ID   CYSP1_HORVU             Reviewed;         371 AA.
AC   P25249;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cysteine proteinase EP-B 1;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=EPB1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Himalaya; TISSUE=Aleurone;
RX   PubMed=2152126; DOI=10.2307/3869175;
RA   Koehler S.M., Ho T.H.D.;
RT   "Hormonal regulation, processing, and secretion of cysteine proteinases in
RT   barley aleurone layers.";
RL   Plant Cell 2:769-783(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Himalaya;
RX   PubMed=8756590; DOI=10.1007/bf00021787;
RA   Mikkonen A.A., Porali I.K., Cercos M., Ho T.H.D.;
RT   "A major cysteine proteinase, EPB, in germinating barley seeds: structure
RT   of two intronless genes and regulation of expression.";
RL   Plant Mol. Biol. 31:239-254(1996).
CC   -!- INDUCTION: Synthesized by the aleurone cells stimulated by gibberellic
CC       acid.
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; U19359; AAA85035.1; -; Genomic_DNA.
DR   PIR; JQ1111; JQ1111.
DR   AlphaFoldDB; P25249; -.
DR   SMR; P25249; -.
DR   MEROPS; C01.024; -.
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; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..133
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026420"
FT   CHAIN           134..371
FT                   /note="Cysteine proteinase EP-B 1"
FT                   /id="PRO_0000026421"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        155..197
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..230
FT                   /evidence="ECO:0000250"
FT   DISULFID        291..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  40358 MW;  C70E1D510EF43D4F CRC64;
     MGLLSKKLLV ASMVAAVLAV AAVELCSAIP MEDKDLESEE ALWDLYERWQ SAHRVRRHHA
     EKHRRFGTFK SNAHFIHSHN KRGDHPYRLH LNRFGDMDQA EFRATFVGDL RRDTPAKPPS
     VPGFMYAALN VSDLPPSVDW RQKGAVTGVK DQGKCGSCWA FSTVVSVEGI NAIRTGSLVS
     LSEQELIDCD TADNDGCQGG LMDNAFEYIK NNGGLITEAA YPYRAARGTC NVARAAQNSP
     VVVHIDGHQD VPANSEEDLA RAVANQPVSV AVEASGKAFM FYSEGVFTGD CGTELDHGVA
     VVGYGVAEDG KAYWTVKNSW GPSWGEQGYI RVEKDSGASG GLCGIAMEAS YPVKTYNKPM
     PRRALGAWES Q