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Prostatic acid phosphatase (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (Fluoride-resistant acid phosphatase) (FRAP) (Thiamine monophosphatase) (TMPase)

 PPAP_RAT                Reviewed;         381 AA.
P20646; A6XJQ5;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
23-MAY-2018, entry version 126.
RecName: Full=Prostatic acid phosphatase;
EC=3.1.3.2;
AltName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
AltName: Full=Ecto-5'-nucleotidase;
AltName: Full=Fluoride-resistant acid phosphatase;
Short=FRAP;
AltName: Full=Thiamine monophosphatase;
Short=TMPase;
Flags: Precursor;
Name=Acpp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=2373368; DOI=10.1016/0378-1119(90)90009-G;
Roiko K., Jaenne O.A., Vihko P.;
"Primary structure of rat secretory acid phosphatase and comparison to
other acid phosphatases.";
Gene 89:223-229(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
PubMed=17638863; DOI=10.1158/0008-5472.CAN-07-1651;
Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M.,
Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J.,
Hirvikoski P.P., Vihko P.T.;
"Prostatic acid phosphatase is not a prostate specific target.";
Cancer Res. 67:6549-6554(2007).
[3]
TISSUE SPECIFICITY.
PubMed=2421214; DOI=10.1016/0304-3940(86)90346-0;
McMahon S.B.;
"The localization of fluoride-resistant acid phosphatase (FRAP) in the
pelvic nerves and sacral spinal cord of rats.";
Neurosci. Lett. 64:305-310(1986).
[4]
ACTIVE SITE, SUBUNIT, ENZYME REGULATION, SUBSTRATE SPECIFICITY, AND
MUTAGENESIS OF TRP-137; HIS-143; TYR-154; ARG-158 AND ASP-289.
PubMed=8077215;
Porvari K.S., Herrala A.M., Kurkela R.M., Taavitsainen P.A.,
Lindqvist Y., Schneider G., Vihko P.T.;
"Site-directed mutagenesis of prostatic acid phosphatase.
Catalytically important aspartic acid 258, substrate specificity, and
oligomerization.";
J. Biol. Chem. 269:22642-22646(1994).
[5]
TISSUE SPECIFICITY.
PubMed=20084276; DOI=10.1371/journal.pone.0008674;
Taylor-Blake B., Zylka M.J.;
"Prostatic acid phosphatase is expressed in peptidergic and
nonpeptidergic nociceptive neurons of mice and rats.";
PLoS ONE 5:E8674-E8674(2010).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT, AND GLYCOSYLATION AT
ASN-93 AND ASN-332.
PubMed=8334986;
Schneider G., Lindqvist Y., Vihko P.;
"Three-dimensional structure of rat acid phosphatase.";
EMBO J. 12:2609-2615(1993).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH L(+)-TARTRATE,
AND GLYCOSYLATION AT ASN-93 AND ASN-332.
PubMed=8407898;
Lindqvist Y., Schneider G., Vihko P.;
"Three-dimensional structure of rat acid phosphatase in complex with
L(+)-tartrate.";
J. Biol. Chem. 268:20744-20746(1993).
-!- FUNCTION: A non-specific tyrosine phosphatase that
dephosphorylates a diverse number of substrates under acidic
conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate
monoesters and phosphorylated proteins. Has lipid phosphatase
activity and inactivates lysophosphatidic acid in seminal plasma
(By similarity). {ECO:0000250}.
-!- FUNCTION: Isoform 2: the cellular form also has ecto-5'-
nucleotidase activity in dorsal root ganglion (DRG) neurons.
Generates adenosine from AMP which acts as a pain suppressor.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- ENZYME REGULATION: Inhibited by L(+)-tartrate.
{ECO:0000269|PubMed:8077215}.
-!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
activity. {ECO:0000269|PubMed:8077215, ECO:0000269|PubMed:8334986,
ECO:0000269|PubMed:8407898}.
