Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20646

- PPAP_RAT

UniProt

P20646 - PPAP_RAT

Protein

Prostatic acid phosphatase

Gene

Acpp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. adenosine metabolic process Source: Ensembl
    2. dephosphorylation Source: RGD
    3. nucleotide metabolic process Source: Ensembl
    4. purine nucleobase metabolic process Source: Ensembl

    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 region Source: UniProtKB-SubCell
    3. filopodium Source: Ensembl
    4. Golgi cisterna Source: RGD
    5. integral component of membrane Source: Ensembl
    6. lysosomal membrane Source: UniProtKB-SubCell
    7. multivesicular body Source: RGD
    8. plasma membrane Source: UniProtKB-SubCell
    9. secretory granule Source: RGD

    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

    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 – 4210
    Helixi59 – 613
    Beta strandi62 – 643
    Helixi71 – 8818
    Helixi90 – 923
    Turni98 – 1003
    Beta strandi102 – 1054
    Helixi109 – 12214
    Helixi127 – 1293
    Helixi147 – 1493
    Beta strandi152 – 1543
    Helixi161 – 17212
    Helixi174 – 1807
    Helixi181 – 1833
    Helixi184 – 1896
    Helixi191 – 1944
    Helixi201 – 2077
    Helixi209 – 2168
    Turni217 – 2193
    Helixi228 – 24619
    Beta strandi247 – 2504
    Helixi251 – 2566
    Helixi259 – 27214
    Beta strandi275 – 2773
    Beta strandi281 – 2877
    Helixi289 – 29911
    Beta strandi312 – 3198
    Beta strandi321 – 33111
    Beta strandi334 – 3363
    Beta strandi348 – 3514
    Helixi352 – 3598
    Turni360 – 3623
    Helixi367 – 3715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InParanoidiA6XJQ5.
    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

    MRAVPLHLVG TASLTLGFLL LLSLRLDPGQ AKELKFVTLV FRHGDRGPIE    50
    TFPNDPIKES SWPQGFGQLT KWGMGQHYEL GSYIRRRYGR FLNNSYKHDQ 100
    VYIRSTDVDR TLMSAMTNLA ALFPPEGISI WNPRLLWQPI PVHTVSLSED 150
    RLLYLPFRDC PRFQELKSET LKSEEFLKRL QPYKSFIDTL PSLSGFEDQD 200
    LFEIWSRLYD PLYCESVHNF TFRTWATEDA MTKLKELSEL SLLSLYGIHK 250
    QKEKSRLQGG VLVNEILKNM KLATQPQKAR KLIMYSAYDT TVSGLQMALE 300
    LYNGLLPPYA SCHIMELYQD NGGTFVEMYY RNETQNEPYP LTLPGCTHSC 350
    PLEKFAELLD PVIPQDWATE CMGTSNHQAS L 381
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 A6XJQ5.
    KOi K14410.
    OrthoDBi EOG7GXPBJ.
    PhylomeDBi P20646.
    TreeFami TF312893.

    Miscellaneous databases

    EvolutionaryTracei P20646.
    NextBioi 611179.
    PROi P20646.

    Gene expression databases

    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: October 1, 2014
    This is version 103 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