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 27-MAR-2024, entry version 99.
DE RecName: Full=Cysteine proteinase EP-B 1 {ECO:0000303|PubMed:8756590};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P80884};
DE Flags: Precursor;
GN Name=EPB1 {ECO:0000303|PubMed:8756590};
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], AND INDUCTION BY GIBBERELLIC ACID.
RC STRAIN=cv. Himalaya; TISSUE=Aleurone;
RX PubMed=2152126; DOI=10.1105/tpc.2.8.769;
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], INDUCTION BY GIBBERELLIC ACID, AND
RP REPRESSION BY ABSCISIC ACID.
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 (GA) (PubMed:2152126, PubMed:8756590). Repressed by abscisic acid
CC (ABA) (PubMed:8756590). {ECO:0000269|PubMed:2152126,
CC ECO:0000269|PubMed:8756590}.
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 GlyCosmos; P25249; 1 site, No reported glycans.
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 Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF778; CYSTEINE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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:0000250|UniProtKB:P00785"
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:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 155..197
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT DISULFID 189..230
FT /evidence="ECO:0000250|UniProtKB:P25250"
FT DISULFID 291..343
FT /evidence="ECO:0000250|UniProtKB:P25250"
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
//
