P25779 · CYSP_TRYCR

  • Protein
    Cruzipain
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.
The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.

Miscellaneous

Purified cruzipain is able to degrade itself, yielding a complex mixture of small peptides, and a major 25 kDa fragment.

Catalytic activity

  • Broad endopeptidase specificity similar to that of cathepsin L.
    EC:3.4.22.51 (UniProtKB | ENZYME | Rhea)

Activity regulation

Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site147
Active site284
Active site304
Site337-338Cleavage; by autolysis

GO annotations

AspectTerm
Cellular Componentextracellular space
Cellular Componentlysosome
Molecular Functioncysteine-type endopeptidase activity
Biological Processproteolysis involved in protein catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Cruzipain
  • EC number
  • Alternative names
    • Cruzaine
    • Major cysteine proteinase

Organism names

  • Taxonomic identifier
  • Strains
    • Tulahuen
    • Tulahuen 2
    • RA
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Trypanosoma > Schizotrypanum

Accessions

  • Primary accession
    P25779

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant9in clone 1800-2
Natural variant35in clone 1800-2
Natural variant39in clone 1800-2
Natural variant51in clone 1800-4
Natural variant56in clone 1800-2
Natural variant76in clone 1800-4
Natural variant109in clone 1800-4
Natural variant117in clone 1800-2
Natural variant146
Natural variant157-158in strain: RA
Natural variant186in clones 1800-2 and 1800-4
Natural variant204in strain: RA
Natural variant250-251in clones 1800-2 and 1800-4
Natural variant261-262in strain: RA
Natural variant286in clone 1800-4
Natural variant286in strain: RA
Natural variant308in clone 1800-2
Natural variant313
Natural variant409in clone 1800-2
Natural variant427in clone 1800-2
Natural variant430in clone 1800-2
Natural variant457in clone 1800-2
Natural variant461in clone 1800-2

Variants

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

The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

    • DB022003-[N-[benzyloxycarbonyl]-phenylalaninyl-amino]-5-phenyl-pentane-1-sulfonylmethylbenzene
    • DB020514-Nitrophenyl (3S)-3-({N-[(benzyloxy)carbonyl]-L-phenylalanyl}amino)-5-phenyl-1-pentanesulfonate
    • DB01871[1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
    • DB01810[1-(1-Methyl-4,5-Dioxo-Pent-2-Enylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
    • DB02128[1-(3-hydroxy-2-oxo-1-phenethyl-propylcarbamoyl)2-phenyl-ethyl]-carbamic acid pyridin-4-ylmethyl ester

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
PropeptidePRO_000002637219-122Activation peptide
ChainPRO_0000026373123-467Cruzipain
Disulfide bond144↔185
Glycosylation169N-linked (GlcNAc...) asparagine
Disulfide bond178↔223
Disulfide bond277↔325
Glycosylation292N-linked (GlcNAc...) asparagine
Glycosylation377N-linked (GlcNAc...) asparagine

Keywords

Expression

Developmental stage

Present in all developmental stages.

Interaction

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region333-355Disordered

Sequence similarities

Belongs to the peptidase C1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    467
  • Mass (Da)
    49,836
  • Last updated
    1992-05-01 v1
  • Checksum
    B93EBA49B511363D
MSGWARALLLAAVLVVMACLVPAATASLHAEETLTSQFAEFKQKHGRVYESAAEEAFRLSVFRENLFLARLHAAANPHATFGVTPFSDLTREEFRSRYHNGAAHFAAAQERARVPVKVEVVGAPAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENNGAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQLDHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVGGPGPTPEPTTTTTTSAPGPSPSYFVQMSCTDAACIVGCENVTLPTGQCLLTTSGVSAIVTCGAETLTEEVFLTSTHCSGPSVRSSVPLNKCNRLLRGSVEFFCGSSSSGRLADVDRQRRHQPYHSRHRRL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict357in Ref. 4

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M84342
EMBL· GenBank· DDBJ
AAA30181.1
EMBL· GenBank· DDBJ
Genomic DNA
M69121
EMBL· GenBank· DDBJ
AAA30269.1
EMBL· GenBank· DDBJ
Genomic DNA
M69121
EMBL· GenBank· DDBJ
AAA30270.1
EMBL· GenBank· DDBJ
Genomic DNA
X54414
EMBL· GenBank· DDBJ
CAA38278.1
EMBL· GenBank· DDBJ
mRNA
M27305
EMBL· GenBank· DDBJ
AAA30180.1
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