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P20646

- PPAP_RAT

UniProt

P20646 - PPAP_RAT

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Protein

Prostatic acid phosphatase

Gene

Acpp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).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 activityi

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

Enzyme regulationi

Inhibited by L+-tartrate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421SubstrateBy similarity
Active sitei43 – 431Nucleophile1 Publication
Binding sitei46 – 461SubstrateBy similarity
Sitei48 – 481Important for substrate specificityBy similarity
Binding sitei110 – 1101SubstrateBy similarity
Sitei137 – 1371Required for dimerization
Sitei143 – 1431Required for dimerization
Sitei205 – 2051Required for structural stabilityBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Active sitei289 – 2891Proton donor1 Publication

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: UniProtKB-EC
  2. acid phosphatase activity Source: RGD
  3. choline binding Source: RGD
  4. lysophosphatidic acid phosphatase activity Source: Ensembl
  5. protein homodimerization activity Source: UniProtKB
  6. thiamine phosphate phosphatase activity Source: Ensembl

GO - Biological processi

  1. adenosine metabolic process Source: Ensembl
  2. dephosphorylation Source: RGD
  3. nucleotide metabolic process Source: Ensembl
  4. positive regulation of adenosine receptor signaling pathway Source: Ensembl
  5. purine nucleobase metabolic process Source: Ensembl
  6. regulation of sensory perception of pain Source: Ensembl
  7. thiamine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Prostatic acid phosphatase (EC:3.1.3.2)
Alternative name(s):
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Ecto-5'-nucleotidase
Fluoride-resistant acid phosphatase
Short name:
FRAP
Thiamine monophosphatase
Short name:
TMPase
Gene namesi
Name:Acpp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi2023. Acpp.

Subcellular locationi

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

GO - Cellular componenti

  1. apical part of cell Source: RGD
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. filopodium Source: Ensembl
  5. Golgi cisterna Source: RGD
  6. integral component of membrane Source: Ensembl
  7. lysosomal membrane Source: Ensembl
  8. multivesicular body Source: RGD
  9. nucleus Source: Ensembl
  10. plasma membrane Source: UniProtKB-KW
  11. secretory granule Source: RGD
  12. vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lysosome, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371W → E: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with D-143. 1 Publication
Mutagenesisi143 – 1431H → D: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with E-137. 1 Publication
Mutagenesisi154 – 1541Y → 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. 1 Publication
Mutagenesisi158 – 1581R → 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. 1 Publication
Mutagenesisi289 – 2891D → A or S: Abolishes almost all enzyme activity. 1 Publication
Mutagenesisi289 – 2891D → N: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 381350Prostatic acid phosphatasePRO_0000023964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)2 Publications
Disulfide bondi160 ↔ 371
Disulfide bondi214 ↔ 312By similarity
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)2 Publications
Disulfide bondi346 ↔ 350

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP20646.
PRIDEiP20646.

Expressioni

Tissue specificityi

Expressed in prostate epithelium. Also expressed in the pelvic nerve and sacral spinal cord. Localizes in peptidergic and non-peptidergic nociceptive (pain-sensing) neurons.2 Publications

Gene expression databases

ExpressionAtlasiP20646. baseline and differential.
GenevestigatoriP20646.

