Q91790 (DUS1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 1-A
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
XCL100
XCL100-alfa

Gene names

Name:

dusp1-a

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity during the meiotic cell cycle. Ref.1 Ref.2
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.1 Ref.2 Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1 Ref.2
Subcellular location	Nucleus Ref.1.
Tissue specificity	Expressed in XIK-2 kidney cells. Ref.1
Developmental stage	Present in both immature and mature oocytes (at protein level). Expressed at a constant level during oocyte growth as well as during oocyte maturation. Levels decline somewhat during cleavage (stages 3-6). Levels rise dramatically during the mid-blastula transition. This higher level of expression is then maintained through gastrulation and all subsequent developmental stages. Ref.1
Induction	By serum stimulation, heat shock and oxidative stress. Ref.1
Post-translational modification	Phosphorylated by MAPK1/ERK2 at Thr-168 and at one or more serine residues in a progesterone-dependent manner. Phosphorylation reduces its rate of degradation but does not seem to affect phosphatase activity. Ref.2
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 rhodanese domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Meiosis Stress response
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	meiosis Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Dual specificity protein phosphatase 1-A		PRO_0000421473
Regions
	Domain	21 – 138	118	Rhodanese
	Domain	175 – 369	195	Tyrosine-protein phosphatase
Sites
	Active site	260	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	168	1	Phosphothreonine; by MAPK1 Ref.2
Experimental info
	Mutagenesis	168	1	T → E: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2
	Mutagenesis	168	1	T → V: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2
	Mutagenesis	260	1	C → S: Loss of phosphatase activity. Increases stability. Enables stable complex formation with active MAPK1. Abolishes threonine phosphorylation; when associated with E-168 or V-168. No effect on phosphatase activity and MAPK1 binding; when associated with E-168 or V-168. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q91790 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 14336CA5EC35AAF7	FASTA	369	40,264
	10 20 30 40 50 60 MVNMETCAMD CCVLKALLAE RAHKCLILDC RSFFSFSSCS IVGSSNVRLS TIVKRRAKGS 70 80 90 100 110 120 MGLEHIVPNE EQRCRLVAGM YEAVVLLDER TSELDMLRKD STMMLAVNAL CRDSRGSSIY 130 140 150 160 170 180 FLKGGYETFS AQCPEFCTKN SPPVGLSLPL CANNVPGSAD SNCTPCGTPL YDQGGPVEIL 190 200 210 220 230 240 PFLYLGSAYH ASRKDMLDTL GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN 250 260 270 280 290 300 EAIDFIDSVK NSGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN 310 320 330 340 350 360 FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH SGANSLSYLQ NPITTSPSC

References

[1]

"XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis: its role in MAP kinase inactivation in differentiated cells and its expression during early development." Lewis T., Groom L.A., Sneddon A.A., Smythe C., Keyse S.M. J. Cell Sci. 108:2885-2896(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. Tissue: Embryonic kidney.

[2]

"Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes." Sohaskey M.L., Ferrell J.E. Jr. Mol. Biol. Cell 13:454-468(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-168, PHOSPHORYLATION AT SERINE RESIDUES, MUTAGENESIS OF THR-168 AND CYS-260. Tissue: Ovary.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83742 mRNA. Translation: CAA58710.1. AJ320158 mRNA. Translation: CAC44126.1.
RefSeq	NP_001080570.1. NM_001087101.1.
UniGene	Xl.1243.
3D structure databases
HSSP	HSSP built from PDB template 1M3G based on UniProtKB Q05923.
ProteinModelPortal	Q91790.
SMR	Q91790. Positions 173-315.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380262.
KEGG	xla:380262.
Organism-specific databases
CTD	1843.
Xenbase	XB-GENE-975062. dusp1.
Phylogenomic databases
HOVERGEN	HBG007347.
KO	K04459.
Family and domain databases
Gene3D	3.40.250.10. 1 hit.
InterPro	IPR020417. Atypical_DUSP. IPR020420. Atypical_DUSP_famB. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR008343. MKP. IPR001763. Rhodanese-like_dom. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. PF00581. Rhodanese. 1 hit. [Graphical view]
PIRSF	PIRSF000939. MAPK_Ptase. 1 hit.
PRINTS	PR01908. ADSPHPHTASE. PR01910. ADSPHPHTASEB. PR01764. MAPKPHPHTASE.
SMART	SM00195. DSPc. 1 hit. SM00450. RHOD. 1 hit. [Graphical view]
SUPFAM	SSF52821. Rhodanese-like. 1 hit.
PROSITE	PS50206. RHODANESE_3. 1 hit. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DUS1A_XENLA

Accession

Primary (citable) accession number: Q91790
Secondary accession number(s): Q90W59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2013
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program