O13453 (PMP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase pmp1
EC=3.1.3.48

Gene names

Name:	pmp1
ORF Names:	SPBC1685.01

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Dual specificity phosphatase that dephosphorylates MAP kinase pmk1 on a Tyr. Has a role in chloride ion homeostasis by inactivating this pmk1 MAP kinase pathway. Ref.1
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Ontologies

Keywords
Biological process	Cell cycle
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Non-traceable author statement. Source: PomBase cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular chloride ion homeostasis Inferred from mutant phenotype Ref.1. Source: PomBase cellular response to salt stress Inferred from mutant phenotype Ref.1. Source: PomBase positive regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 12172965. Source: PomBase regulation of cell cycle cytokinesis Inferred from mutant phenotype Ref.1. Source: PomBase regulation of cell morphogenesis Inferred from mutant phenotype Ref.1. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	MAP kinase tyrosine phosphatase activity Inferred from direct assay Ref.1. Source: PomBase MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from direct assay Ref.1. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 278	278	Tyrosine-protein phosphatase pmp1		PRO_0000094917
Sites
	Active site	158	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13453 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 0EA71219ED32483F	FASTA	278	31,628
	10 20 30 40 50 60 MSQKLPPLKI YTSQLPLVSH KNMLENEEEA SHSQLFTPCP VPPSFPKASK PNSNQPYPNG 70 80 90 100 110 120 PVCIYPPNIY LYAKPTMPII QSFDVVINVA KEVLHPFRTD GRHYRDSKHN LDIQVFDHIE 130 140 150 160 170 180 YVHIHWDHDT QFALELDKLV SFVAYNAMQL NKKVLINCQM GISRSACLMI AFIMKTLNLN 190 200 210 220 230 240 VSDAYEYVKE RSPWIGPNMS LIFQLSEYQQ IIRKNSSQGP YQSSSLKQSK RKSEGNLLFP 250 260 270 EKPHSAQLPL VSPSTSESSM FTNLRRTRSS GSISNDAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"pmp1+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast." Sugiura R., Toda T., Shuntoh H., Yanagida M., Kuno T. EMBO J. 17:140-148(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D82022 Genomic DNA. Translation: BAA22897.1. CU329671 Genomic DNA. Translation: CAA20049.1.
PIR	T39517.
RefSeq	NP_595205.1. NM_001021111.2.
3D structure databases
ProteinModelPortal	O13453.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC1685.01-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC1685.01.1; SPBC1685.01.1:pep; SPBC1685.01.
GeneID	2540019.
KEGG	spo:SPBC1685.01.
Organism-specific databases
PomBase	SPBC1685.01.
Phylogenomic databases
eggNOG	COG2453.
KO	K11240.
OrthoDB	EOG45B4R5.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. False negative. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801162.

Entry information

Entry name

PMP1_SCHPO

Accession

Primary (citable) accession number: O13453

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program