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P20646 (PPAP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostatic acid phosphatase
EC=3.1.3.2
Alternative name(s):
5'-nucleotidase
Short name=5'-NT
EC=3.1.3.5
Ecto-5'-nucleotidase
Fluoride-resistant acid phosphatase
Short name=FRAP
Thiamine monophosphatase
Short name=TMPase
Gene names
Name:Acpp
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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 + H2O = an alcohol + phosphate.

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Enzyme regulation

Inhibited by L+-tartrate. Ref.4

Subunit structure

Homodimer; dimer formation is required for phosphatase activity. Ref.4 Ref.6

Subcellular location

Isoform 1: Secreted.

Isoform 2: Cell membrane; Single-pass type I membrane protein By similarity. Lysosome membrane; Single-pass type I membrane protein By similarity. 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 By similarity.

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. Ref.3 Ref.5

Post-translational modification

N-glycosylated. Ref.6 Ref.7

Sequence similarities

Belongs to the histidine acid phosphatase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20646-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20646-2)

Also known as: TMPase; TM-PAP; cellular PAP; cPAP;

The sequence of this isoform differs from the canonical sequence as follows:
     379-381: ASL → VLRVILATTFCLVTGILVILLLVLIRHGPCWQRDVYRNI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 381350Prostatic acid phosphatase
PRO_0000023964

Sites

Active site431Nucleophile Ref.4
Active site2891Proton donor Probable
Binding site421Substrate By similarity
Binding site461Substrate By similarity
Binding site1101Substrate By similarity
Binding site2881Substrate By similarity
Site481Important for substrate specificity By similarity
Site1371Required for dimerization
Site1431Required for dimerization
Site2051Required for structural stability By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Ref.6 Ref.7
Disulfide bond160 ↔ 371
Disulfide bond214 ↔ 312 By similarity
Disulfide bond346 ↔ 350

Natural variations

Alternative sequence379 – 3813ASL → VLRVILATTFCLVTGILVIL LLVLIRHGPCWQRDVYRNI in isoform 2.
VSP_036025

Experimental info

Mutagenesis1371W → E: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with D-143. Ref.4
Mutagenesis1431H → D: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with E-137. Ref.4
Mutagenesis1541Y → 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. Ref.4
Mutagenesis1581R → 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. Ref.4
Mutagenesis2891D → A or S: Abolishes almost all enzyme activity. Ref.4
Mutagenesis2891D → N: Abolishes enzyme activity. Ref.4
Sequence conflict222 – 2232FR → LP in ABH07387. Ref.2
Sequence conflict2881Y → H in ABH07387. Ref.2
Sequence conflict300 – 3012EL → DV in ABH07387. Ref.2
Sequence conflict3241T → H in ABH07387. Ref.2

Secondary structure

1 ....................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 5EEBFF67B062FF76

FASTA38143,850
        10         20         30         40         50         60 
MRAVPLHLVG TASLTLGFLL LLSLRLDPGQ AKELKFVTLV FRHGDRGPIE TFPNDPIKES 

        70         80         90        100        110        120 
SWPQGFGQLT KWGMGQHYEL GSYIRRRYGR FLNNSYKHDQ VYIRSTDVDR TLMSAMTNLA 

       130        140        150        160        170        180 
ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFQELKSET LKSEEFLKRL 

       190        200        210        220        230        240 
QPYKSFIDTL PSLSGFEDQD LFEIWSRLYD PLYCESVHNF TFRTWATEDA MTKLKELSEL 

       250        260        270        280        290        300 
SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKAR KLIMYSAYDT TVSGLQMALE 

       310        320        330        340        350        360 
LYNGLLPPYA SCHIMELYQD NGGTFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD 

       370        380 
PVIPQDWATE CMGTSNHQAS L

« Hide

Isoform 2 (TMPase) (TM-PAP) (cellular PAP) (cPAP) [UniParc].

Checksum: 9B0877CC941A7A5A
Show »

FASTA41748,053

References

[1]"Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases."
Roiko K., Jaenne O.A., Vihko P.
Gene 89:223-229(1990) [PubMed: 2373368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Prostate.
[2]"Prostatic acid phosphatase is not a prostate specific target."
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.
Cancer Res. 67:6549-6554(2007) [PubMed: 17638863] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: Sprague-Dawley.
[3]"The localization of fluoride-resistant acid phosphatase (FRAP) in the pelvic nerves and sacral spinal cord of rats."
McMahon S.B.
Neurosci. Lett. 64:305-310(1986) [PubMed: 2421214] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and oligomerization."
Porvari K.S., Herrala A.M., Kurkela R.M., Taavitsainen P.A., Lindqvist Y., Schneider G., Vihko P.T.
J. Biol. Chem. 269:22642-22646(1994) [PubMed: 8077215] [Abstract]
Cited for: ACTIVE SITE, SUBUNIT, ENZYME REGULATION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF TRP-137; HIS-143; TYR-154; ARG-158 AND ASP-289.
[5]"Prostatic acid phosphatase is expressed in peptidergic and nonpeptidergic nociceptive neurons of mice and rats."
Taylor-Blake B., Zylka M.J.
PLoS ONE 5:E8674-E8674(2010) [PubMed: 20084276] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Three-dimensional structure of rat acid phosphatase."
Schneider G., Lindqvist Y., Vihko P.
EMBO J. 12:2609-2615(1993) [PubMed: 8334986] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT, GLYCOSYLATION AT ASN-93 AND ASN-332.
[7]"Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate."
Lindqvist Y., Schneider G., Vihko P.
J. Biol. Chem. 268:20744-20746(1993) [PubMed: 8407898] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH L(+)-TARTRATE, GLYCOSYLATION AT ASN-93 AND ASN-332.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M32397 mRNA. Translation: AAA41806.1.
DQ826426 mRNA. Translation: ABH07387.1.
IPIIPI00201376.
IPI00914298.
PIRJH0152.
RefSeqNP_001128373.1. NM_001134901.1.
NP_064457.1. NM_020072.1.
UniGeneRn.40121.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPAX-ray3.00A32-373[»]
1RPTX-ray3.00A32-373[»]
ProteinModelPortalP20646.
SMRP20646. Positions 32-373.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20646.

Proteomic databases

PRIDEP20646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016222; ENSRNOP00000016222; ENSRNOG00000011820.
GeneID56780.
KEGGrno:56780.
UCSCNM_020072. rat.

Organism-specific databases

CTD55.
RGD2023. Acpp.

Phylogenomic databases

eggNOGroNOG04279.
HOVERGENHBG002203.
InParanoidP20646.

Gene expression databases

ArrayExpressP20646.
GenevestigatorP20646.
GermOnlineENSRNOG00000011820. Rattus norvegicus.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
[Graphical view]
KOK14410.
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio611179.

Entry information

Entry namePPAP_RAT
AccessionPrimary (citable) accession number: P20646
Secondary accession number(s): A6XJQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents