ID   CYSP2_MAIZE             Reviewed;         360 AA.
AC   Q10717;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cysteine proteinase 2;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=CCP2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=7548211; DOI=10.1016/0167-4781(95)00138-7;
RA   Domoto C., Watanabe H., Abe M., Abe K., Arai S.;
RT   "Isolation and characterization of two distinct cDNA clones encoding corn
RT   seed cysteine proteinases.";
RL   Biochim. Biophys. Acta 1263:241-244(1995).
CC   -!- FUNCTION: Involved in the degradation of the storage protein zein. May
CC       play a role in proteolysis during emergencies.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at the onset of germination.
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; D45403; BAA08245.1; -; mRNA.
DR   PIR; S59598; S59598.
DR   AlphaFoldDB; Q10717; -.
DR   SMR; Q10717; -.
DR   STRING; 4577.GRMZM2G038636_P01; -.
DR   MEROPS; C01.041; -.
DR   MEROPS; I29.003; -.
DR   PaxDb; Q10717; -.
DR   MaizeGDB; 25431; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q10717; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IEA:EnsemblPlants.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Signal;
KW   Thiol protease; Vacuole; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..142
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026430"
FT   CHAIN           143..360
FT                   /note="Cysteine proteinase 2"
FT                   /id="PRO_0000026431"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  39199 MW;  8B5788F1B0C3FC1C CRC64;
     MVPRRLFVLA VVVLADTAAV VNSGFADSNP IRPVTDRAAS ALESTVFAAL GRTRDALRFA
     RFAVRYGKSY ESAAEVHKRF RIFSESLQLV RSTNRKGLSY RLGINRFADM SWEEFRATRL
     GAAQNCSATL TGNHRMRAAA VALPETKDWR EDGIVSPVKN QGHCGSCWTF STTGALEAAY
     TQATGKPISL SEQQLVDCGF AFNNFGCNGG LPSQAFEYIK YNGGLDTEES YPYQGVNGIC
     KFKNENVGVK VLDSVNITLG AEDELKDAVG LVRPVSVAFE VITGFRLYKS GVYTSDHCGT
     TPMDVNHAVL AVGYGVEDGV PYWLIKNSWG ADWGDEGYFK MEMGKNMCGV ATCASYPIVA