[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; Connerton I.F.; Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 135-352. PubMed=2106878 [NCBI, ExPASy, EBI, Israel, Japan] Watson D.C., Yaguchi M., Lynn K.R.; "The amino acid sequence of chymopapain from Carica papaya."; Biochem. J. 266:75-81(1990).
[3]	PROTEIN SEQUENCE OF 135-352. PubMed=2500950 [NCBI, ExPASy, EBI, Israel, Japan] Jacquet A., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.; "The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain."; Biol. Chem. Hoppe-Seyler 370:425-434(1989).
[4]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). DOI=10.1021/bi961491w; PubMed=8973203 [NCBI, ExPASy, EBI, Israel, Japan] Maes D., Bouckaert J., Poortmans F., Wyns L., Looze Y.; "Structure of chymopapain at 1.7-A resolution."; Biochemistry 35:16292-16298(1996).

Comments

CATALYTIC ACTIVITY: Specificity similar to that of papain.
SIMILARITY: Belongs to the peptidase C1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X97789; CAA66378.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09760; T09760.

3D structure databases

PDB

1YAL; X-ray; 1.70 A; A=135-352.

[ExPASy / RCSB / EBI]

1YAL; -.

P14080; 38-349.

Protein family/group databases

MEROPS

C01.002; -.

Ontologies

GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Other

P14080; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`PROPEP`	`19 134`	`116`	`Activation peptide.`	`PRO_0000026408`
`CHAIN`	`135 352`	`218`	`Chymopapain.`	`PRO_0000026409`
`ACT_SITE`	`159 159`
`ACT_SITE`	`293 293`
`ACT_SITE`	`313 313`
`DISULFID`	`156 197`
`DISULFID`	`190 229`
`DISULFID`	`287 338`
`TURN`	`141 145`	`5`
`STRAND`	`155 157`	`3`
`HELIX`	`159 176`	`18`
`HELIX`	`184 190`	`7`
`HELIX`	`202 212`	`11`
`TURN`	`217 219`	`3`
`HELIX`	`231 233`	`3`
`STRAND`	`242 246`	`5`
`STRAND`	`249 251`	`3`
`HELIX`	`252 259`	`8`
`STRAND`	`264 268`	`5`
`HELIX`	`273 276`	`4`
`STRAND`	`280 283`	`4`
`STRAND`	`293 303`	`11`
`STRAND`	`306 312`	`7`
`STRAND`	`324 328`	`5`
`STRAND`	`332 334`	`3`
`HELIX`	`337 339`	`3`
`STRAND`	`345 348`	`4`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 39415 Da [This is the MW of the unprocessed precursor]

CRC64: 50EA31EBFCF0AF9F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATMSSISKI IFLATCLIIH MGLSSADFYT VGYSQDDLTS IERLIQLFDS WMLKHNKIYE 

        70         80         90        100        110        120 
SIDEKIYRFE IFRDNLMYID ETNKKNNSYW LGLNGFADLS NDEFKKKYVG FVAEDFTGLE 

       130        140        150        160        170        180 
HFDNEDFTYK HVTNYPQSID WRAKGAVTPV KNQGACGSCW AFSTIATVEG INKIVTGNLL 

       190        200        210        220        230        240 
ELSEQELVDC DKHSYGCKGG YQTTSLQYVA NNGVHTSKVY PYQAKQYKCR ATDKPGPKVK 

       250        260        270        280        290        300 
ITGYKRVPSN CETSFLGALA NQPLSVLVEA GGKPFQLYKS GVFDGPCGTK LDHAVTAVGY 

       310        320        330        340        350 
GTSDGKNYII IKNSWGPNWG EKGYMRLKRQ SGNSQGTCGV YKSSYYPFKG FA

P14080 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools