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P25779

- CYSP_TRYCR

UniProt

P25779 - CYSP_TRYCR

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Protein

Cruzipain

Gene
N/A
Organism
Trypanosoma cruzi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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 – 1284Combined sources
Helixi129 – 1324Combined sources
Beta strandi143 – 1453Combined sources
Helixi147 – 16216Combined sources
Helixi172 – 1787Combined sources
Beta strandi180 – 1823Combined sources
Helixi184 – 1863Combined sources
Helixi190 – 20011Combined sources
Beta strandi204 – 2074Combined sources
Turni208 – 2103Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi230 – 23910Combined sources
Helixi244 – 25411Combined sources
Beta strandi257 – 2615Combined sources
Helixi266 – 2683Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi284 – 29714Combined sources
Beta strandi299 – 3035Combined sources
Turni307 – 3093Combined sources
Beta strandi315 – 3228Combined sources
Helixi324 – 3263Combined sources
Beta strandi329 – 3368Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSGWARALLL AAVLVVMACL VPAATASLHA EETLTSQFAE FKQKHGRVYE
60 70 80 90 100
SAAEEAFRLS VFRENLFLAR LHAAANPHAT FGVTPFSDLT REEFRSRYHN
110 120 130 140 150
GAAHFAAAQE RARVPVKVEV VGAPAAVDWR ARGAVTAVKD QGQCGSCWAF
160 170 180 190 200
SAIGNVECQW FLAGHPLTNL SEQMLVSCDK TDSGCSGGLM NNAFEWIVQE
210 220 230 240 250
NNGAVYTEDS YPYASGEGIS PPCTTSGHTV GATITGHVEL PQDEAQIAAW
260 270 280 290 300
LAVNGPVAVA VDASSWMTYT GGVMTSCVSE QLDHGVLLVG YNDSAAVPYW
310 320 330 340 350
IIKNSWTTQW GEEGYIRIAK GSNQCLVKEE ASSAVVGGPG PTPEPTTTTT
360 370 380 390 400
TSAPGPSPSY FVQMSCTDAA CIVGCENVTL PTGQCLLTTS GVSAIVTCGA
410 420 430 440 450
ETLTEEVFLT STHCSGPSVR SSVPLNKCNR LLRGSVEFFC GSSSSGRLAD
460
VDRQRRHQPY HSRHRRL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 107 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