RT   "Site-directed mutagenesis of prostatic acid phosphatase. Catalytically
RT   important aspartic acid 258, substrate specificity, and oligomerization.";
RL   J. Biol. Chem. 269:22642-22646(1994).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=20084276; DOI=10.1371/journal.pone.0008674;
RA   Taylor-Blake B., Zylka M.J.;
RT   "Prostatic acid phosphatase is expressed in peptidergic and nonpeptidergic
RT   nociceptive neurons of mice and rats.";
RL   PLoS ONE 5:E8674-E8674(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION AT ASN-93
RP   AND ASN-332.
RX   PubMed=8334986; DOI=10.1002/j.1460-2075.1993.tb05921.x;
RA   Schneider G., Lindqvist Y., Vihko P.;
RT   "Three-dimensional structure of rat acid phosphatase.";
RL   EMBO J. 12:2609-2615(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH L(+)-TARTRATE, AND
RP   GLYCOSYLATION AT ASN-93 AND ASN-332.
RX   PubMed=8407898; DOI=10.1016/s0021-9258(19)36845-0;
RA   Lindqvist Y., Schneider G., Vihko P.;
RT   "Three-dimensional structure of rat acid phosphatase in complex with L(+)-
RT   tartrate.";
RL   J. Biol. Chem. 268:20744-20746(1993).
CC   -!- FUNCTION: [Isoform 1]: A non-specific tyrosine phosphatase that
CC       dephosphorylates a diverse number of substrates under acidic conditions
CC       (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and
CC       phosphorylated proteins. Has lipid phosphatase activity and inactivates
CC       lysophosphatidic acid in seminal plasma. {ECO:0000269|PubMed:8077215}.
CC   -!- FUNCTION: [Isoform 2]: In addition to its tyrosine phosphatase
CC       activity, also has ecto-5'-nucleotidase activity in dorsal root
CC       ganglion (DRG) neurons. Generates adenosine from AMP. This
CC       extracellular adenosine leads to a decrease in chronic pain by
CC       activating A1R in nociceptive neurons. {ECO:0000250|UniProtKB:Q8CE08}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000269|PubMed:8077215};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000250|UniProtKB:Q8CE08};
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:0000250|UniProtKB:P15309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000250|UniProtKB:P15309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000250|UniProtKB:P15309};
CC   -!- ACTIVITY REGULATION: Inhibited by L(+)-tartrate.
CC       {ECO:0000269|PubMed:8077215}.
CC   -!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
CC       activity. {ECO:0000269|PubMed:8077215, ECO:0000269|PubMed:8334986,
CC       ECO:0000269|PubMed:8407898}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC       {ECO:0000250|UniProtKB:P15309}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC       {ECO:0000250|UniProtKB:P15309}; Single-pass type I membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P15309};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=Appears to
CC       shuttle between the cell membrane and intracellular vesicles.
CC       Colocalizes with FLOT1 at cell membrane and in intracellular vesicles.
CC       Colocalizes with LAMP2 on the lysosome membrane.
CC       {ECO:0000250|UniProtKB:P15309}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P20646-1; Sequence=Displayed;
CC       Name=2; Synonyms=TMPase, TM-PAP, cellular PAP, cPAP;
CC         IsoId=P20646-2; Sequence=VSP_036025;
CC   -!- TISSUE SPECIFICITY: Expressed in prostate epithelium. Also expressed in
CC       the pelvic nerve and sacral spinal cord. Localizes in peptidergic and
CC       non-peptidergic nociceptive (pain-sensing) neurons.
CC       {ECO:0000269|PubMed:20084276, ECO:0000269|PubMed:2421214}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8334986,
CC       ECO:0000269|PubMed:8407898}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; M32397; AAA41806.1; -; mRNA.
DR   EMBL; DQ826426; ABH07387.1; -; mRNA.
DR   EMBL; AABR07071383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JH0152; JH0152.
DR   RefSeq; NP_001128373.1; NM_001134901.1. [P20646-2]
DR   RefSeq; NP_064457.1; NM_020072.1. [P20646-1]
DR   PDB; 1RPA; X-ray; 3.00 A; A=32-373.
DR   PDB; 1RPT; X-ray; 3.00 A; A=32-373.
DR   PDBsum; 1RPA; -.
DR   PDBsum; 1RPT; -.
DR   AlphaFoldDB; P20646; -.
DR   SMR; P20646; -.
DR   STRING; 10116.ENSRNOP00000072975; -.
DR   GlyCosmos; P20646; 3 sites, No reported glycans.
DR   GlyGen; P20646; 3 sites.
DR   iPTMnet; P20646; -.
DR   PhosphoSitePlus; P20646; -.
DR   PaxDb; 10116-ENSRNOP00000016222; -.
DR   Ensembl; ENSRNOT00000016222.6; ENSRNOP00000016222.5; ENSRNOG00000011820.7. [P20646-1]
DR   Ensembl; ENSRNOT00000085585.2; ENSRNOP00000072975.1; ENSRNOG00000011820.7. [P20646-2]
DR   Ensembl; ENSRNOT00055022057; ENSRNOP00055017899; ENSRNOG00055012887. [P20646-1]
DR   Ensembl; ENSRNOT00060013250; ENSRNOP00060010062; ENSRNOG00060008023. [P20646-1]
DR   Ensembl; ENSRNOT00065012587; ENSRNOP00065009263; ENSRNOG00065007977. [P20646-1]
DR   GeneID; 56780; -.
