Skip Header

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

Q06031 (GP63_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leishmanolysin homolog

EC=3.4.24.36
Alternative name(s):
Cell surface protease
Major surface glycoprotein
Protein gp63
Gene names
Name:gp63
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeCrithidia

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays 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.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the peptidase M8 family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
Zymogen
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4545 By similarity
Propeptide46 – 11368Activation peptide By similarity
PRO_0000028652
Chain114 – 628515Leishmanolysin homolog
PRO_0000028653
Propeptide629 – 65325Removed in mature form Potential
PRO_0000028654

Sites

Active site2771 By similarity
Metal binding2761Zinc; catalytic Potential
Metal binding2801Zinc; catalytic Potential
Metal binding3461Zinc; catalytic By similarity

Amino acid modifications

Lipidation6281GPI-anchor amidated serine Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Disulfide bond138 ↔ 155 By similarity
Disulfide bond203 ↔ 242 By similarity
Disulfide bond326 ↔ 398 By similarity
Disulfide bond405 ↔ 468 By similarity
Disulfide bond418 ↔ 437 By similarity
Disulfide bond427 ↔ 502 By similarity
Disulfide bond479 ↔ 524 By similarity
Disulfide bond529 ↔ 579 By similarity
Disulfide bond549 ↔ 572 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06031 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 263A1DA7568034B6

FASTA65369,171
        10         20         30         40         50         60 
MHAPPTATRR SGPRRTHGIM ARLVRLAAGV LVVTLVIGAL TALSADDAKT HPHKVCIHDE 

        70         80         90        100        110        120 
LQQSLLDSVA QQGLAPQRVS RVGLPYVASA TAAPAAQVGG VDFALAGDSA PDVTRSAEWG 

       130        140        150        160        170        180 
ELRITVSAEE LTDPAYHCAT VGQVISNHID DYVTCTADDI MTAEKLDILM NYLIPEALQM 

       190        200        210        220        230        240 
HKDRLQVQQV QGTWKVARMT SYCGRFKVPE EHFTTGLSNT DFVLYVASVP TSPGVLAWAN 

       250        260        270        280        290        300 
TCQVFSNDQP AVGVINIPAA TITERYDHLM VHAVTHEIAH SLGFSNAFFT NTGIGQFVTG 

       310        320        330        340        350        360 
VRGNPDTVPV INSPTVVAKA REHYGCDDVT YVELEDAGGS GTMGSHWKIR NAQDELMAGI 

       370        380        390        400        410        420 
SGVAYYTSLT LSAFEDLGYY KANYSNAETM KWGKDVGCAF LTGKCVVDNV TQFPSMYCDK 

       430        440        450        460        470        480 
DENVYRCHTA RLNLGSCEVT DYTFDLPDYL QYFTVPSVGG SADYYDYCPY IVRSPIGSCT 

       490        500        510        520        530        540 
QAASSASPFV SAFNTFSMAS RCIDGTFTPK STGGATVTAH LGMCTNVACN TADKTYSIQV 

       550        560        570        580        590        600 
YGNGAYIPCT PGATISLDTV SDAFEAGGNI TCPPYLEVCQ SNVKGAMDYE SMTNSGSGSS 

       610        620        630        640        650 
RPAPVEPSGS GSGSSAATTA PSPTRDGSAA ADRIAPRTAA VALLALAVAA ACV 

« Hide

References

[1]"Crithidia fasciculata contains a transcribed leishmanial surface proteinase (gp63) gene homologue."
Inverso J.A., Medina-Acosta E., O'Connor J., Russell D.G., Cross G.A.M.
Mol. Biochem. Parasitol. 57:47-54(1993) [PubMed: 8426615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11745.
[2]Inverso J.A., Medina-Acosta E., O'Connor J., Russell D.G., Cross G.A.M.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO LEU-122.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94364 Genomic DNA. Translation: AAA30319.1.
M94365 Genomic DNA. Translation: AAA30320.2.
PIRA60961.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001577. 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_CRIFA
AccessionPrimary (citable) accession number: Q06031
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 5, 2010
Last modified: November 16, 2011
This is version 70 of the entry and version 2 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