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P25779

- CYSP_TRYCR

UniProt

P25779 - CYSP_TRYCR

Protein

Cruzipain

Gene
N/A
Organism
Trypanosoma cruzi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

    Broad endopeptidase specificity similar to that of cathepsin L.

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei147 – 1471
    Active sitei284 – 2841
    Active sitei304 – 3041
    Sitei337 – 3382Cleavage; by autolysis1 Publication

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    SABIO-RKP25779.

    Protein family/group databases

    MEROPSiC01.075.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cruzipain (EC:3.4.22.51)
    Alternative name(s):
    Cruzaine
    Major cysteine proteinase
    OrganismiTrypanosoma cruzi
    Taxonomic identifieri5693 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818CuratedAdd
    BLAST
    Propeptidei19 – 122104Activation peptide1 PublicationPRO_0000026372Add
    BLAST
    Chaini123 – 467345CruzipainPRO_0000026373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi144 ↔ 185
    Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi178 ↔ 223
    Disulfide bondi277 ↔ 325
    Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Developmental stagei

    Present in all developmental stages.

    Interactioni

    Structurei

    Secondary structure

    1
    467
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi125 – 1284
    Helixi129 – 1324
    Beta strandi143 – 1453
    Helixi147 – 16216
    Helixi172 – 1787
    Beta strandi180 – 1823
    Helixi184 – 1863
    Helixi190 – 20011
    Beta strandi204 – 2074
    Turni208 – 2103
    Beta strandi216 – 2183
    Beta strandi225 – 2273
    Beta strandi230 – 23910
    Helixi244 – 25411
    Beta strandi257 – 2615
    Helixi266 – 2683
    Beta strandi271 – 2744
    Beta strandi284 – 29714
    Beta strandi299 – 3035
    Turni307 – 3093
    Beta strandi315 – 3228
    Helixi324 – 3263
    Beta strandi329 – 3368

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AIMX-ray2.00A123-337[»]
    1EWLX-ray2.00A123-337[»]
    1EWMX-ray2.00A123-337[»]
    1EWOX-ray2.10A123-337[»]
    1EWPX-ray1.75A123-337[»]
    1F29X-ray2.15A/B/C123-337[»]
    1F2AX-ray1.60A123-337[»]
    1F2BX-ray1.80A123-337[»]
    1F2CX-ray2.00A123-337[»]
    1ME3X-ray1.20A123-337[»]
    1ME4X-ray1.20A123-337[»]
    1U9QX-ray2.30X123-337[»]
    2AIMX-ray2.20A123-337[»]
    2OZ2X-ray1.95A/C123-337[»]
    3HD3X-ray1.75A/B123-337[»]
    3I06X-ray1.10A123-337[»]
    3IUTX-ray1.20A123-337[»]
    3KKUX-ray1.28A123-337[»]
    3LXSX-ray1.50A/C123-337[»]
    4KLBX-ray2.62A/B/C/D/E123-337[»]
    ProteinModelPortaliP25779.
    SMRiP25779. Positions 123-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25779.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR021981. DUF3586.
    IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF12131. DUF3586. 1 hit.
    PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25779-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGWARALLL AAVLVVMACL VPAATASLHA EETLTSQFAE FKQKHGRVYE    50
    SAAEEAFRLS VFRENLFLAR LHAAANPHAT FGVTPFSDLT REEFRSRYHN 100
    GAAHFAAAQE RARVPVKVEV VGAPAAVDWR ARGAVTAVKD QGQCGSCWAF 150
    SAIGNVECQW FLAGHPLTNL SEQMLVSCDK TDSGCSGGLM NNAFEWIVQE 200
    NNGAVYTEDS YPYASGEGIS PPCTTSGHTV GATITGHVEL PQDEAQIAAW 250
    LAVNGPVAVA VDASSWMTYT GGVMTSCVSE QLDHGVLLVG YNDSAAVPYW 300
    IIKNSWTTQW GEEGYIRIAK GSNQCLVKEE ASSAVVGGPG PTPEPTTTTT 350
    TSAPGPSPSY FVQMSCTDAA CIVGCENVTL PTGQCLLTTS GVSAIVTCGA 400
    ETLTEEVFLT STHCSGPSVR SSVPLNKCNR LLRGSVEFFC GSSSSGRLAD 450
    VDRQRRHQPY HSRHRRL 467
    Length:467
    Mass (Da):49,836
    Last modified:May 1, 1992 - v1
    Checksum:iB93EBA49B511363D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti357 – 3571S → C(PubMed:2038364)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91L → S in clone 1800-2.
    Natural varianti35 – 351T → A in clone 1800-2.
    Natural varianti39 – 391A → V in clone 1800-2.
    Natural varianti51 – 511S → N in clone 1800-4.
    Natural varianti56 – 561A → R in clone 1800-2.
    Natural varianti76 – 761N → G in clone 1800-4.
    Natural varianti109 – 1091Q → G in clone 1800-4.
    Natural varianti117 – 1171K → N in clone 1800-2.
    Natural varianti146 – 1461S → G.
    Natural varianti157 – 1582EC → SG in strain: RA.
    Natural varianti186 – 1861S → G in clones 1800-2 and 1800-4.
    Natural varianti204 – 2041A → G in strain: RA.
    Natural varianti250 – 2512WL → CV in clones 1800-2 and 1800-4.
    Natural varianti261 – 2622VD → H in strain: RA.
    Natural varianti286 – 2861V → F in clone 1800-4.
    Natural varianti286 – 2861V → L in strain: RA.
    Natural varianti308 – 3081T → A in clone 1800-2.
    Natural varianti313 – 3131E → D.
    Natural varianti409 – 4091L → F in clone 1800-2.
    Natural varianti427 – 4271K → Q in clone 1800-2.
    Natural varianti430 – 4301R → W in clone 1800-2.
    Natural varianti457 – 4571H → Y in clone 1800-2.
    Natural varianti461 – 4611H → Q in clone 1800-2.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84342 Genomic DNA. Translation: AAA30181.1.
    M69121 Genomic DNA. Translation: AAA30269.1.
    M69121 Genomic DNA. Translation: AAA30270.1.
    X54414 mRNA. Translation: CAA38278.1.
    M27305 Genomic DNA. Translation: AAA30180.1.
    PIRiA60667.
    S16162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84342 Genomic DNA. Translation: AAA30181.1 .
    M69121 Genomic DNA. Translation: AAA30269.1 .
    M69121 Genomic DNA. Translation: AAA30270.1 .
    X54414 mRNA. Translation: CAA38278.1 .
    M27305 Genomic DNA. Translation: AAA30180.1 .
    PIRi A60667.
    S16162.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AIM X-ray 2.00 A 123-337 [» ]
    1EWL X-ray 2.00 A 123-337 [» ]
    1EWM X-ray 2.00 A 123-337 [» ]
    1EWO X-ray 2.10 A 123-337 [» ]
    1EWP X-ray 1.75 A 123-337 [» ]
    1F29 X-ray 2.15 A/B/C 123-337 [» ]
    1F2A X-ray 1.60 A 123-337 [» ]
    1F2B X-ray 1.80 A 123-337 [» ]
    1F2C X-ray 2.00 A 123-337 [» ]
    1ME3 X-ray 1.20 A 123-337 [» ]
    1ME4 X-ray 1.20 A 123-337 [» ]
    1U9Q X-ray 2.30 X 123-337 [» ]
    2AIM X-ray 2.20 A 123-337 [» ]
    2OZ2 X-ray 1.95 A/C 123-337 [» ]
    3HD3 X-ray 1.75 A/B 123-337 [» ]
    3I06 X-ray 1.10 A 123-337 [» ]
    3IUT X-ray 1.20 A 123-337 [» ]
    3KKU X-ray 1.28 A 123-337 [» ]
    3LXS X-ray 1.50 A/C 123-337 [» ]
    4KLB X-ray 2.62 A/B/C/D/E 123-337 [» ]
    ProteinModelPortali P25779.
    SMRi P25779. Positions 123-337.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P25779.
    ChEMBLi CHEMBL3563.

