ID   MEX1_JACME              Reviewed;         214 AA.
AC   P84346;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Mexicain;
DE            EC=3.4.22.-;
OS   Jacaratia mexicana (Wild papaya) (Pileus mexicanus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Caricaceae; Jacaratia.
OX   NCBI_TaxID=309130;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RA   Lian Z.;
RT   "Modification of calcite crystal morphology by designed phosphopeptides and
RT   primary structures and substrate specificities of the cysteine proteases
RT   mexicain and chymomexicain.";
RL   Thesis (1999), Boston University, United States.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH INHIBITOR, DISULFIDE
RP   BONDS, AND ACTIVE SITE.
RX   PubMed=17452780; DOI=10.1107/s0907444907005616;
RA   Gavira J.A., Gonzalez-Ramirez L.A., Oliver-Salvador M.C.,
RA   Soriano-Garcia M., Garcia-Ruiz J.M.;
RT   "Structure of the mexicain-E-64 complex and comparison with other cysteine
RT   proteases of the papain family.";
RL   Acta Crystallogr. D 63:555-563(2007).
CC   -!- FUNCTION: Cysteine protease. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in latex.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   PDB; 2BDZ; X-ray; 2.10 A; A/B/C/D=1-214.
DR   PDBsum; 2BDZ; -.
DR   AlphaFoldDB; P84346; -.
DR   SMR; P84346; -.
DR   PRIDE; P84346; -.
DR   EvolutionaryTrace; P84346; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA: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; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 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; Secreted; Thiol protease.
FT   CHAIN           1..214
FT                   /note="Mexicain"
FT                   /id="PRO_0000050556"
FT   ACT_SITE        25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088,
FT                   ECO:0000269|PubMed:17452780"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089,
FT                   ECO:0000269|PubMed:17452780"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090,
FT                   ECO:0000269|PubMed:17452780"
FT   DISULFID        22..63
FT                   /evidence="ECO:0000269|PubMed:17452780,
FT                   ECO:0007744|PDB:2BDZ"
FT   DISULFID        56..95
FT                   /evidence="ECO:0000269|PubMed:17452780,
FT                   ECO:0007744|PDB:2BDZ"
FT   DISULFID        153..200
FT                   /evidence="ECO:0000269|PubMed:17452780,
FT                   ECO:0007744|PDB:2BDZ"
FT   TURN            7..11
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           25..42
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           50..56
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           118..127
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          159..166
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          194..197
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:2BDZ"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:2BDZ"
SQ   SEQUENCE   214 AA;  23765 MW;  2E79A1C58DF9A12F CRC64;
     YPESIDWREK GAVTPVKNQN PCGSCWAFST VATIEGINKI ITGQLISLSE QELLDCEYRS
     HGCDGGYQTP SLQYVVDNGV HTEREYPYEK KQGRCRAKDK KGPKVYITGY KYVPANDEIS
     LIQAIANQPV SVVTDSRGRG FQFYKGGIYE GPCGTNTDHA VTAVGYGKTY LLLKNSWGPN
     WGEKGYIRIK RASGRSKGTC GVYTSSFFPI KGYR