Low molecular weight phosphotyrosine protein phosphatase

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P11064 (PPAC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acid phosphatase activity Inferred from electronic annotation. Source: EC non-membrane spanning protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 158

157

Low molecular weight phosphotyrosine protein phosphatase

PRO_0000046557

Sites

Active site

Nucleophile Ref.3 Ref.4

Active site

Ref.3 Ref.4

Active site

130

Proton donor Ref.3 Ref.4

Amino acid modifications

Modified residue

N-acetylalanine Ref.1

Modified residue

132

Phosphotyrosine By similarity

Modified residue

133

Phosphotyrosine By similarity

Experimental info

Mutagenesis

C → A or S: Inactive. Ref.5

Mutagenesis

C → S: Greatly decreases activity. Ref.5

Mutagenesis

C → S: 2.5-fold increase in activity. Ref.5

Mutagenesis

H → E: Decreased activity. Ref.6 Ref.7

Mutagenesis

H → E: Decreased activity. Ref.6 Ref.7

Mutagenesis

146

C → S: No effect on activity. Ref.5

Sequence conflict

D → N AA sequence Ref.2

Secondary structure

158

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11064 [UniParc].

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

158

18,055

        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.

IPI

IPI00693380.

PIR

A42082.

RefSeq

NP_776403.1. NM_173978.2.

UniGene

Bt.9965.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BVH	NMR	-	A	2-157	[»]
1C0E	X-ray	2.20	A/B	2-157	[»]
1DG9	X-ray	1.90	A	2-158	[»]
1PHR	X-ray	2.10	A	2-158	[»]
1PNT	X-ray	2.20	A	2-157	[»]
1Z12	X-ray	2.20	A	2-158	[»]
1Z13	X-ray	2.20	A	2-158	[»]

ProteinModelPortal

P11064.

SMR

P11064. Positions 2-158.

ModBase

Search...

Proteomic databases

PRIDE

P11064.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498.

GeneID

280977.

KEGG

bta:280977.

Organism-specific databases

CTD

52.

Phylogenomic databases

eggNOG

COG0394.

GeneTree

ENSGT00500000044891.

HOGENOM

HOG000273094.

HOVERGEN

HBG007540.

InParanoid

P11064.

K14394.

OMA

WHEGEPA.

OrthoDB

EOG4DR9DN.

Enzyme and pathway databases

SABIO-RK

P11064.

Gene expression databases

ArrayExpress

P11064.

Family and domain databases

InterPro

IPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]

PANTHER

PTHR11717. PTHR11717. 1 hit.

Pfam

PF01451. LMWPc. 1 hit.
[Graphical view]

PRINTS

PR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.

SMART

SM00226. LMWPc. 1 hit.
[Graphical view]

SUPFAM

SSF52788. Tyr_Pase_low_mol_wt. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075054.

EvolutionaryTrace

P11064.

NextBio

20805080.

Entry information

Entry name

PPAC_BOVIN

Accession

Primary (citable) accession number: P11064

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents