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Protein

Protein tyrosine phosphatase PRL-1

Gene

PRL-1

Organism
Leishmania major
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has protein tyrosine phosphatase activity and may act as a virulence factor to support intracellular survival in host macrophages.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Enzyme regulationi

Activated in a reduced environment which promotes the reduction of the disulfide bond between the regulatory Cys-53 and catalytic Cys-114 residues.1 Publication

pH dependencei

Optimum pH is 6.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei76Proton donorCurated1
Active sitei114Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • dephosphorylation Source: UniProtKB
  • pathogenesis Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processVirulence

Names & Taxonomyi

Protein namesi
Recommended name:
Protein tyrosine phosphatase PRL-1Curated (EC:3.1.3.481 Publication)
Gene namesi
Name:PRL-11 Publication
ORF Names:LMJF_16_0230Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 16

Subcellular locationi

  • Cytoplasm 1 Publication
  • kinetoplast 1 Publication
  • exosome 1 Publication
  • Secreted 1 Publication
  • Note: Enriched around the kinetoplast.1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • host cell cytoplasm Source: UniProtKB
  • kinetoplast Source: UniProtKB
  • nucleus Source: GO_Central

Keywords - Cellular componenti

Cytoplasm, Kinetoplast, Mitochondrion, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53C → S: Increases catalytic activity. 1 Publication1
Mutagenesisi114C → S: Loss of catalytic activity. 1 Publication1
Mutagenesisi172C → S: Probable loss of farnesylation. Loss of kinetoplast localization. Does not affect exosome localization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004416371 – 172Protein tyrosine phosphatase PRL-1Add BLAST172
PropeptideiPRO_0000441640173 – 175Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 114Combined sources2 Publications
Modified residuei172Cysteine methyl esterCurated1
Lipidationi172S-farnesyl cysteine1 Publication1

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Expressioni

Developmental stagei

Expressed at the promastigote life cycle stage during the logarithmic growth and the stationary phase (at protein level). Expressed at lower levels at the amastigote life cycle stage (at protein level).1 Publication

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.16.0230.

Structurei

Secondary structure

1175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Beta strandi18 – 26Combined sources9
Helixi31 – 33Combined sources3
Helixi34 – 42Combined sources9
Turni43 – 45Combined sources3
Beta strandi46 – 51Combined sources6
Helixi60 – 63Combined sources4
Turni64 – 66Combined sources3
Beta strandi68 – 71Combined sources4
Helixi82 – 101Combined sources20
Beta strandi109 – 113Combined sources5
Beta strandi115 – 119Combined sources5
Helixi120 – 131Combined sources12
Helixi137 – 147Combined sources11
Helixi154 – 162Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S4OX-ray2.30A/B4-165[»]
ProteinModelPortaliQ4QEZ7.
SMRiQ4QEZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 164Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST94

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni116 – 120Substrate binding1 Publication5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2836. Eukaryota.
ENOG4111I7J. LUCA.
HOGENOMiHOG000231265.
InParanoidiQ4QEZ7.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiView protein in InterPro
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
PfamiView protein in Pfam
PF00782. DSPc. 1 hit.
SMARTiView protein in SMART
SM00404. PTPc_motif. 1 hit.
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiView protein in PROSITE
PS50056. TYR_PHOSPHATASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4QEZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVNATLIDC CDPQKPSRVL FHFLILDAPS PSNLPTYIKE LQHRGVRHLV
60 70 80 90 100
RVCGPTYDAT LVKSRGIDVH SWPFDDGAPP TRAVLDSWLK LLDTELARQQ
110 120 130 140 150
EDPSVPPPTI GVHCVAGLGR APILVALALV EYGNVSALDA IALIREKRKG
160 170
AINQTQMHWI TKYKRRHQGA GCVIM
Length:175
Mass (Da):19,376
Last modified:July 19, 2005 - v1
Checksum:i61E5BE241E99CE4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796412 Genomic DNA. Translation: CAJ03450.1.
RefSeqiXP_001682101.1. XM_001682049.1.

Genome annotation databases

EnsemblProtistsiLmjF.16.0230:mRNA; LmjF.16.0230:pep; LmjF.16.0230.
GeneDBiLmjF.16.0230:pep.
GeneIDi5650568.
KEGGilma:LMJF_16_0230.

Similar proteinsi

Entry informationi

Entry nameiPRL1_LEIMA
AccessioniPrimary (citable) accession number: Q4QEZ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: July 19, 2005
Last modified: November 22, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families