ID   CYSP1_MAIZE             Reviewed;         371 AA.
AC   Q10716;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cysteine proteinase 1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=CCP1;
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].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 227-371.
RC   STRAIN=cv. DEA; TISSUE=Root meristem;
RX   PubMed=7632917; DOI=10.1007/bf00020395;
RA   Chevalier C., Bourgeois E., Pradet A., Raymond P.;
RT   "Molecular cloning and characterization of six cDNAs expressed during
RT   glucose starvation in excised maize (Zea mays L.) root tips.";
RL   Plant Mol. Biol. 28:473-485(1995).
CC   -!- FUNCTION: Involved in the degradation of the storage protein zein. May
CC       play a role in proteolysis during emergencies.
CC   -!- TISSUE SPECIFICITY: Expressed during the late stages of seed ripening,
CC       in mature seeds and during 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; D45402; BAA08244.1; -; mRNA.
DR   EMBL; X82185; CAA57675.1; -; mRNA.
DR   PIR; S59597; S59597.
DR   PIR; S60456; S60456.
DR   RefSeq; NP_001105685.1; NM_001112215.1.
DR   AlphaFoldDB; Q10716; -.
DR   SMR; Q10716; -.
DR   STRING; 4577.GRMZM2G098298_P01; -.
DR   MEROPS; C01.022; -.
DR   PaxDb; Q10716; -.
DR   PRIDE; Q10716; -.
DR   GeneID; 542701; -.
DR   MaizeGDB; 25431; -.
DR   eggNOG; KOG1542; Eukaryota.
DR   OrthoDB; 1264766at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q10716; 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: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   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..136
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026428"
FT   CHAIN           137..371
FT                   /note="Cysteine proteinase 1"
FT                   /id="PRO_0000026429"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        158..208
FT                   /evidence="ECO:0000250"
FT   DISULFID        196..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        297..345
FT                   /evidence="ECO:0000250"
FT   CONFLICT        269
FT                   /note="L -> R (in Ref. 2; CAA57675)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="I -> M (in Ref. 2; CAA57675)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   371 AA;  40347 MW;  59042B03266E6058 CRC64;
     MAHRVLLLLS LASAAAVAAA VDAEDPLIRQ VVPGGDDNDL ELNAESHFLS FVQRFGKSYK
     DADEHAYRLS VFKDNLRRAR RHQLLDPSAE HGVTKFSDLT PAEFRRTYLG LRKSRRALLR
     ELGESAHEAP VLPTDGLPDD FDWRDHGAVG PVKNQGSCGS CWSFSASGAL EGAHYLATGK
     LEVLSEQQFV DCDHECDSSE PDSCDSGCNG GLMTTAFSYL QKAGGLESEK DYPYTGSDGK
     CKFDKSKIVA SVQNFSVVSV DEAQISANLI KHGPLAIGIN AAYMQTYIGG VSCPYICGRH
     LDHGVLLVGY GASGFAPIRL KDKPYWIIKN SWGENWGENG YYKICRGSNV RNKCGVDSMV
     STVSAVHASK E