ID   CYSP4_BRANA             Reviewed;         328 AA.
AC   P25251;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cysteine proteinase COT44;
DE            EC=3.4.22.-;
DE   Flags: Precursor; Fragment;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=2535469; DOI=10.2307/3869063;
RA   Dietrich R.A., Maslyar D.J., Heupel R.C., Harada J.J.;
RT   "Spatial patterns of gene expression in Brassica napus seedlings:
RT   identification of a cortex-specific gene and localization of mRNAs encoding
RT   isocitrate lyase and a polypeptide homologous to proteinases.";
RL   Plant Cell 1:73-80(1989).
CC   -!- FUNCTION: May function in an early event in cortical cell
CC       differentiation.
CC   -!- TISSUE SPECIFICITY: Present in both cotyledons and axes.
CC   -!- DEVELOPMENTAL STAGE: Expressed maximally during postgerminative growth.
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   PIR; JQ1121; JQ1121.
DR   AlphaFoldDB; P25251; -.
DR   SMR; P25251; -.
DR   MEROPS; C01.021; -.
DR   PRIDE; P25251; -.
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; 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; Germination; Glycoprotein; Hydrolase; Protease;
KW   Thiol protease; Zymogen.
FT   PROPEP          <1..99
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026402"
FT   CHAIN           100..328
FT                   /note="Cysteine proteinase COT44"
FT                   /id="PRO_0000026403"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..163
FT                   /evidence="ECO:0000250"
FT   DISULFID        155..196
FT                   /evidence="ECO:0000250"
FT   DISULFID        254..305
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   328 AA;  36277 MW;  9C95B3C488E8D0D6 CRC64;
     MSIYLRWSLE HGKSNSNSNG IINQQDERFN IFKDNLRFID LHNENNKNAT YKLGLTIFAN
     LTNDEYRSLY LGARTEPVRR ITKAKNVNMK YSAAVNVDEV PVTVDWRQKG AVNAIKDQGT
     CGSCWAFSTA AAVEGINKIV TGELVSLSEQ ELVDCDKSYN QGCNGGLMDY AFQFIMKNGG
     LNTEKDYPYH GTNGKCNSLL KNSRVVTIDG YEDVPSKDET ALKRAVSYQP VSVAIDAGGR
     AFQHYQSGIF TGKCGTNMDH AVVAVGYGSE NGVDYWIVRN SWGTRWGEDG YIRMERNVAS
     KSGKCGIAIE ASYPVKYSPN PVRGTSSV