Interactioni

Subunit structurei

Homodimer; dimer formation is required for phosphatase activity.3 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016222.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 4210Combined sources
Helixi59 – 613Combined sources
Beta strandi62 – 643Combined sources
Helixi71 – 8818Combined sources
Helixi90 – 923Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1054Combined sources
Helixi109 – 12214Combined sources
Helixi127 – 1293Combined sources
Helixi147 – 1493Combined sources
Beta strandi152 – 1543Combined sources
Helixi161 – 17212Combined sources
Helixi174 – 1807Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 1896Combined sources
Helixi191 – 1944Combined sources
Helixi201 – 2077Combined sources
Helixi209 – 2168Combined sources
Turni217 – 2193Combined sources
Helixi228 – 24619Combined sources
Beta strandi247 – 2504Combined sources
Helixi251 – 2566Combined sources
Helixi259 – 27214Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi281 – 2877Combined sources
Helixi289 – 29911Combined sources
Beta strandi312 – 3198Combined sources
Beta strandi321 – 33111Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi348 – 3514Combined sources
Helixi352 – 3598Combined sources
Turni360 – 3623Combined sources
Helixi367 – 3715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPAX-ray3.00A32-373[»]
1RPTX-ray3.00A32-373[»]
ProteinModelPortaliP20646.
SMRiP20646. Positions 32-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20646.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85977.
GeneTreeiENSGT00530000062956.
HOGENOMiHOG000231439.
HOVERGENiHBG002203.
InParanoidiP20646.
KOiK14410.
OrthoDBiEOG7GXPBJ.
PhylomeDBiP20646.
TreeFamiTF312893.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20646-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRAVPLHLVG TASLTLGFLL LLSLRLDPGQ AKELKFVTLV FRHGDRGPIE
60 70 80 90 100
TFPNDPIKES SWPQGFGQLT KWGMGQHYEL GSYIRRRYGR FLNNSYKHDQ
110 120 130 140 150
VYIRSTDVDR TLMSAMTNLA ALFPPEGISI WNPRLLWQPI PVHTVSLSED
160 170 180 190 200
RLLYLPFRDC PRFQELKSET LKSEEFLKRL QPYKSFIDTL PSLSGFEDQD
210 220 230 240 250
LFEIWSRLYD PLYCESVHNF TFRTWATEDA MTKLKELSEL SLLSLYGIHK
260 270 280 290 300
QKEKSRLQGG VLVNEILKNM KLATQPQKAR KLIMYSAYDT TVSGLQMALE
310 320 330 340 350
LYNGLLPPYA SCHIMELYQD NGGTFVEMYY RNETQNEPYP LTLPGCTHSC
360 370 380
PLEKFAELLD PVIPQDWATE CMGTSNHQAS L
Length:381
Mass (Da):43,850
Last modified:February 1, 1991 - v1
Checksum:i5EEBFF67B062FF76
GO
Isoform 2 (identifier: P20646-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:417
Mass (Da):48,053
Checksum:i9B0877CC941A7A5A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2232FR → LP in ABH07387. (PubMed:17638863)Curated
Sequence conflicti288 – 2881Y → H in ABH07387. (PubMed:17638863)Curated
Sequence conflicti300 – 3012EL → DV in ABH07387. (PubMed:17638863)Curated
Sequence conflicti324 – 3241T → H in ABH07387. (PubMed:17638863)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei379 – 3813ASL → VLRVILATTFCLVTGILVIL LLVLIRHGPCWQRDVYRNI in isoform 2. 1 PublicationVSP_036025

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32397 mRNA. Translation: AAA41806.1.
DQ826426 mRNA. Translation: ABH07387.1.
PIRiJH0152.
RefSeqiNP_001128373.1. NM_001134901.1.
NP_064457.1. NM_020072.1. [P20646-1]
UniGeneiRn.40121.

Genome annotation databases

EnsembliENSRNOT00000016222; ENSRNOP00000016222; ENSRNOG00000011820.
GeneIDi56780.
KEGGirno:56780.
UCSCiRGD:2023. rat. [P20646-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32397 mRNA. Translation: AAA41806.1 .
DQ826426 mRNA. Translation: ABH07387.1 .
PIRi JH0152.
RefSeqi NP_001128373.1. NM_001134901.1.
NP_064457.1. NM_020072.1. [P20646-1 ]
UniGenei Rn.40121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RPA X-ray 3.00 A 32-373 [» ]
1RPT X-ray 3.00 A 32-373 [» ]
ProteinModelPortali P20646.
SMRi P20646. Positions 32-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000016222.

Proteomic databases

PaxDbi P20646.
PRIDEi P20646.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016222 ; ENSRNOP00000016222 ; ENSRNOG00000011820 .
GeneIDi 56780.
KEGGi rno:56780.
UCSCi RGD:2023. rat. [P20646-1 ]

Organism-specific databases

CTDi 55.
RGDi 2023. Acpp.

Phylogenomic databases

eggNOGi NOG85977.
GeneTreei ENSGT00530000062956.
HOGENOMi HOG000231439.
HOVERGENi HBG002203.
InParanoidi P20646.
KOi K14410.
OrthoDBi EOG7GXPBJ.
PhylomeDBi P20646.
TreeFami TF312893.

Miscellaneous databases

EvolutionaryTracei P20646.
NextBioi 611179.
PROi P20646.

Gene expression databases

ExpressionAtlasi P20646. baseline and differential.
Genevestigatori P20646.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Prostate.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH L(+)-TARTRATE, GLYCOSYLATION AT ASN-93 AND ASN-332.

Entry informationi

Entry nameiPPAP_RAT
AccessioniPrimary (citable) accession number: P20646
Secondary accession number(s): A6XJQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3