P40347 (PPAL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low molecular weight phosphotyrosine protein phosphatase
EC=3.1.3.48

Alternative name(s):
Low molecular weight cytosolic acid phosphatase
EC=3.1.3.2
PTPase

Gene names

Name:	LTP1
Ordered Locus Names:	YPR073C
ORF Names:	YP9499.28C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
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 By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphate monoester + H2O = an alcohol + phosphate.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 3500 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	acid phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine phosphatase activity Inferred from direct assay PubMed 15358193. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MOT1	P32333	1	EBI-13757,EBI-11152

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 161

161

Low molecular weight phosphotyrosine protein phosphatase

PRO_0000046565

Sites

Active site

14

1

Nucleophile By similarity

Active site

20

1

By similarity

Active site

133

1

Proton donor By similarity

Amino acid modifications

Modified residue

57

1

Phosphoserine Ref.6

Secondary structure

1

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161

Helix Strand Turn

Details...

Beta strand

8 – 19

12

Helix

20 – 34

15

Helix

38 – 40

3

Beta strand

41 – 50

10

Turn

52 – 55

4

Helix

60 – 68

9

Helix

82 – 86

5

Beta strand

89 – 95

7

Helix

96 – 105

10

Beta strand

113 – 116

4

Helix

117 – 120

4

Beta strand

124 – 127

4

Helix

139 – 160

22

Sequences

	Sequence		Length	Mass (Da)
	P40347 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 0911F4B85C050AB3	FASTA	161	18,675
	10 20 30 40 50 60 MTIEKPKISV AFICLGNFCR SPMAEAIFKH EVEKANLENR FNKIDSFGTS NYHVGESPDH 70 80 90 100 110 120 RTVSICKQHG VKINHKGKQI KTKHFDEYDY IIGMDESNIN NLKKIQPEGS KAKVCLFGDW 130 140 150 160 NTNDGTVQTI IEDPWYGDIQ DFEYNFKQIT YFSKQFLKKE L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase." Ostanin K., Pokalsky C., Wang S., van Etten R.L. J. Biol. Chem. 270:18491-18499(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: Y133.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U11057 mRNA. Translation: AAA99546.1.
L48604 Genomic DNA. Translation: AAA80146.1.
Z49219 Genomic DNA. Translation: CAA89190.1.
Z71255 Genomic DNA. Translation: CAA94981.1.
U51033 Genomic DNA. Translation: AAB68124.1.
AY692891 Genomic DNA. Translation: AAT92910.1.
BK006949 Genomic DNA. Translation: DAA11493.1.

PIR

A57390.

RefSeq

NP_015398.1. NM_001184170.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D1P	X-ray	2.20	A/B	2-161	[»]
1D1Q	X-ray	1.70	A/B	1-161	[»]
1D2A	X-ray	1.90	A/B	2-161	[»]

ProteinModelPortal

P40347.

SMR

P40347. Positions 5-161.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6559N.

IntAct

P40347. 1 interaction.

MINT

MINT-689803.

STRING

4932.YPR073C.

Proteomic databases

PaxDb

P40347.

PeptideAtlas

P40347.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR073C; YPR073C; YPR073C.

GeneID

856187.

KEGG

sce:YPR073C.

Organism-specific databases

CYGD

YPR073c.

SGD

S000006277. LTP1.

Phylogenomic databases

eggNOG

COG0394.

GeneTree

ENSGT00500000044891.

HOGENOM

HOG000273094.

KO

K14394.

OMA

WHEGEPA.

OrthoDB

EOG4SXRP0.

Gene expression databases

Genevestigator

P40347.

GermOnline

YPR073C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR023485. Ptyr_pPase_SF.
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.

SMART

SM00226. LMWPc. 1 hit.
[Graphical view]

SUPFAM

SSF52788. Tyr_Pase_low_mol_wt. 1 hit.

ProtoNet

Search...

Other

BindingDB

P40347.

ChEMBL

CHEMBL5397.

DrugBank

DB00173. Adenine.

EvolutionaryTrace

P40347.

NextBio

981369.

Entry information

Entry name

PPAL_YEAST

Accession

Primary (citable) accession number: P40347
Secondary accession number(s): D6W477

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program