PAPA3_CARPA
ID PAPA3_CARPA Reviewed; 348 AA.
AC P10056;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Caricain;
DE EC=3.4.22.30;
DE AltName: Full=Papaya peptidase A;
DE AltName: Full=Papaya proteinase III;
DE Short=PPIII;
DE AltName: Full=Papaya proteinase omega;
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 Baker K.C., Revell D.F., Cummings N.J., Collins M.E., Goodenough P.W.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 133-348.
RX PubMed=3063283; DOI=10.1515/bchm3.1988.369.2.741;
RA Dubois T., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.;
RT "The thiol proteinases from the latex of Carica papaya L. II. The primary
RT structure of proteinase omega.";
RL Biol. Chem. Hoppe-Seyler 369:741-754(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-348.
RC TISSUE=Leaf;
RA Collins M.E., Revell D.F., Sumner I.G., Pickersgill R.W., Goodenough P.W.;
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Pickersgill R.W., Rizkallah P., Harris G.W., Goodenough P.W.;
RT "Determination of the structure of papaya protease omega.";
RL Acta Crystallogr. B 47:766-771(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-290.
RX PubMed=8769310; DOI=10.1016/0014-5793(96)00697-7;
RA Katerelos N.A., Taylor M.A.J., Scott M., Goodenough P.W., Pickersgill R.W.;
RT "Crystal structure of a caricain D158E mutant in complex with E-64.";
RL FEBS Lett. 392:35-39(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF PRO-CARICAIN.
RX PubMed=8939744; DOI=10.1016/s0969-2126(96)00127-x;
RA Groves M.R., Taylor M.A., Scott M., Cummings N.J., Pickersgill R.W.,
RA Jenkins J.A.;
RT "The prosequence of procaricain forms an alpha-helical domain that prevents
RT access to the substrate-binding cleft.";
RL Structure 4:1193-1203(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, similar to those of papain and chymopapain.; EC=3.4.22.30;
CC -!- SUBUNIT: Monomer.
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; X66060; CAA46862.1; -; mRNA.
DR EMBL; X51899; CAA36180.1; -; mRNA.
DR PIR; JN0633; JN0633.
DR PDB; 1MEG; X-ray; 2.00 A; A=133-348.
DR PDB; 1PCI; X-ray; 3.20 A; A/B/C=27-348.
DR PDB; 1PPO; X-ray; 1.80 A; A=133-348.
DR PDBsum; 1MEG; -.
DR PDBsum; 1PCI; -.
DR PDBsum; 1PPO; -.
DR AlphaFoldDB; P10056; -.
DR SMR; P10056; -.
DR Allergome; 1539; Cari p Endoproteinase.
DR MEROPS; C01.003; -.
DR MEROPS; I29.003; -.
DR KEGG; ag:CAA46862; -.
DR BRENDA; 3.4.22.30; 1191.
DR EvolutionaryTrace; P10056; -.
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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..132
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3063283"
FT /id="PRO_0000026410"
FT CHAIN 133..348
FT /note="Caricain"
FT /id="PRO_0000026411"
FT ACT_SITE 157
FT ACT_SITE 291
FT ACT_SITE 311
FT DISULFID 154..195
FT DISULFID 188..227
FT DISULFID 285..336
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:1PCI"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1PCI"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:1PCI"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1PCI"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:1PCI"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1PCI"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1PCI"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 157..174
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1PCI"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1MEG"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1MEG"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 291..301
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1PPO"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1PPO"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1PPO"
SQ SEQUENCE 348 AA; 38788 MW; 328F5C6BF45B4A07 CRC64;
MAMIPSISKL LFVAICLFVH MSVSFGDFSI VGYSQDDLTS TERLIQLFNS WMLNHNKFYE
NVDEKLYRFE IFKDNLNYID ETNKKNNSYW LGLNEFADLS NDEFNEKYVG SLIDATIEQS
YDEEFINEDT VNLPENVDWR KKGAVTPVRH QGSCGSCWAF SAVATVEGIN KIRTGKLVEL
SEQELVDCER RSHGCKGGYP PYALEYVAKN GIHLRSKYPY KAKQGTCRAK QVGGPIVKTS
GVGRVQPNNE GNLLNAIAKQ PVSVVVESKG RPFQLYKGGI FEGPCGTKVD HAVTAVGYGK
SGGKGYILIK NSWGTAWGEK GYIRIKRAPG NSPGVCGLYK SSYYPTKN