DR   KEGG; rno:56780; -.
DR   UCSC; RGD:2023; rat. [P20646-1]
DR   AGR; RGD:2023; -.
DR   CTD; 55; -.
DR   RGD; 2023; Acp3.
DR   eggNOG; KOG3720; Eukaryota.
DR   GeneTree; ENSGT00940000160450; -.
DR   InParanoid; P20646; -.
DR   OMA; GMKQHYE; -.
DR   OrthoDB; 5489935at2759; -.
DR   PhylomeDB; P20646; -.
DR   TreeFam; TF312893; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   EvolutionaryTrace; P20646; -.
DR   PRO; PR:P20646; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000011820; Expressed in esophagus and 14 other cell types or tissues.
DR   GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0030175; C:filopodium; ISO:RGD.
DR   GO; GO:0031985; C:Golgi cisterna; IDA:RGD.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0030141; C:secretory granule; IDA:RGD.
DR   GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR   GO; GO:0008253; F:5'-nucleotidase activity; ISO:RGD.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:RGD.
DR   GO; GO:0033265; F:choline binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISO:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0016791; F:phosphatase activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042131; F:thiamine phosphate phosphatase activity; ISO:RGD.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046085; P:adenosine metabolic process; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IDA:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; ISO:RGD.
DR   GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; ISO:RGD.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
DR   GO; GO:0006772; P:thiamine metabolic process; ISO:RGD.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11567:SF32; PROSTATIC ACID PHOSPHATASE; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Hydrolase; Lipid metabolism; Lysosome; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   CHAIN           32..381
FT                   /note="Prostatic acid phosphatase"
FT                   /id="PRO_0000023964"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   ACT_SITE        289
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:8077215"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   SITE            48
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000250"
FT   SITE            137
FT                   /note="Required for dimerization"
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   SITE            143
FT                   /note="Required for dimerization"
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   SITE            205
FT                   /note="Required for structural stability"
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8334986,
FT                   ECO:0000269|PubMed:8407898"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8334986,
FT                   ECO:0000269|PubMed:8407898"
FT   DISULFID        160..371
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   DISULFID        214..312
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   DISULFID        346..350
FT                   /evidence="ECO:0000250|UniProtKB:P15309"
FT   VAR_SEQ         379..381
FT                   /note="ASL -> VLRVILATTFCLVTGILVILLLVLIRHGPCWQRDVYRNI (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17638863"
FT                   /id="VSP_036025"
FT   MUTAGEN         137
FT                   /note="W->E: Abolishes most of enzyme activity and dimer
FT                   formation. No enzyme activity nor dimer formation; when
FT                   associated with D-143."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   MUTAGEN         143
FT                   /note="H->D: Abolishes most of enzyme activity and dimer
FT                   formation. No enzyme activity nor dimer formation; when
FT                   associated with E-137."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   MUTAGEN         154
FT                   /note="Y->K: PH optimum at 5.4 as for wild type and no
FT                   change in specific activity. Lower pH maximum around 4.5
FT                   and more sensitive to L(+)tartrate inhibition but no change
FT                   in specific activity; when associated with G-158."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   MUTAGEN         158
FT                   /note="R->G: Broader pH maximum levels around 5.4 but no
FT                   change in specific activity. Lower pH maximum around 4.5
FT                   and more sensitive to L(+)tartrate inhibition but no change
FT                   in specific activity; when associated with K-154."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   MUTAGEN         289
FT                   /note="D->A,S: Abolishes almost all enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   MUTAGEN         289
FT                   /note="D->N: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:8077215"
FT   CONFLICT        222..223
FT                   /note="LP -> FR (in Ref. 1; AAA41806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="H -> Y (in Ref. 1; AAA41806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300..301
FT                   /note="DV -> EL (in Ref. 1; AAA41806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="H -> T (in Ref. 1; AAA41806)"
FT                   /evidence="ECO:0000305"
FT   STRAND          33..42
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           71..88
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           109..122
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           161..172
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           174..180
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           184..189
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           191..194
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           201..207
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           209..216
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           228..246
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          247..250
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           251..256
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           259..272
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:1RPT"
FT   STRAND          281..287
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           289..299
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          312..319
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          321..331
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:1RPT"
FT   STRAND          348..351
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           352..359
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   TURN            360..362
FT                   /evidence="ECO:0007829|PDB:1RPA"
FT   HELIX           367..371
FT                   /evidence="ECO:0007829|PDB:1RPA"
SQ   SEQUENCE   381 AA;  43739 MW;  2CDD713D44560FE4 CRC64;
     MRAVPLHLVG TASLTLGFLL LLSLRLDPGQ AKELKFVTLV FRHGDRGPIE TFPNDPIKES
     SWPQGFGQLT KWGMGQHYEL GSYIRRRYGR FLNNSYKHDQ VYIRSTDVDR TLMSAMTNLA
     ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFQELKSET LKSEEFLKRL
     QPYKSFIDTL PSLSGFEDQD LFEIWSRLYD PLYCESVHNF TLPTWATEDA MTKLKELSEL
     SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKAR KLIMYSAHDT TVSGLQMALD
     VYNGLLPPYA SCHIMELYQD NGGHFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD
     PVIPQDWATE CMGTSNHQAS L
//