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

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.
SIMILARITY: Belongs to the peptidase C1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X05167; CAA28804.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25492; KHBH.

3D structure databases

HSSP

O46427; 8PCH. [HSSP ENTRY / PDB]

ModBase

P05167.

Protein family/group databases

MEROPS

C01.041; -.

Organism-specific databases

Gramene

P05167; -.

Ontologies

GO:0005773;	Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Germination; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Vacuole; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 143`	`121`	`Activation peptide (Potential).`	`PRO_0000026416`
`CHAIN`	`144 362`	`219`	`Thiol protease aleurain.`	`PRO_0000026417`
`ACT_SITE`	`168 168`		`By similarity.`
`ACT_SITE`	`308 308`		`By similarity.`
`ACT_SITE`	`328 328`		`By similarity.`
`CARBOHYD`	`188 188`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`257 257`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`165 208`		`By similarity.`
`DISULFID`	`199 241`		`By similarity.`
`DISULFID`	`299 349`		`By similarity.`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 39122 Da [This is the MW of the unprocessed precursor]

CRC64: A70CCD4A843A1686 [This is a checksum on the sequence]

        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

P05167 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools