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Protein

Prostatic acid phosphatase

Gene

Acpp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei42SubstrateBy similarity1
Active sitei43Nucleophile1 Publication1
Binding sitei46SubstrateBy similarity1
Sitei48Important for substrate specificityBy similarity1
Binding sitei110SubstrateBy similarity1
Sitei137Required for dimerization1
Sitei143Required for dimerization1
Sitei205Required for structural stabilityBy similarity1
Binding sitei288SubstrateBy similarity1
Active sitei289Proton donor1 Publication1

GO - Molecular functioni

  • 5'-nucleotidase activity Source: UniProtKB-EC
  • acid phosphatase activity Source: RGD
  • choline binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation Source: RGD
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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2023. Acpp.

Subcellular locationi

Isoform 1 :
  • Secreted By similarity
Isoform 2 :
  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Lysosome membrane By similarity; Single-pass type I membrane protein Sequence analysis

  • 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

GO - Cellular componenti

  • apical part of cell Source: RGD
  • extracellular region Source: UniProtKB-SubCell
  • Golgi cisterna Source: RGD
  • lysosomal membrane Source: UniProtKB-SubCell
  • multivesicular body Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lysosome, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137W → E: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with D-143. 1 Publication1
Mutagenesisi143H → D: Abolishes most of enzyme activity and dimer formation. No enzyme activity nor dimer formation; when associated with E-137. 1 Publication1
Mutagenesisi154Y → 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 Publication1
Mutagenesisi158R → 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 Publication1
Mutagenesisi289D → A or S: Abolishes almost all enzyme activity. 1 Publication1
Mutagenesisi289D → N: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000002396432 – 381Prostatic acid phosphataseAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi93N-linked (GlcNAc...)2 Publications1
Disulfide bondi160 ↔ 371
Disulfide bondi214 ↔ 312By similarity
Glycosylationi219N-linked (GlcNAc...)Sequence analysis1
Glycosylationi332N-linked (GlcNAc...)2 Publications1
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

BgeeiENSRNOG00000011820.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016222.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 42Combined sources10
Helixi59 – 61Combined sources3
Beta strandi62 – 64Combined sources3
Helixi71 – 88Combined sources18
Helixi90 – 92Combined sources3
Turni98 – 100Combined sources3
Beta strandi102 – 105Combined sources4
Helixi109 – 122Combined sources14
Helixi127 – 129Combined sources3
Helixi147 – 149Combined sources3
Beta strandi152 – 154Combined sources3
Helixi161 – 172Combined sources12
Helixi174 – 180Combined sources7
Helixi181 – 183Combined sources3
Helixi184 – 189Combined sources6
Helixi191 – 194Combined sources4
Helixi201 – 207Combined sources7
Helixi209 – 216Combined sources8
Turni217 – 219Combined sources3
Helixi228 – 246Combined sources19
Beta strandi247 – 250Combined sources4
Helixi251 – 256Combined sources6
Helixi259 – 272Combined sources14
Beta strandi275 – 277Combined sources3
Beta strandi281 – 287Combined sources7
Helixi289 – 299Combined sources11
Beta strandi312 – 319Combined sources8
Beta strandi321 – 331Combined sources11
Beta strandi334 – 336Combined sources3
Beta strandi348 – 351Combined sources4
Helixi352 – 359Combined sources8
Turni360 – 362Combined sources3
Helixi367 – 371Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20646.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3720. Eukaryota.
ENOG410ZVBQ. LUCA.
HOGENOMiHOG000231439.
HOVERGENiHBG002203.
InParanoidiP20646.
KOiK19283.
PhylomeDBiP20646.
TreeFamiTF312893.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti222 – 223FR → LP in ABH07387 (PubMed:17638863).Curated2
Sequence conflicti288Y → H in ABH07387 (PubMed:17638863).Curated1
Sequence conflicti300 – 301EL → DV in ABH07387 (PubMed:17638863).Curated2
Sequence conflicti324T → H in ABH07387 (PubMed:17638863).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036025379 – 381ASL → VLRVILATTFCLVTGILVIL LLVLIRHGPCWQRDVYRNI in isoform 2. 1 Publication3

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

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.
PIRiJH0152.
RefSeqiNP_001128373.1. NM_001134901.1.
NP_064457.1. NM_020072.1. [P20646-1]
UniGeneiRn.40121.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016222.

Proteomic databases

PaxDbiP20646.
PRIDEiP20646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56780.
KEGGirno:56780.
UCSCiRGD:2023. rat. [P20646-1]

Organism-specific databases

CTDi55.
RGDi2023. Acpp.

Phylogenomic databases

eggNOGiKOG3720. Eukaryota.
ENOG410ZVBQ. LUCA.
HOGENOMiHOG000231439.
HOVERGENiHBG002203.
InParanoidiP20646.
KOiK19283.
PhylomeDBiP20646.
TreeFamiTF312893.

Miscellaneous databases

EvolutionaryTraceiP20646.
PROiP20646.

Gene expression databases

BgeeiENSRNOG00000011820.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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]
ProtoNetiSearch...

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 2, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.