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted
{ECO:0000250|UniProtKB:P15309}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000250|UniProtKB:P15309}; Single-pass type I membrane
protein {ECO:0000255}. Lysosome membrane
{ECO:0000250|UniProtKB:P15309}; Single-pass type I membrane
protein {ECO:0000255}. Note=Appears to shuttle between the cell
membrane and intracellular vesicles. Colocalizes with FLOT1 at
cell membrane and in intracellular vesicles. Colocalizes with
LAMP2 on the lysosome membrane. {ECO:0000250|UniProtKB:P15309}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20646-1; Sequence=Displayed;
Name=2; Synonyms=TMPase, TM-PAP, cellular PAP, cPAP;
IsoId=P20646-2; Sequence=VSP_036025;
-!- TISSUE SPECIFICITY: Expressed in prostate epithelium. Also
expressed in the pelvic nerve and sacral spinal cord. Localizes in
peptidergic and non-peptidergic nociceptive (pain-sensing)
neurons. {ECO:0000269|PubMed:20084276,
ECO:0000269|PubMed:2421214}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8334986,
ECO:0000269|PubMed:8407898}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M32397; AAA41806.1; -; mRNA.
EMBL; DQ826426; ABH07387.1; -; mRNA.
PIR; JH0152; JH0152.
RefSeq; NP_001128373.1; NM_001134901.1.
RefSeq; NP_064457.1; NM_020072.1. [P20646-1]
UniGene; Rn.40121; -.
PDB; 1RPA; X-ray; 3.00 A; A=32-373.
PDB; 1RPT; X-ray; 3.00 A; A=32-373.
PDBsum; 1RPA; -.
PDBsum; 1RPT; -.
ProteinModelPortal; P20646; -.
SMR; P20646; -.
STRING; 10116.ENSRNOP00000016222; -.
iPTMnet; P20646; -.
PaxDb; P20646; -.
PRIDE; P20646; -.
GeneID; 56780; -.
KEGG; rno:56780; -.
UCSC; RGD:2023; rat. [P20646-1]
CTD; 55; -.
RGD; 2023; Acpp.
eggNOG; KOG3720; Eukaryota.
eggNOG; ENOG410ZVBQ; LUCA.
HOGENOM; HOG000231439; -.
HOVERGEN; HBG002203; -.
InParanoid; P20646; -.
KO; K19283; -.
PhylomeDB; P20646; -.
TreeFam; TF312893; -.
EvolutionaryTrace; P20646; -.
PRO; PR:P20646; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0031985; C:Golgi cisterna; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005771; C:multivesicular body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-EC.
GO; GO:0003993; F:acid phosphatase activity; IDA:RGD.
GO; GO:0033265; F:choline binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:RGD.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane;
Reference proteome; Secreted; Signal.
SIGNAL 1 31
CHAIN 32 381 Prostatic acid phosphatase.
/FTId=PRO_0000023964.
ACT_SITE 43 43 Nucleophile.
{ECO:0000269|PubMed:8077215}.
ACT_SITE 289 289 Proton donor.
{ECO:0000305|PubMed:8077215}.
BINDING 42 42 Substrate. {ECO:0000250}.
BINDING 46 46 Substrate. {ECO:0000250}.
BINDING 110 110 Substrate. {ECO:0000250}.
BINDING 288 288 Substrate. {ECO:0000250}.
SITE 48 48 Important for substrate specificity.
{ECO:0000250}.
SITE 137 137 Required for dimerization.
SITE 143 143 Required for dimerization.
SITE 205 205 Required for structural stability.
{ECO:0000250}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8334986,
ECO:0000269|PubMed:8407898}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8334986,
ECO:0000269|PubMed:8407898}.
DISULFID 160 371
DISULFID 214 312 {ECO:0000250}.
DISULFID 346 350
VAR_SEQ 379 381 ASL -> VLRVILATTFCLVTGILVILLLVLIRHGPCWQRD
VYRNI (in isoform 2).
{ECO:0000303|PubMed:17638863}.
/FTId=VSP_036025.
MUTAGEN 137 137 W->E: Abolishes most of enzyme activity
and dimer formation. No enzyme activity
nor dimer formation; when associated with
D-143. {ECO:0000269|PubMed:8077215}.
MUTAGEN 143 143 H->D: Abolishes most of enzyme activity
and dimer formation. No enzyme activity
nor dimer formation; when associated with
E-137. {ECO:0000269|PubMed:8077215}.
MUTAGEN 154 154 Y->K: PH optimum at 5.4 as for wild type
and no change in specific activity. Lower
pH maximum around 4.5 and more sensitive
to L(+)tartrate inhibition but no change
in specific activity; when associated
with G-158. {ECO:0000269|PubMed:8077215}.
