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P29288

- PPA5_RAT

UniProt

P29288 - PPA5_RAT

Protein

Tartrate-resistant acid phosphatase type 5

Gene

Acp5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    May play a role in the process of bone resorption. The osteoclastic trap acts on nucleotide tri- and diphosphates with higher affinity, compared with other substrates.

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.

    Cofactori

    Binds 2 iron ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi35 – 351Iron 1
    Metal bindingi73 – 731Iron 1
    Metal bindingi73 – 731Iron 2
    Metal bindingi76 – 761Iron 1
    Metal bindingi112 – 1121Iron 2
    Metal bindingi207 – 2071Iron 2
    Metal bindingi242 – 2421Iron 2
    Metal bindingi244 – 2441Iron 1

    GO - Molecular functioni

    1. acid phosphatase activity Source: RGD
    2. ferric iron binding Source: UniProtKB
    3. ferrous iron binding Source: UniProtKB
    4. hydrolase activity Source: RGD

    GO - Biological processi

    1. bone resorption Source: RGD
    2. dephosphorylation Source: GOC
    3. metabolic process Source: GOC
    4. multicellular organismal response to stress Source: RGD
    5. negative regulation of cell adhesion Source: RGD
    6. ossification Source: RGD
    7. osteoclast differentiation Source: RGD
    8. positive regulation of cell migration Source: RGD
    9. response to cholesterol Source: RGD
    10. response to L-ascorbic acid Source: RGD
    11. response to organic cyclic compound Source: RGD
    12. response to zinc ion Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tartrate-resistant acid phosphatase type 5 (EC:3.1.3.2)
    Short name:
    TR-AP
    Alternative name(s):
    Tartrate-resistant acid ATPase
    Short name:
    TrATPase
    Type 5 acid phosphatase
    Gene namesi
    Name:Acp5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi2022. Acp5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: RGD
    2. integral component of membrane Source: RGD
    3. lysosome Source: RGD

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 327305Tartrate-resistant acid phosphatase type 5PRO_0000023985Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi118 – 1181N-linked (GlcNAc...)
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi163 ↔ 221

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP29288.

    Miscellaneous databases

    PMAP-CutDBP29288.

    Expressioni

    Tissue specificityi

    Characteristic constituent of osteoclasts and some mononuclear preosteoclasts. Preferentially expressed in skeletal tissues.

    Gene expression databases

    ArrayExpressiP29288.
    GenevestigatoriP29288.

    Interactioni

    Subunit structurei

    Exists either as monomer or, after proteolytic processing, as a dimer of two chains linked by disulfide bond(s).

    Protein-protein interaction databases

    IntActiP29288. 1 interaction.
    MINTiMINT-8283229.

