ID   ALEU_HORVU              Reviewed;         362 AA.
AC   P05167;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Thiol protease aleurain;
DE            EC=3.4.22.16;
DE   Flags: Precursor;
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].
RX   PubMed=3901004; DOI=10.1073/pnas.82.19.6512;
RA   Rogers J.C., Dean D., Heck G.R.;
RT   "Aleurain: a barley thiol protease closely related to mammalian cathepsin
RT   H.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6512-6516(1985).
RN   [2]
RP   SEQUENCE REVISION.
RA   Rogers J.C.;
RL   Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC         cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=Vacuole-like subcellular
CC       compartment.
CC   -!- INDUCTION: Aleurain is synthesized by the aleurone cells stimulated by
CC       gibberellic or abscisic 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; X05167; CAA28804.1; -; Genomic_DNA.
DR   PIR; A25492; KHBH.
DR   AlphaFoldDB; P05167; -.
DR   SMR; P05167; -.
DR   MEROPS; C01.041; -.
DR   MEROPS; I29.003; -.
DR   PRIDE; P05167; -.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0397830.1; HORVU.MOREX.r2.5HG0397830.1; HORVU.MOREX.r2.5HG0397830.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0397830.1.mrna1; HORVU.MOREX.r2.5HG0397830.1.mrna1; HORVU.MOREX.r2.5HG0397830.1.
DR   Gramene; HORVU.MOREX.r2.5HG0397830.1; HORVU.MOREX.r2.5HG0397830.1; HORVU.MOREX.r2.5HG0397830.
DR   Gramene; HORVU.MOREX.r2.5HG0397830.1.mrna1; HORVU.MOREX.r2.5HG0397830.1.mrna1; HORVU.MOREX.r2.5HG0397830.1.
DR   OMA; AYNNFGC; -.
DR   ExpressionAtlas; P05167; baseline and differential.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
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; Vacuole; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..143
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026416"
FT   CHAIN           144..362
FT                   /note="Thiol protease aleurain"
FT                   /id="PRO_0000026417"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        165..208
FT                   /evidence="ECO:0000250"
FT   DISULFID        199..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        299..349
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  39122 MW;  A70CCD4A843A1686 CRC64;
     MAHARVLLLA LAVLATAAVA VASSSSFADS NPIRPVTDRA ASTLESAVLG ALGRTRHALR
     FARFAVRYGK SYESAAEVRR RFRIFSESLE EVRSTNRKGL PYRLGINRFS DMSWEEFQAT
     RLGAAQTCSA TLAGNHLMRD AAALPETKDW REDGIVSPVK NQAHCGSCWT FSTTGALEAA
     YTQATGKNIS LSEQQLVDCA GGFNNFGCNG GLPSQAFEYI KYNGGIDTEE SYPYKGVNGV
     CHYKAENAAV QVLDSVNITL NAEDELKNAV GLVRPVSVAF QVIDGFRQYK SGVYTSDHCG
     TTPDDVNHAV LAVGYGVENG VPYWLIKNSW GADWGDNGYF KMEMGKNMCA IATCASYPVV
     AA