MUTAGEN 158 158 R->G: Broader pH maximum levels around
5.4 but no change in specific activity.
Lower pH maximum around 4.5 and more
sensitive to L(+)tartrate inhibition but
no change in specific activity; when
associated with K-154.
{ECO:0000269|PubMed:8077215}.
MUTAGEN 289 289 D->A,S: Abolishes almost all enzyme
activity. {ECO:0000269|PubMed:8077215}.
MUTAGEN 289 289 D->N: Abolishes enzyme activity.
{ECO:0000269|PubMed:8077215}.
CONFLICT 222 223 FR -> LP (in Ref. 2; ABH07387).
{ECO:0000305}.
CONFLICT 288 288 Y -> H (in Ref. 2; ABH07387).
{ECO:0000305}.
CONFLICT 300 301 EL -> DV (in Ref. 2; ABH07387).
{ECO:0000305}.
CONFLICT 324 324 T -> H (in Ref. 2; ABH07387).
{ECO:0000305}.
STRAND 33 42 {ECO:0000244|PDB:1RPA}.
HELIX 59 61 {ECO:0000244|PDB:1RPA}.
STRAND 62 64 {ECO:0000244|PDB:1RPA}.
HELIX 71 88 {ECO:0000244|PDB:1RPA}.
HELIX 90 92 {ECO:0000244|PDB:1RPA}.
TURN 98 100 {ECO:0000244|PDB:1RPA}.
STRAND 102 105 {ECO:0000244|PDB:1RPA}.
HELIX 109 122 {ECO:0000244|PDB:1RPA}.
HELIX 127 129 {ECO:0000244|PDB:1RPA}.
HELIX 147 149 {ECO:0000244|PDB:1RPA}.
STRAND 152 154 {ECO:0000244|PDB:1RPA}.
HELIX 161 172 {ECO:0000244|PDB:1RPA}.
HELIX 174 180 {ECO:0000244|PDB:1RPA}.
HELIX 181 183 {ECO:0000244|PDB:1RPA}.
HELIX 184 189 {ECO:0000244|PDB:1RPA}.
HELIX 191 194 {ECO:0000244|PDB:1RPA}.
HELIX 201 207 {ECO:0000244|PDB:1RPA}.
HELIX 209 216 {ECO:0000244|PDB:1RPA}.
TURN 217 219 {ECO:0000244|PDB:1RPA}.
HELIX 228 246 {ECO:0000244|PDB:1RPA}.
STRAND 247 250 {ECO:0000244|PDB:1RPA}.
HELIX 251 256 {ECO:0000244|PDB:1RPA}.
HELIX 259 272 {ECO:0000244|PDB:1RPA}.
STRAND 275 277 {ECO:0000244|PDB:1RPT}.
STRAND 281 287 {ECO:0000244|PDB:1RPA}.
HELIX 289 299 {ECO:0000244|PDB:1RPA}.
STRAND 312 319 {ECO:0000244|PDB:1RPA}.
STRAND 321 331 {ECO:0000244|PDB:1RPA}.
STRAND 334 336 {ECO:0000244|PDB:1RPT}.
STRAND 348 351 {ECO:0000244|PDB:1RPA}.
HELIX 352 359 {ECO:0000244|PDB:1RPA}.
TURN 360 362 {ECO:0000244|PDB:1RPA}.
HELIX 367 371 {ECO:0000244|PDB:1RPA}.
SEQUENCE 381 AA; 43850 MW; 5EEBFF67B062FF76 CRC64;
MRAVPLHLVG TASLTLGFLL LLSLRLDPGQ AKELKFVTLV FRHGDRGPIE TFPNDPIKES
SWPQGFGQLT KWGMGQHYEL GSYIRRRYGR FLNNSYKHDQ VYIRSTDVDR TLMSAMTNLA
ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFQELKSET LKSEEFLKRL
QPYKSFIDTL PSLSGFEDQD LFEIWSRLYD PLYCESVHNF TFRTWATEDA MTKLKELSEL
SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKAR KLIMYSAYDT TVSGLQMALE
LYNGLLPPYA SCHIMELYQD NGGTFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD
PVIPQDWATE CMGTSNHQAS L


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