    Protein family/group databases

    MEROPSi C01.075.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P25779.

    Miscellaneous databases

    EvolutionaryTracei P25779.

    Family and domain databases

    InterProi IPR021981. DUF3586.
    IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF12131. DUF3586. 1 hit.
    PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi."
      Eakin A.E., Mills A.A., Harth G., McKerrow J.H., Craik C.S.
      J. Biol. Chem. 267:7411-7420(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Tulahuen.
    2. "The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes."
      Campetella O., Henriksson J., Aaslund L., Frasch A.C.C., Pettersson U., Cazzulo J.J.
      Mol. Biochem. Parasitol. 50:225-234(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES 1800-2 AND 1800-4).
      Strain: Tulahuen 2.
    3. "Amplification and sequencing of genomic DNA fragments encoding cysteine proteases from protozoan parasites."
      Eakin A.E., Bouvier J., Sakanari J.A., Craik C.S., McKerrow J.H.
      Mol. Biochem. Parasitol. 39:1-8(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-306.
      Strain: RA.
    4. "The C-terminal extension of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi."
      Aaslund L., Henriksson J., Campetella O., Frasch A.C.C., Pettersson U., Cazzulo J.J.
      Mol. Biochem. Parasitol. 45:345-348(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 295-467.
      Strain: Tulahuen 2.
    5. "Self-proteolysis of the cysteine proteinase, cruzipain, from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain."
      Hellman U., Wernstedt C., Cazzulo J.J.
      Mol. Biochem. Parasitol. 44:15-21(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOCATALYSIS OF C-TERMINAL.
      Strain: Tulahuen 2.
    6. "Some kinetic properties of a cysteine proteinase (cruzipain) from Trypanosoma cruzi."
      Cazzulo J.J., Cazzulo-Franke M.C., Martinez J., Franke de Cazzulo B.M.
      Biochim. Biophys. Acta 1037:186-191(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SPECIFICITY.
      Strain: Tulahuen 2.
    7. "Further characterization and partial amino acid sequence of a cysteine proteinase from Trypanosoma cruzi."
      Cazzulo J.J., Couso R., Raimondi A., Wernstedt C., Hellman U.
      Mol. Biochem. Parasitol. 33:33-42(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 123-146 AND 304-317.
    8. "Structural determinants of specificity in the cysteine protease cruzain."
      Gillmor S.A., Craik C.S., Fletterick R.J.
      Protein Sci. 6:1603-1611(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 123-337.

    Entry informationi

    Entry nameiCYSP_TRYCR
    AccessioniPrimary (citable) accession number: P25779
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3