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P29288

- PPA5_RAT

UniProt

P29288 - PPA5_RAT

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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

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

Fe cationNote: 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_249545. Vitamin B2 (riboflavin) metabolism.

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
Complete GO annotation...

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

ExpressionAtlasiP29288. baseline and differential.
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 – 336Combined sources
Beta strandi40 – 445Combined sources
Helixi47 – 6317Combined sources
Beta strandi66 – 705Combined sources
Turni76 – 783Combined sources
Turni83 – 853Combined sources
Helixi87 – 904Combined sources
Turni91 – 955Combined sources
Helixi99 – 1013Combined sources
Helixi114 – 1163Combined sources
Helixi119 – 1246Combined sources
Helixi125 – 1273Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi151 – 1566Combined sources
Helixi159 – 1635Combined sources
Helixi166 – 1683Combined sources
Helixi180 – 19415Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi214 – 2163Combined sources
Helixi220 – 2256Combined sources
Helixi227 – 2337Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi242 – 2509Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi262 – 2643Combined sources
Helixi273 – 2753Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi293 – 2997Combined sources
Beta strandi301 – 31010Combined sources
Beta strandi315 – 3228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP29288.
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

        10         20         30         40         50
MDTWMVLLGL QILLLPLLAH CTAPASTLRF VAVGDWGGVP NAPFHTAREM
60 70 80 90 100
ANAKEIARTV QIMGADFIMS LGDNFYFTGV HDANDKRFQE TFEDVFSDRA
110 120 130 140 150
LRNIPWYVLA GNHDHLGNVS AQIAYSKISK RWNFPSPYYR LRFKVPRSNI
160 170 180 190 200
TVAIFMLDTV MLCGNSDDFV SQQPEMPRDL GVARTQLSWL KKQLAAAKED
210 220 230 240 250
YVLVAGHYPI WSIAEHGPTR CLVKNLRPLL AAYGVTAYLC GHDHNLQYLQ
260 270 280 290 300
DENGVGYVLS GAGNFMDPSV RHQRKVPNGY LRFHYGSEDS LGGFTYVEIG
310 320
SKEMSITYVE ASGKSLFKTS LPRRPRP
Length:327
Mass (Da):36,726
Last modified:December 1, 1992 - v1
Checksum:i5121A66A635ED854
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006242692.2.
XP_006242755.1. XM_006242693.2.
XP_006242756.1. XM_006242694.2.
UniGeneiRn.171928.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006242692.2.
XP_006242755.1. XM_006242693.2.
XP_006242756.1. XM_006242694.2.
UniGenei Rn.171928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P29288.
KOi K14379.
OMAi GEEMDIN.
OrthoDBi EOG7WHH9R.
PhylomeDBi P29288.

Enzyme and pathway databases

Reactomei REACT_249545. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

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

Gene expression databases

ExpressionAtlasi P29288. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 111 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