Q8MNZ1 · GP63_LEITR
- ProteinLeishmanolysin
- GenemspC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids657 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Has an integral role during the infection of macrophages in the mammalian host.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 266 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 267 | ||||
Binding site | 270 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 336 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | cell adhesion | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLeishmanolysin
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania
Accessions
- Primary accessionQ8MNZ1
- Secondary accessions
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 44-611 | Extracellular | |||
Transmembrane | 612-632 | Helical | |||
Topological domain | 633-657 | Cytoplasmic | |||
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | 596-611 | in 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.
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-41 | ||||
Propeptide | PRO_0000028672 | 42-102 | Activation peptide | ||
Chain | PRO_0000028673 | 103-657 | Leishmanolysin | ||
Glycosylation | 107 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 127↔144 | ||||
Disulfide bond | 193↔232 | ||||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 316↔388 | ||||
Disulfide bond | 395↔458 | ||||
Glycosylation | 399 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 408↔427 | ||||
Glycosylation | 409 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 417↔492 | ||||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 466 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 469↔513 | ||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 518↔568 | ||||
Disulfide bond | 538↔561 | ||||
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length657
- Mass (Da)70,343
- Last updated2002-10-01 v1
- Checksum83FBC04757887E51
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ495008 EMBL· GenBank· DDBJ | CAD42817.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ495009 EMBL· GenBank· DDBJ | CAD42818.1 EMBL· GenBank· DDBJ | Genomic DNA |