Reviewed, UniProtKB/Swiss-Prot P11064 (PPAC_BOVIN)

Names and origin

Protein names

Recommended name:
    Low molecular weight phosphotyrosine protein phosphatase
      Short name=LMW-PTPase
      Short name=LMW-PTP
    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)

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 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 Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
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

1

1

Removed Ref.2

Chain

2 – 158

157

Low molecular weight phosphotyrosine protein phosphatase

PRO_0000046557

Sites

Active site

13

1

Nucleophile Ref.3 Ref.4

Active site

19

1

Ref.3 Ref.4

Active site

130

1

Proton donor Ref.3 Ref.4

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.1

Modified residue

132

1

Phosphotyrosine By similarity

Modified residue

133

1

Phosphotyrosine By similarity

Modified residue

156

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

13

1

C → A or S: Inactive. Ref.5

Mutagenesis

18

1

C → S: Greatly decreases activity. Ref.5

Mutagenesis

63

1

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

Mutagenesis

67

1

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

Mutagenesis

73

1

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

Mutagenesis

146

1

C → S: No effect on activity. Ref.5

Sequence conflict

57

1

D → N AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

158

Helix Strand Turn

Details...

Beta strand

7 – 18

12

Helix

19 – 33

15

Helix

37 – 39

3

Beta strand

40 – 49

10

Turn

50 – 53

4

Helix

58 – 66

9

Helix

82 – 85

4

Beta strand

87 – 93

7

Helix

94 – 103

10

Beta strand

113 – 116

4

Helix

117 – 120

4

Helix

136 – 154

19

Sequences

	Sequence		Length	Mass (Da)
	P11064-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5925D5048C42BE02	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

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: 1339287] [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: 2644264] [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: 8319676] [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: 8132604] [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: 1526287] [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: 8135752] [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: 8110762] [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: 8052313] [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: 8993313] [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: 8172896] [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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P11064.

Genome annotation databases

Ensembl

ENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498; Bos taurus. [Genome view]

GeneID

280977.

KEGG

bta:280977.

Organism-specific databases

CTD

280977.

Phylogenomic databases

eggNOG

maNOG19349.

HOVERGEN

P11064.

InParanoid

P11064.

OMA

HRGTQAI.

OrthoDB

EOG9SJ80C.

PhylomeDB

P11064.

Enzyme and pathway databases

BRENDA

3.1.3.2. 251.
3.1.3.48. 251.

Family and domain databases

InterPro

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

PANTHER

PTHR11717. Low_mwt_PTPase. 1 hit.

Pfam

PF01451. LMWPc. 1 hit.
[Graphical view]

PRINTS

PR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.

SMART

SM00226. LMWPc. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	January 19, 2010
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)