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Reviewed, UniProtKB/Swiss-Prot P05167 (ALEU_HORVU)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Thiol protease aleurain
    EC=3.4.22.16
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

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Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

Subcellular location

Vacuole. Note: Vacuole-like subcellular compartment.

Induction

Aleurain is synthesized by the aleurone cells stimulated by gibberellic or abscisic acid.

Sequence similarities

Belongs to the peptidase C1 family.

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Ontologies

Keywords
   Biological processGermination
   Cellular componentVacuole
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 143121Activation peptide Potential
PRO_0000026416
Chain144 – 362219Thiol protease aleurain
PRO_0000026417

Sites

Active site1681 By similarity
Active site3081 By similarity
Active site3281 By similarity

Amino acid modifications

Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Disulfide bond165 ↔ 208 By similarity
Disulfide bond199 ↔ 241 By similarity
Disulfide bond299 ↔ 349 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P05167-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: A70CCD4A843A1686

FASTA36239,122
        10         20         30         40         50         60 
MAHARVLLLA LAVLATAAVA VASSSSFADS NPIRPVTDRA ASTLESAVLG ALGRTRHALR 

        70         80         90        100        110        120 
FARFAVRYGK SYESAAEVRR RFRIFSESLE EVRSTNRKGL PYRLGINRFS DMSWEEFQAT 

       130        140        150        160        170        180 
RLGAAQTCSA TLAGNHLMRD AAALPETKDW REDGIVSPVK NQAHCGSCWT FSTTGALEAA 

       190        200        210        220        230        240 
YTQATGKNIS LSEQQLVDCA GGFNNFGCNG GLPSQAFEYI KYNGGIDTEE SYPYKGVNGV 

       250        260        270        280        290        300 
CHYKAENAAV QVLDSVNITL NAEDELKNAV GLVRPVSVAF QVIDGFRQYK SGVYTSDHCG 

       310        320        330        340        350        360 
TTPDDVNHAV LAVGYGVENG VPYWLIKNSW GADWGDNGYF KMEMGKNMCA IATCASYPVV 


AA

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References

[1]"Aleurain: a barley thiol protease closely related to mammalian cathepsin H."
Rogers J.C., Dean D., Heck G.R.
Proc. Natl. Acad. Sci. U.S.A. 82:6512-6516(1985) [PubMed: 3901004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Rogers J.C.
Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

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Cross-references

Sequence databases

X05167 Genomic DNA. Translation: CAA28804.1.
PIRKHBH. A25492.

3D structure databases

HSSPHSSP built from PDB template 8PCH based on UniProtKB O46427.
ModBaseSearch...

Protein family/group databases

MEROPSC01.041.

Organism-specific databases

GrameneP05167.

Enzyme and pathway databases

BRENDA3.4.22.16. 283.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameALEU_HORVU
AccessionPrimary (citable) accession number: P05167
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents