CYSP2_HORVU
ID CYSP2_HORVU Reviewed; 373 AA.
AC P25250;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cysteine proteinase EP-B 2;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=EPB2;
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; U19384; AAA85036.1; -; Genomic_DNA.
DR PIR; JQ1110; JQ1110.
DR PDB; 2FO5; X-ray; 2.20 A; A/B/C/D=131-373.
DR PDBsum; 2FO5; -.
DR AlphaFoldDB; P25250; -.
DR SMR; P25250; -.
DR MEROPS; C01.024; -.
DR MEROPS; I29.003; -.
DR EvolutionaryTrace; P25250; -.
DR ExpressionAtlas; P25250; baseline.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Germination; Glycoprotein; Hydrolase;
KW Protease; Signal; 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_0000026422"
FT CHAIN 134..373
FT /note="Cysteine proteinase EP-B 2"
FT /id="PRO_0000026423"
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"
FT TURN 140..144
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2FO5"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:2FO5"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2FO5"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:2FO5"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:2FO5"
SQ SEQUENCE 373 AA; 40511 MW; 439C56A3EF2851DB CRC64;
MGLLSKKLLV ASMVAAVLAV AAVELCSAIP MEDKDLESEE ALWDLYERWQ SAHRVRRHHA
EKHRRFGTFK SNAHFIHSHN KRGDHPYRLH LNRFGDMDQA EFRATFVGDL RRDTPSKPPS
VPGFMYAALN VSDLPPSVDW RQKGAVTGVK DQGKCGSCWA FSTVVSVEGI NAIRTGSLVS
LSEQELIDCD TADNDGCQGG LMDNAFEYIK NNGGLITEAA YPYRAARGTC NVARAAQNSP
VVVHIDGHQD VPANSEEDLA RAVANQPVSV AVEASGKAFM FYSEGVFTGE CGTELDHGVA
VVGYGVAEDG KAYWTVKNSW GPSWGEQGYI RVEKDSGASG GLCGIAMEAS YPVKTYSKPK
PTPRRALGAR ESL
