ID   CPGP2_ZINOF             Reviewed;         221 AA.
AC   P82474;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Zingipain-2;
DE            EC=3.4.22.67;
DE   AltName: Full=Cysteine proteinase GP-II;
OS   Zingiber officinale (Ginger) (Amomum zingiber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=94328;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Root;
RX   PubMed=10691991; DOI=10.1046/j.1432-1327.2000.01152.x;
RA   Choi K.H., Laursen R.A.;
RT   "Amino-acid sequence and glycan structures of cysteine proteases with
RT   proline specificity from ginger rhizome Zingiber officinale.";
RL   Eur. J. Biochem. 267:1516-1526(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), DISULFIDE BONDS, AND GLYCOSYLATION.
RX   PubMed=10512617; DOI=10.1021/bi990651b;
RA   Choi K.H., Laursen R.A., Allen K.N.;
RT   "The 2.1 A structure of a cysteine protease with proline specificity from
RT   ginger rhizome, Zingiber officinale.";
RL   Biochemistry 38:11624-11633(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of peptides with a proline residue at
CC         the P2 position.; EC=3.4.22.67;
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   PIR; A59041; A59041.
DR   PDB; 1CQD; X-ray; 2.10 A; A/B/C/D=1-221.
DR   PDBsum; 1CQD; -.
DR   AlphaFoldDB; P82474; -.
DR   SMR; P82474; -.
DR   MEROPS; C01.017; -.
DR   GlyConnect; 117; 2 N-Linked glycans (2 sites).
DR   BRENDA; 3.4.22.67; 6754.
DR   EvolutionaryTrace; P82474; -.
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; 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; Glycoprotein;
KW   Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..221
FT                   /note="Zingipain-2"
FT                   /id="PRO_0000050569"
FT   ACT_SITE        27
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10512617"
FT                   /id="CAR_000190"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10512617"
FT                   /id="CAR_000200"
FT   DISULFID        24..65
FT                   /evidence="ECO:0000269|PubMed:10512617"
FT   DISULFID        58..98
FT                   /evidence="ECO:0000269|PubMed:10512617"
FT   DISULFID        155..206
FT                   /evidence="ECO:0000269|PubMed:10512617"
FT   TURN            9..13
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           27..44
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           52..58
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           70..80
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           120..127
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          161..171
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:1CQD"
FT   STRAND          213..216
FT                   /evidence="ECO:0007829|PDB:1CQD"
SQ   SEQUENCE   221 AA;  23922 MW;  909A312BD8632D42 CRC64;
     DDLPDSIDWR ENGAVVPVKN QGGCGSCWAF STVAAVEGIN QIVTGDLISL SEQQLVDCTT
     ANHGCRGGWM NPAFQFIVNN GGINSEETYP YRGQDGICNS TVNAPVVSID SYENVPSHNE
     QSLQKAVANQ PVSVTMDAAG RDFQLYRSGI FTGSCNISAN HALTVVGYGT ENDKDFWIVK
     NSWGKNWGES GYIRAERNIE NPDGKCGITR FASYPVKKGT N