[1]	PROTEIN SEQUENCE. PubMed=6617663 [NCBI, ExPASy, EBI, Israel, Japan] Baudys M., Kostka V.; "Covalent structure of chicken pepsinogen."; Eur. J. Biochem. 136:89-99(1983).

Comments

FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
CATALYTIC ACTIVITY: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
SIMILARITY: Belongs to the peptidase A1 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

UniGene

Gga.402

3D structure databases

HSSP

P00794; 4CMS. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P00793.

Ontologies

GO:0004190;	Molecular function: aspartic-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0007586;	Biological process: digestion (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001969; Pept_Asp_AS.
IPR009007; Pept_Aspartc_cat.
IPR001461; Peptidase_A1.
IPR012848; Propep_A1.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.70.10; Pept_Aspartc_cat; 1.

PANTHER

PTHR13683; Peptidase_A1; 1.

Pfam

PF07966; A1_Propeptide; 1.
PF00026; Asp; 1.
Pfam graphical view of domain structure.

PRINTS

PR00792; PEPSIN.

PROSITE

PS00141; ASP_PROTEASE; 2.

ProtoNet

P00793.

Genome annotation databases

Ensembl

ENSGALG00000024059; Gallus gallus. [Contig view]

Phylogenomic databases

HOVERGEN

P00793; -.

Other

UniRef

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

Keywords

Aspartyl protease; Digestion; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 42`	`42`	`Activation peptide.`	`PRO_0000026046`
`CHAIN`	`43 367`	`325`	`Pepsin A.`	`PRO_0000026047`
`ACT_SITE`	`77 77`
`ACT_SITE`	`260 260`
`CARBOHYD`	`113 113`		`N-linked (GlcNAc...).`
`DISULFID`	`90 95`
`DISULFID`	`251 255`
`DISULFID`	`290 323`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 40432 Da [This is the MW of the unprocessed precursor]

CRC64: 0C547E7FD8F5B341 [This is a checksum on the sequence]

        10         20         30         40         50         60 
SIHRVPLKKG KSLRKQLKDH GLLEDFLKKH PYNPASKYHP VLTATESYEP MTNYMDASYY 

        70         80         90        100        110        120 
GTISIGTPQQ DFSVIFDTGS SNLWVPSIYC KSSACSNHKR FDPSKSSTYV STNETVYIAY 

       130        140        150        160        170        180 
GTGSMSGILG YDTVAVSSID VQNQIFGLSE TEPGSFFYYC NFDGILGLAF PSISSSGATP 

       190        200        210        220        230        240 
VFDNMMSQHL VAQDLFSVYL SKDGETGSFV LFGGIDPNYT TKGIYWVPLS AETYWQITMD 

       250        260        270        280        290        300 
RVTVGNKYVA CFFTCQAIVD TGTSLLVMPQ GAYNRIIKDL GVSSDGEISC DDISKLPDVT 

       310        320        330        340        350        360 
FHINGHAFTL PASAYVLNED GSCMLGFENM GTPTELGEQW ILGDVFIREY YVIFDRANNK 


VGLSPLS

P00793 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