    Structurei

    Secondary structure

    1
    327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 336
    Beta strandi40 – 445
    Helixi47 – 6317
    Beta strandi66 – 705
    Turni76 – 783
    Turni83 – 853
    Helixi87 – 904
    Turni91 – 955
    Helixi99 – 1013
    Helixi114 – 1163
    Helixi119 – 1246
    Helixi125 – 1273
    Beta strandi130 – 1334
    Beta strandi136 – 1449
    Beta strandi146 – 1483
    Beta strandi151 – 1566
    Helixi159 – 1635
    Helixi166 – 1683
    Helixi180 – 19415
    Beta strandi200 – 2056
    Beta strandi214 – 2163
    Helixi220 – 2256
    Helixi227 – 2337
    Beta strandi237 – 2404
    Beta strandi242 – 2509
    Beta strandi256 – 2605
    Beta strandi262 – 2643
    Helixi273 – 2753
    Beta strandi281 – 2855
    Beta strandi293 – 2997
    Beta strandi301 – 31010
    Beta strandi315 – 3228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QFCX-ray2.70A22-327[»]
    1QHWX-ray2.20A1-327[»]
    ProteinModelPortaliP29288.
    SMRiP29288. Positions 26-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29288.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    GeneTreeiENSGT00390000016735.
    HOVERGENiHBG000433.
    KOiK14379.
    OMAiGEEMDIN.
    OrthoDBiEOG7WHH9R.
    PhylomeDBiP29288.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR024927. Acid_Pase_5.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000898. Acid_Ptase_5. 1 hit.
    SUPFAMiSSF56300. SSF56300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29288-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTWMVLLGL QILLLPLLAH CTAPASTLRF VAVGDWGGVP NAPFHTAREM    50
    ANAKEIARTV QIMGADFIMS LGDNFYFTGV HDANDKRFQE TFEDVFSDRA 100
    LRNIPWYVLA GNHDHLGNVS AQIAYSKISK RWNFPSPYYR LRFKVPRSNI 150
    TVAIFMLDTV MLCGNSDDFV SQQPEMPRDL GVARTQLSWL KKQLAAAKED 200
    YVLVAGHYPI WSIAEHGPTR CLVKNLRPLL AAYGVTAYLC GHDHNLQYLQ 250
    DENGVGYVLS GAGNFMDPSV RHQRKVPNGY LRFHYGSEDS LGGFTYVEIG 300
    SKEMSITYVE ASGKSLFKTS LPRRPRP 327
    Length:327
    Mass (Da):36,726
    Last modified:December 1, 1992 - v1
    Checksum:i5121A66A635ED854
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76110 mRNA. Translation: AAA42305.1.
    BC078847 mRNA. Translation: AAH78847.1.
    PIRiA41720.
    RefSeqiNP_001257818.1. NM_001270889.1.
    NP_062017.2. NM_019144.2.
    XP_006242754.1. XM_006242692.1.
    XP_006242755.1. XM_006242693.1.
    XP_006242756.1. XM_006242694.1.
    UniGeneiRn.171928.

    Genome annotation databases

    EnsembliENSRNOT00000075237; ENSRNOP00000066364; ENSRNOG00000046261.
    GeneIDi25732.
    KEGGirno:25732.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76110 mRNA. Translation: AAA42305.1 .
    BC078847 mRNA. Translation: AAH78847.1 .
    PIRi A41720.
    RefSeqi NP_001257818.1. NM_001270889.1.
    NP_062017.2. NM_019144.2.
    XP_006242754.1. XM_006242692.1.
    XP_006242755.1. XM_006242693.1.
    XP_006242756.1. XM_006242694.1.
    UniGenei Rn.171928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QFC X-ray 2.70 A 22-327 [» ]
    1QHW X-ray 2.20 A 1-327 [» ]
    ProteinModelPortali P29288.
    SMRi P29288. Positions 26-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P29288. 1 interaction.
    MINTi MINT-8283229.

    Proteomic databases

    PRIDEi P29288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000075237 ; ENSRNOP00000066364 ; ENSRNOG00000046261 .
    GeneIDi 25732.
    KEGGi rno:25732.

    Organism-specific databases

    CTDi 54.
    RGDi 2022. Acp5.

    Phylogenomic databases

    GeneTreei ENSGT00390000016735.
    HOVERGENi HBG000433.
    KOi K14379.
    OMAi GEEMDIN.
    OrthoDBi EOG7WHH9R.
    PhylomeDBi P29288.

    Miscellaneous databases

    EvolutionaryTracei P29288.
    NextBioi 607863.
    PMAP-CutDB P29288.
    PROi P29288.

    Gene expression databases

    ArrayExpressi P29288.
    Genevestigatori P29288.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR024927. Acid_Pase_5.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000898. Acid_Ptase_5. 1 hit.
    SUPFAMi SSF56300. SSF56300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone."
      Ek-Rylander B., Bill P., Norgaard M., Nilsson S., Andersson G.
      J. Biol. Chem. 266:24684-24689(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. "Characterization of a tartrate-resistant acid phosphatase (ATPase) from rat bone: hydrodynamic properties and N-terminal amino acid sequence."
      Ek-Rylander B., Bergman T., Andersson G.
      J. Bone Miner. Res. 6:365-373(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-42.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-327.
    5. "Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a gamma-(hydr)oxo bridged di-iron center."
      Lindqvist Y., Johansson E., Kaija H., Vihko P., Schneider G.
      J. Mol. Biol. 291:135-147(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiPPA5_RAT
    AccessioniPrimary (citable) accession number: P29288
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 109 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, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3