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
//
