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Protein

Tartrate-resistant acid phosphatase type 5

Gene

Acp5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi35Iron 11
Metal bindingi73Iron 11
Metal bindingi73Iron 21
Metal bindingi76Iron 11
Metal bindingi112Iron 21
Metal bindingi207Iron 21
Metal bindingi242Iron 21
Metal bindingi244Iron 11

GO - Molecular functioni

  • acid phosphatase activity Source: RGD
  • ferric iron binding Source: UniProtKB
  • ferrous iron binding Source: UniProtKB
  • hydrolase activity Source: RGD

GO - Biological processi

  • bone resorption Source: RGD
  • multicellular organismal response to stress Source: RGD
  • negative regulation of cell adhesion Source: RGD
  • ossification Source: RGD
  • osteoclast differentiation Source: RGD
  • positive regulation of cell migration Source: RGD
  • response to cholesterol Source: RGD
  • response to L-ascorbic acid Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to zinc ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-196843. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi2022. Acp5.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • integral component of membrane Source: RGD
  • lysosome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000002398523 – 327Tartrate-resistant acid phosphatase type 5Add BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi118N-linked (GlcNAc...)1
Glycosylationi149N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi163 ↔ 221

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP29288.
PRIDEiP29288.

Miscellaneous databases

PMAP-CutDBP29288.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000046261.
ExpressionAtlasiP29288. baseline and differential.
GenevisibleiP29288. RN.

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 interactor.
MINTiMINT-8283229.
STRINGi10116.ENSRNOP00000066364.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 33Combined sources6
Beta strandi40 – 44Combined sources5
Helixi47 – 63Combined sources17
Beta strandi66 – 70Combined sources5
Turni76 – 78Combined sources3
Turni83 – 85Combined sources3
Helixi87 – 90Combined sources4
Turni91 – 95Combined sources5
Helixi99 – 101Combined sources3
Helixi114 – 116Combined sources3
Helixi119 – 124Combined sources6
Helixi125 – 127Combined sources3
Beta strandi130 – 133Combined sources4
Beta strandi136 – 144Combined sources9
Beta strandi146 – 148Combined sources3
Beta strandi151 – 156Combined sources6
Helixi159 – 163Combined sources5
Helixi166 – 168Combined sources3
Helixi180 – 194Combined sources15
Beta strandi200 – 205Combined sources6
Beta strandi214 – 216Combined sources3
Helixi220 – 225Combined sources6
Helixi227 – 233Combined sources7
Beta strandi237 – 240Combined sources4
Beta strandi242 – 250Combined sources9
Beta strandi256 – 260Combined sources5
Beta strandi262 – 264Combined sources3
Helixi273 – 275Combined sources3
Beta strandi281 – 285Combined sources5
Beta strandi293 – 299Combined sources7
Beta strandi301 – 310Combined sources10
Beta strandi315 – 322Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFCX-ray2.70A22-327[»]
1QHWX-ray2.20A1-327[»]
ProteinModelPortaliP29288.
SMRiP29288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29288.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2679. Eukaryota.
COG1409. LUCA.
GeneTreeiENSGT00390000016735.
HOVERGENiHBG000433.
InParanoidiP29288.
KOiK14379.
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_006242692.3.
XP_006242755.1. XM_006242693.3.
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.
PIRiA41720.
RefSeqiNP_001257818.1. NM_001270889.1.
NP_062017.2. NM_019144.2.
XP_006242754.1. XM_006242692.3.
XP_006242755.1. XM_006242693.3.
XP_006242756.1. XM_006242694.2.
UniGeneiRn.171928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFCX-ray2.70A22-327[»]
1QHWX-ray2.20A1-327[»]
ProteinModelPortaliP29288.
SMRiP29288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29288. 1 interactor.
MINTiMINT-8283229.
STRINGi10116.ENSRNOP00000066364.

Proteomic databases

PaxDbiP29288.
PRIDEiP29288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54.
RGDi2022. Acp5.

Phylogenomic databases

eggNOGiKOG2679. Eukaryota.
COG1409. LUCA.
GeneTreeiENSGT00390000016735.
HOVERGENiHBG000433.
InParanoidiP29288.
KOiK14379.
PhylomeDBiP29288.

Enzyme and pathway databases

ReactomeiR-RNO-196843. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

EvolutionaryTraceiP29288.
PMAP-CutDBP29288.
PROiP29288.

Gene expression databases

BgeeiENSRNOG00000046261.
ExpressionAtlasiP29288. baseline and differential.
GenevisibleiP29288. RN.

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.
ProtoNetiSearch...

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 30, 2016
This is version 125 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

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.