Q8MNZ1 · GP63_LEITR

  • Protein
    Leishmanolysin
  • Gene
    mspC
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Has an integral role during the infection of macrophages in the mammalian host.

Catalytic activity

  • Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
    EC:3.4.24.36 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

165750100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site266Zn2+ (UniProtKB | ChEBI); catalytic
Active site267
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site336Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processcell adhesion
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Leishmanolysin
  • EC number
  • Alternative names
    • Cell surface protease
    • Major surface glycoprotein
    • Major surface protease
    • Promastigote surface endopeptidase
    • Protein gp63

Gene names

    • Name
      mspC

Organism names

  • Taxonomic identifier
  • Strain
    • MHOM/SU/1974/K27
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    Q8MNZ1
  • Secondary accessions
    • Q8MNZ0

Organism-specific databases

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain44-611Extracellular
Transmembrane612-632Helical
Topological domain633-657Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant596-611in allele mspCLtA2

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, propeptide, chain, glycosylation, disulfide bond.

Type
IDPosition(s)Description
Signal1-41
PropeptidePRO_000002867242-102Activation peptide
ChainPRO_0000028673103-657Leishmanolysin
Glycosylation107N-linked (GlcNAc...) asparagine
Disulfide bond127↔144
Disulfide bond193↔232
Glycosylation302N-linked (GlcNAc...) asparagine
Disulfide bond316↔388
Disulfide bond395↔458
Glycosylation399N-linked (GlcNAc...) asparagine
Disulfide bond408↔427
Glycosylation409N-linked (GlcNAc...) asparagine
Disulfide bond417↔492
Glycosylation445N-linked (GlcNAc...) asparagine
Glycosylation466N-linked (GlcNAc...) asparagine
Disulfide bond469↔513
Glycosylation501N-linked (GlcNAc...) asparagine
Disulfide bond518↔568
Disulfide bond538↔561

Keywords

PTM databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase M8 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    657
  • Mass (Da)
    70,343
  • Last updated
    2002-10-01 v1
  • Checksum
    83FBC04757887E51
MSVDSSSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCIHDAMQARVRQSVARHHTAPGAVSAVGLPYVTLDAAHTAAAADPRPGSAPTVVRAANWSTLRVAVSTEDLTDPAYHCARVGQRVNNHAGAIVTCTAEDILTDEKRDILRKYLIPQALQLHTERLKARQVQGKWKVTGMVDEICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQVFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSEEFFTAARIVAHVSNVRHKTLKVPVVNSSTAVAKAREQYGCGTLEYLEIEDQGGAGSAGSHIKMRNAQDELMAPAAAGGYYTALTMAVFQDLGFYQADFNKAKVMPWGRNAGCAFLSEKCMEQNITKWRAMFCNESEDVMRCPTSRLSLGTCGIRGYRPPLPRYWQYFTNASLGGYSPFMDYCPVVIGYANGSCNQDASSAAEFLAAFNVFSEAARCIDGAFTPKNRTAADGYYAGLCANVRCDTATRTYSVQVRGSMDYVSCTPGLRVELSTVSNAFEEGGCITCPPYVEVCQGNVKGAKDFAGDSDSSSSADDAAGKAAMLRWNDRMVGLATAATVLLGMVLSLMALVVVWLLLVSCPWWCCKLGGPPASVTPACSPETE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ495008
EMBL· GenBank· DDBJ
CAD42817.1
EMBL· GenBank· DDBJ
Genomic DNA
AJ495009
EMBL· GenBank· DDBJ
CAD42818.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp