PAPA1_CARPA
ID PAPA1_CARPA Reviewed; 345 AA.
AC P00784;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Papain;
DE EC=3.4.22.2;
DE AltName: Full=Papaya proteinase I;
DE Short=PPI;
DE AltName: Allergen=Car p 1;
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].
RX PubMed=2881845; DOI=10.1016/0378-1119(86)90080-6;
RA Cohen L.W., Coghlan V.M., Dihel L.C.;
RT "Cloning and sequencing of papain-encoding cDNA.";
RL Gene 48:219-227(1986).
RN [2]
RP PROTEIN SEQUENCE OF 134-345.
RX PubMed=5470818; DOI=10.1016/s0021-9258(18)62954-0;
RA Mitchel R.E.J., Chaiken I.M., Smith E.L.;
RT "The complete amino acid sequence of papain. Additions and corrections.";
RL J. Biol. Chem. 245:3485-3492(1970).
RN [3]
RP SEQUENCE REVISION TO 197.
RX PubMed=5435495; DOI=10.1042/bj1160689;
RA Husain S.S., Lowe G.;
RT "A reinvestigation of residues 64-68 and 175 in papain. Evidence that
RT residues 64 and 175 are asparagine.";
RL Biochem. J. 116:689-692(1970).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5681232; DOI=10.1038/218929a0;
RA Drenth J., Jansonius J.N., Koekoek R., Swen H.M., Wolthers B.G.;
RT "Structure of papain.";
RL Nature 218:929-932(1968).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=6502713; DOI=10.1016/0022-2836(84)90467-4;
RA Kamphuis I.G., Kalk K.H., Swarte M.B.A., Drenth J.;
RT "Structure of papain refined at 1.65-A resolution.";
RL J. Mol. Biol. 179:233-256(1984).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2347312; DOI=10.1002/j.1460-2075.1990.tb08321.x;
RA Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V.;
RT "The refined 2.4 A X-ray crystal structure of recombinant human stefin B in
RT complex with the cysteine proteinase papain: a novel type of proteinase
RT inhibitor interaction.";
RL EMBO J. 9:1939-1947(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=1445868; DOI=10.1021/bi00161a007;
RA Yamamoto A., Tomoo K., Doi M., Ohishi H., Inoue M., Ishida T., Yamamoto D.,
RA Tsuboi S., Okamoto H., Okada Y.;
RT "Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide
RT complex at 1.7-A resolution: noncovalent binding mode of a common sequence
RT of endogenous thiol protease inhibitors.";
RL Biochemistry 31:11305-11309(1992).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RA Pickersgill R.W., Harris G.W., Garman E.;
RT "Structure of monoclinic papain at 1.60-A resolution.";
RL Acta Crystallogr. B 48:59-67(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, but preference for an amino acid bearing a large hydrophobic
CC side chain at the P2 position. Does not accept Val in P1'.;
CC EC=3.4.22.2;
CC -!- INTERACTION:
CC P00784; P01040: CSTA; Xeno; NbExp=2; IntAct=EBI-8501709, EBI-724303;
CC -!- ALLERGEN: Causes an allergic reaction in human.
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}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="http://www.worthington-biochem.com/PAP/";
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DR EMBL; M15203; AAB02650.1; -; mRNA.
DR PIR; A26466; PPPA.
DR PDB; 1BP4; X-ray; 2.20 A; A=134-345.
DR PDB; 1BQI; X-ray; 2.50 A; A=134-345.
DR PDB; 1CVZ; X-ray; 1.70 A; A=134-345.
DR PDB; 1KHP; X-ray; 2.00 A; A=134-345.
DR PDB; 1KHQ; X-ray; 1.60 A; A=134-345.
DR PDB; 1PAD; X-ray; 2.80 A; A=134-345.
DR PDB; 1PE6; X-ray; 2.10 A; A=134-345.
DR PDB; 1PIP; X-ray; 1.70 A; A=134-345.
DR PDB; 1POP; X-ray; 2.10 A; A=134-345.
DR PDB; 1PPD; X-ray; 2.00 A; A=134-345.
DR PDB; 1PPN; X-ray; 1.60 A; A=134-345.
DR PDB; 1PPP; X-ray; 1.90 A; A=134-345.
DR PDB; 1STF; X-ray; 2.37 A; E=134-345.
DR PDB; 2CIO; X-ray; 1.50 A; A=134-345.
DR PDB; 2PAD; X-ray; 2.80 A; A=134-345.
DR PDB; 3E1Z; X-ray; 1.86 A; B=134-345.
DR PDB; 3IMA; X-ray; 2.03 A; A/C=134-345.
DR PDB; 3LFY; X-ray; 2.60 A; A/C=134-345.
DR PDB; 3TNX; X-ray; 2.62 A; A/C=27-345.
DR PDB; 3USV; X-ray; 3.80 A; A/C=27-345.
DR PDB; 4PAD; X-ray; 2.80 A; A=134-345.
DR PDB; 4QRG; X-ray; 2.50 A; A/B=27-345.
DR PDB; 4QRV; X-ray; 1.98 A; A/B=27-345.
DR PDB; 4QRX; X-ray; 3.14 A; A/C=27-345.
DR PDB; 5PAD; X-ray; 2.80 A; A=134-345.
DR PDB; 6H8T; X-ray; 2.10 A; A/J=134-345.
DR PDB; 6PAD; X-ray; 2.80 A; A=134-345.
DR PDB; 6TCX; X-ray; 1.65 A; AAA=134-345.
DR PDB; 9PAP; X-ray; 1.65 A; A=134-345.
DR PDBsum; 1BP4; -.
DR PDBsum; 1BQI; -.
DR PDBsum; 1CVZ; -.
DR PDBsum; 1KHP; -.
DR PDBsum; 1KHQ; -.
DR PDBsum; 1PAD; -.
DR PDBsum; 1PE6; -.
DR PDBsum; 1PIP; -.
DR PDBsum; 1POP; -.
DR PDBsum; 1PPD; -.
DR PDBsum; 1PPN; -.
DR PDBsum; 1PPP; -.
DR PDBsum; 1STF; -.
DR PDBsum; 2CIO; -.
DR PDBsum; 2PAD; -.
DR PDBsum; 3E1Z; -.
DR PDBsum; 3IMA; -.
DR PDBsum; 3LFY; -.
DR PDBsum; 3TNX; -.
DR PDBsum; 3USV; -.
DR PDBsum; 4PAD; -.
DR PDBsum; 4QRG; -.
DR PDBsum; 4QRV; -.
DR PDBsum; 4QRX; -.
DR PDBsum; 5PAD; -.
DR PDBsum; 6H8T; -.
DR PDBsum; 6PAD; -.
DR PDBsum; 6TCX; -.
DR PDBsum; 9PAP; -.
DR AlphaFoldDB; P00784; -.
DR PCDDB; P00784; -.
DR SMR; P00784; -.
DR IntAct; P00784; 1.
DR MINT; P00784; -.
DR BindingDB; P00784; -.
DR ChEMBL; CHEMBL4779; -.
DR Allergome; 709; Cari p Papain.
DR MEROPS; C01.001; -.
DR MEROPS; I29.003; -.
DR BRENDA; 3.4.22.2; 1191.
DR SABIO-RK; P00784; -.
DR EvolutionaryTrace; P00784; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0097655; F:serpin family protein binding; IPI:UniProtKB.
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; Allergen; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..133
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:5470818"
FT /id="PRO_0000026406"
FT CHAIN 134..345
FT /note="Papain"
FT /id="PRO_0000026407"
FT ACT_SITE 158
FT /evidence="ECO:0000269|PubMed:5681232"
FT ACT_SITE 292
FT ACT_SITE 308
FT /evidence="ECO:0000269|PubMed:5681232"
FT DISULFID 155..196
FT /evidence="ECO:0000269|PubMed:5470818"
FT DISULFID 189..228
FT /evidence="ECO:0000269|PubMed:5470818"
FT DISULFID 286..333
FT /evidence="ECO:0000269|PubMed:5470818"
FT CONFLICT 180
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="YP -> PY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:4QRV"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:4QRV"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:4QRV"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4QRV"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4QRV"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:4QRV"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4QRV"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3TNX"
FT TURN 140..144
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2CIO"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:2CIO"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1BP4"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1CVZ"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:2CIO"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3LFY"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2CIO"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2CIO"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1BQI"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4QRG"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2CIO"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:2CIO"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2CIO"
SQ SEQUENCE 345 AA; 38922 MW; 82D9FB35EDCA12EF CRC64;
MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES WMLKHNKIYK
NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS NDEFKEKYTG SIAGNYTTTE
LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE
YSEQELLDCD RRSYGCNGGY PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT
DGVRQVQPYN EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG
PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN
