P43150 · GP63_LEIME
- ProteinLeishmanolysin C1
- Genegp63-C1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids646 (go to sequence)
- Protein existenceEvidence at transcript level
- 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.
GO annotations
Aspect | Term | |
---|---|---|
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 C1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania
Accessions
- Primary accessionP43150
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 | 42-606 | Extracellular | ||||
Sequence: GAPQHRCIHDAMQARVLQSVAAQRMAPSAVSAVGLPYVSVVPVENASTLDYSLSDSTSPGVVRAANWGALRVAVSAEDLTDPAYHCARVGQQVNNHAGDIVTCTAEDILTDEKRDTLVKHLVPQALQLHRERLKVRQVQGKWKVTGMADVICGDFKVPPEHITEGVTNTDFVLYVASVPSEESVLAWATTCQVFPDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHAVGFSGTFFGAVGIVQEVPHLRRKDFNVSVITSSTVVAKAREQYGCNSLEYLEIEDQGGAGSAGSHIKMRNAKDELMAPAASAGYYTALTMAVFQDLGFYQADFSKAEEMPWGRNVGCAFLSEKCMAKNVTKWPAMFCNESAATIRCPTDRLRVGTCGITAYNTSLATYWQYFTNASLGGYSPFLDYCPFVVGYRNGSCNQDASTTPDLLAAFNVFSEAARCIDGAFTPKNRTAADGYYTALCANVKCDTATRTYSVQVRGTNGYANCTPGLRVKLSSVSDAFEKGGYVTCPPYVEVCQGNVKAAKDFAGDTDSSSSADDAADKEAMQRWSDRMAA | ||||||
Transmembrane | 607-627 | Helical | ||||
Sequence: LATATTLLLGMVLSLMALLVV | ||||||
Topological domain | 628-646 | Cytoplasmic | ||||
Sequence: RLLLTSSPWCCCRLGGLPT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-39 | |||||
Sequence: MPVDSSSTHRHRCVAAPLVRLAAAGAAVTVAVGTAAAWA | ||||||
Propeptide | PRO_0000028670 | 40-102 | Activation peptide | |||
Sequence: HAGAPQHRCIHDAMQARVLQSVAAQRMAPSAVSAVGLPYVSVVPVENASTLDYSLSDSTSPGV | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000028671 | 103-646 | Leishmanolysin C1 | |||
Sequence: VRAANWGALRVAVSAEDLTDPAYHCARVGQQVNNHAGDIVTCTAEDILTDEKRDTLVKHLVPQALQLHRERLKVRQVQGKWKVTGMADVICGDFKVPPEHITEGVTNTDFVLYVASVPSEESVLAWATTCQVFPDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHAVGFSGTFFGAVGIVQEVPHLRRKDFNVSVITSSTVVAKAREQYGCNSLEYLEIEDQGGAGSAGSHIKMRNAKDELMAPAASAGYYTALTMAVFQDLGFYQADFSKAEEMPWGRNVGCAFLSEKCMAKNVTKWPAMFCNESAATIRCPTDRLRVGTCGITAYNTSLATYWQYFTNASLGGYSPFLDYCPFVVGYRNGSCNQDASTTPDLLAAFNVFSEAARCIDGAFTPKNRTAADGYYTALCANVKCDTATRTYSVQVRGTNGYANCTPGLRVKLSSVSDAFEKGGYVTCPPYVEVCQGNVKAAKDFAGDTDSSSSADDAADKEAMQRWSDRMAALATATTLLLGMVLSLMALLVVRLLLTSSPWCCCRLGGLPT | ||||||
Disulfide bond | 127↔144 | |||||
Sequence: CARVGQQVNNHAGDIVTC | ||||||
Disulfide bond | 193↔232 | |||||
Sequence: CGDFKVPPEHITEGVTNTDFVLYVASVPSEESVLAWATTC | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 316↔388 | |||||
Sequence: CNSLEYLEIEDQGGAGSAGSHIKMRNAKDELMAPAASAGYYTALTMAVFQDLGFYQADFSKAEEMPWGRNVGC | ||||||
Disulfide bond | 395↔458 | |||||
Sequence: CMAKNVTKWPAMFCNESAATIRCPTDRLRVGTCGITAYNTSLATYWQYFTNASLGGYSPFLDYC | ||||||
Glycosylation | 399 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 408↔427 | |||||
Sequence: CNESAATIRCPTDRLRVGTC | ||||||
Glycosylation | 409 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 417↔492 | |||||
Sequence: CPTDRLRVGTCGITAYNTSLATYWQYFTNASLGGYSPFLDYCPFVVGYRNGSCNQDASTTPDLLAAFNVFSEAARC | ||||||
Glycosylation | 433 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 466 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 469↔513 | |||||
Sequence: CNQDASTTPDLLAAFNVFSEAARCIDGAFTPKNRTAADGYYTALC | ||||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 518↔568 | |||||
Sequence: CDTATRTYSVQVRGTNGYANCTPGLRVKLSSVSDAFEKGGYVTCPPYVEVC | ||||||
Disulfide bond | 538↔561 | |||||
Sequence: CTPGLRVKLSSVSDAFEKGGYVTC |
Keywords
- PTM
PTM databases
Expression
Developmental stage
Expressed in both the promastigote and the amastigote forms.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length646
- Mass (Da)69,054
- Last updated1995-11-01 v1
- ChecksumFE448DDC78C10B0A