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P11064 (PPAC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low molecular weight phosphotyrosine protein phosphatase

Short name=LMW-PTP
Short name=LMW-PTPase
EC=3.1.3.48
Alternative name(s):
Low molecular weight cytosolic acid phosphatase
EC=3.1.3.2
Gene names
Name:ACP1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphate monoester + H2O = an alcohol + phosphate.

Enzyme regulation

Inhibited by sulfhydryl reagents.

Subunit structure

Interacts with the SH3 domain of SPTAN1. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 158157Low molecular weight phosphotyrosine protein phosphatase
PRO_0000046557

Sites

Active site131Nucleophile Ref.3 Ref.4
Active site191 Ref.3 Ref.4
Active site1301Proton donor Ref.3 Ref.4

Amino acid modifications

Modified residue21N-acetylalanine Ref.1
Modified residue1321Phosphotyrosine By similarity
Modified residue1331Phosphotyrosine By similarity

Experimental info

Mutagenesis131C → A or S: Inactive. Ref.5
Mutagenesis181C → S: Greatly decreases activity. Ref.5
Mutagenesis631C → S: 2.5-fold increase in activity. Ref.5
Mutagenesis671H → E: Decreased activity. Ref.6 Ref.7
Mutagenesis731H → E: Decreased activity. Ref.6 Ref.7
Mutagenesis1461C → S: No effect on activity. Ref.5
Sequence conflict571D → N AA sequence Ref.2

Secondary structure

..................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11064 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5925D5048C42BE02

FASTA15818,055
        10         20         30         40         50         60 
MAEQVTKSVL FVCLGNICRS PIAEAVFRKL VTDQNISDNW VIDSGAVSDW NVGRSPDPRA 

        70         80         90        100        110        120 
VSCLRNHGIN TAHKARQVTK EDFVTFDYIL CMDESNLRDL NRKSNQVKNC RAKIELLGSY 

       130        140        150 
DPQKQLIIED PYYGNDADFE TVYQQCVRCC RAFLEKVR 

« Hide

References

[1]"Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart."
Wo Y.Y.P., Zhou M.M., Stevis P.E., Davis J.P., Zhang Z.Y., van Etten R.L.
Biochemistry 31:1712-1721(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase."
Camici G., Manao G., Cappugi G., Modesti A., Stefani M., Ramponi G.
J. Biol. Chem. 264:2560-2567(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-158.
Tissue: Liver.
[3]"The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-M(r) cytosolic phosphotyrosine protein phosphatase."
Cirri P., Chiarugi P., Camici G., Manao G., Raugei G., Cappugi G., Ramponi G.
Eur. J. Biochem. 214:647-657(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES.
[4]"Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase."
Davis J.P., Zhou M.M., van Etten R.L.
J. Biol. Chem. 269:8734-8740(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS.
[5]"Differential role of four cysteines on the activity of a low M(r) phosphotyrosine protein phosphatase."
Chiarugi P., Marzocchini R., Raugei G., Pazzagli C., Berti A., Camici G., Manao G., Cappugi G., Ramponi G.
FEBS Lett. 310:9-12(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-13; CYS-18; CYS-63 AND CYS-146.
[6]"The role of His66 and His72 in the reaction mechanism of bovine liver low-M(r) phosphotyrosine protein phosphatase."
Chiarugi P., Cirri P., Camici G., Manao G., Fiaschi T., Raugei G., Cappugi G., Ramponi G.
Biochem. J. 298:427-433(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-67 AND HIS-73.
[7]"Spectroscopic and kinetic studies of the histidine residues of bovine low-molecular-weight phosphotyrosyl protein phosphatase."
Davis J.P., Zhou M.M., van Etten R.L.
Biochemistry 33:1278-1286(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-67 AND HIS-73.
[8]"The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase."
Su X.-D., Taddei N., Stefani M., Ramponi G., Nordlund P.
Nature 370:575-578(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate."
Zhang M., van Etten R.L., Stauffacher C.V.
Biochemistry 36:15-23(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[10]"Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase."
Zhou M.-M., Logan T.M., Theriault Y., van Etten R.L., Fesik S.W.
Biochemistry 33:5221-5229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83656 mRNA. Translation: AAC37328.1.
PIRA42082.
RefSeqNP_776403.1. NM_173978.2.
UniGeneBt.9965.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVHNMR-A2-157[»]
1C0EX-ray2.20A/B2-157[»]
1DG9X-ray1.90A2-158[»]
1PHRX-ray2.10A2-158[»]
1PNTX-ray2.20A2-157[»]
1Z12X-ray2.20A2-158[»]
1Z13X-ray2.20A2-158[»]
ProteinModelPortalP11064.
SMRP11064. Positions 2-158.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075054.

Proteomic databases

PRIDEP11064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498.
GeneID280977.
KEGGbta:280977.

Organism-specific databases

CTD52.

Phylogenomic databases

eggNOGCOG0394.
GeneTreeENSGT00500000044891.
HOGENOMHOG000273094.
HOVERGENHBG007540.
InParanoidP11064.
KOK14394.
OMAIDITVDS.

Enzyme and pathway databases

SABIO-RKP11064.

Family and domain databases

InterProIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11064.
NextBio20805080.

Entry information

Entry namePPAC_BOVIN
AccessionPrimary (citable) accession number: P11064
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references