NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Japanese white;
TISSUE=Gastric mucosa;
PubMed=2129536 [NCBI, ExPASy, EBI, Israel, Japan]
Kageyama T., Tanabe K., Koiwai O.;
"Structure and development of rabbit pepsinogens. Stage-specific zymogens, nucleotide sequences of cDNAs, molecular evolution, and gene expression during development.";
J. Biol. Chem. 265:17031-17038(1990).

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.
SUBCELLULAR LOCATION: Secreted.
DEVELOPMENTAL STAGE: Early postnatal.
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

EMBL

M59238; AAA31440.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A38302; A38302.

NP_001076165.1; -.

3D structure databases

HSSP

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

ModBase

P27823.

Protein family/group databases

MEROPS

A01.051; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
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

P27823.

Genome annotation databases

GeneID

100009429; -.

Phylogenomic databases

HOVERGEN

P27823; -.

Other

UniRef

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

Keywords

Aspartyl protease; Digestion; Hydrolase; Protease; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 15`	`15`
`PROPEP`	`16 58`	`43`	`Activation peptide.`	`PRO_0000026036`
`CHAIN`	`59 388`	`330`	`Pepsin F.`	`PRO_0000026037`
`ACT_SITE`	`92 92`		`By similarity.`
`ACT_SITE`	`275 275`		`By similarity.`
`DISULFID`	`105 110`		`By similarity.`
`DISULFID`	`266 270`		`By similarity.`
`DISULFID`	`309 343`		`By similarity.`

Sequence information

Length: 388 AA [This is the length of the unprocessed precursor]

Molecular weight: 42786 Da [This is the MW of the unprocessed precursor]

CRC64: 24792BE393594B3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKWLGLLGLV ALSECLVTIP LMKVKSMREN LRENDILLDY LEKHPYRPTY KLLSGQQDPD 

        70         80         90        100        110        120 
VSFEPLRNYL DLAYIGIISI GTPPQEFKVV LDTGSADLWV PSIYCSSPAC GKHNTFNPLL 

       130        140        150        160        170        180 
SSTFLVSGRP INIVYGSGRM SGFLAYDTVQ IAGLVDVAQA FGLSLQEPGK FMEYAVFDGI 

       190        200        210        220        230        240 
LGLSYPSLSF EGITPVFDNL WAQGLISQNL FAFYLSSKEE RGSMLMLGGV DPSYYSGDLH 

       250        260        270        280        290        300 
WVPVSRPLYW QLAVDRISMN GEAIGCDSGC QGIVDTGTSL LIGPRDPVLN IQKIINAQHS 

       310        320        330        340        350        360 
HGGEYIIDCD TISTLPDIIF TIDGVDYPVP ASAYIRKSSV HGCYSNFDES AAHESEPYEV 

       370        380 
WVLGDVFLRL YFTVFDRANN RIGLAPAV

P27823 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