Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8MNZ1 (GP63_LEITR)

Last modified June 16, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leishmanolysin
    EC=3.4.24.36
Alternative name(s):
    Cell surface protease
    Major surface glycoprotein
    Protein gp63
    Promastigote surface endopeptidase
    Major surface protease
Gene names
Name: mspC
OrganismLeishmania tropica
Taxonomic identifier5666 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmania

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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-.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

Belongs to the peptidase M8 family.

Ontologies

Keywords
   Biological processCell adhesion
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Propeptide42 – 10261Activation peptide Potential
PRO_0000028672
Chain103 – 657555Leishmanolysin
PRO_0000028673

Sites

Active site2671 By similarity
Metal binding2661Zinc; catalytic By similarity
Metal binding2701Zinc; catalytic By similarity
Metal binding3361Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Disulfide bond127 ↔ 144 By similarity
Disulfide bond193 ↔ 232 By similarity
Disulfide bond316 ↔ 388 By similarity
Disulfide bond395 ↔ 458 By similarity
Disulfide bond408 ↔ 427 By similarity
Disulfide bond417 ↔ 492 By similarity
Disulfide bond469 ↔ 513 By similarity
Disulfide bond518 ↔ 568 By similarity
Disulfide bond538 ↔ 561 By similarity

Natural variations

Natural variant596 – 61116Missing in allele mspCLtA2.

Sequences

Sequence LengthMass (Da)Tools
Q8MNZ1-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 83FBC04757887E51

FASTA65770,343
        10         20         30         40         50         60 
MSVDSSSSST HRRRCVAARL VRLAAAGAAV TVAVGTAAAW AHAGALQHRC IHDAMQARVR 

        70         80         90        100        110        120 
QSVARHHTAP GAVSAVGLPY VTLDAAHTAA AADPRPGSAP TVVRAANWST LRVAVSTEDL 

       130        140        150        160        170        180 
TDPAYHCARV GQRVNNHAGA IVTCTAEDIL TDEKRDILRK YLIPQALQLH TERLKARQVQ 

       190        200        210        220        230        240 
GKWKVTGMVD EICGDFKVPQ AHITEGFSNT DFVMYVASVP SEEGVLAWAT TCQVFSDGHP 

       250        260        270        280        290        300 
AVGVINIPAA NIASRYDQLV TRVVTHEMAH ALGFSEEFFT AARIVAHVSN VRHKTLKVPV 

       310        320        330        340        350        360 
VNSSTAVAKA REQYGCGTLE YLEIEDQGGA GSAGSHIKMR NAQDELMAPA AAGGYYTALT 

       370        380        390        400        410        420 
MAVFQDLGFY QADFNKAKVM PWGRNAGCAF LSEKCMEQNI TKWRAMFCNE SEDVMRCPTS 

       430        440        450        460        470        480 
RLSLGTCGIR GYRPPLPRYW QYFTNASLGG YSPFMDYCPV VIGYANGSCN QDASSAAEFL 

       490        500        510        520        530        540 
AAFNVFSEAA RCIDGAFTPK NRTAADGYYA GLCANVRCDT ATRTYSVQVR GSMDYVSCTP 

       550        560        570        580        590        600 
GLRVELSTVS NAFEEGGCIT CPPYVEVCQG NVKGAKDFAG DSDSSSSADD AAGKAAMLRW 

       610        620        630        640        650 
NDRMVGLATA ATVLLGMVLS LMALVVVWLL LVSCPWWCCK LGGPPASVTP ACSPETE 

« Hide

References

[1]"Genetic diversity in the Leishmania donovani complex."
Mauricio I.L., Stothard J.R., Miles M.A.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES MSPCLTA1 AND MSPCLTA2).
Strain: MHOM/SU/1974/K27.

Cross-references

Sequence databases

AJ495008 Genomic DNA. Translation: CAD42817.1.
AJ495009 Genomic DNA. Translation: CAD42818.1.

3D structure databases

HSSPHSSP built from PDB template 1LML based on UniProtKB P08148.
SMRQ8MNZ1. Positions 102-577.
ModBaseSearch...

Protein family/group databases

MEROPSM08.001.

Enzyme and pathway databases

BRENDA3.4.24.36. 257177.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR001577. Peptidase_M8.
[Graphical view]
PANTHERPTHR10942. Peptidase_M8. 1 hit.
PfamPF01457. Peptidase_M8. 1 hit.
[Graphical view]
PRINTSPR00782. LSHMANOLYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGP63_LEITR
AccessionPrimary (citable) accession number: Q8MNZ1
Secondary accession number(s): Q8MNZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents