PAPA2_CARPA
ID PAPA2_CARPA Reviewed; 352 AA.
AC P14080;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chymopapain;
DE EC=3.4.22.6;
DE AltName: Full=Papaya proteinase II;
DE Short=PPII;
DE Flags: Precursor;
OS Carica papaya (Papaya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Connerton I.F.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 135-352.
RX PubMed=2106878; DOI=10.1042/bj2660075;
RA Watson D.C., Yaguchi M., Lynn K.R.;
RT "The amino acid sequence of chymopapain from Carica papaya.";
RL Biochem. J. 266:75-81(1990).
RN [3]
RP PROTEIN SEQUENCE OF 135-352.
RX PubMed=2500950; DOI=10.1515/bchm3.1989.370.1.425;
RA Jacquet A., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.;
RT "The thiol proteinases from the latex of Carica papaya L. III. The primary
RT structure of chymopapain.";
RL Biol. Chem. Hoppe-Seyler 370:425-434(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8973203; DOI=10.1021/bi961491w;
RA Maes D., Bouckaert J., Poortmans F., Wyns L., Looze Y.;
RT "Structure of chymopapain at 1.7-A resolution.";
RL Biochemistry 35:16292-16298(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity similar to that of papain.; EC=3.4.22.6;
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; X97789; CAA66378.1; -; mRNA.
DR PIR; T09760; T09760.
DR PDB; 1YAL; X-ray; 1.70 A; A=135-352.
DR PDBsum; 1YAL; -.
DR AlphaFoldDB; P14080; -.
DR SMR; P14080; -.
DR Allergome; 1540; Cari p Chymopapain.
DR MEROPS; C01.002; -.
DR MEROPS; I29.003; -.
DR KEGG; ag:CAA66378; -.
DR BRENDA; 3.4.22.6; 1191.
DR EvolutionaryTrace; P14080; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..134
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2106878,
FT ECO:0000269|PubMed:2500950"
FT /id="PRO_0000026408"
FT CHAIN 135..352
FT /note="Chymopapain"
FT /id="PRO_0000026409"
FT ACT_SITE 159
FT ACT_SITE 293
FT ACT_SITE 313
FT DISULFID 156..197
FT DISULFID 190..229
FT DISULFID 287..338
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:1YAL"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 293..303
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1YAL"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1YAL"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1YAL"
SQ SEQUENCE 352 AA; 39415 MW; 50EA31EBFCF0AF9F CRC64;
MATMSSISKI IFLATCLIIH MGLSSADFYT VGYSQDDLTS IERLIQLFDS WMLKHNKIYE
SIDEKIYRFE IFRDNLMYID ETNKKNNSYW LGLNGFADLS NDEFKKKYVG FVAEDFTGLE
HFDNEDFTYK HVTNYPQSID WRAKGAVTPV KNQGACGSCW AFSTIATVEG INKIVTGNLL
ELSEQELVDC DKHSYGCKGG YQTTSLQYVA NNGVHTSKVY PYQAKQYKCR ATDKPGPKVK
ITGYKRVPSN CETSFLGALA NQPLSVLVEA GGKPFQLYKS GVFDGPCGTK LDHAVTAVGY
GTSDGKNYII IKNSWGPNWG EKGYMRLKRQ SGNSQGTCGV YKSSYYPFKG FA
