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InterPro: IPR012848 Propeptide, peptidase A1

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Matches:

429 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR012848 Propep_A1

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07966	A1_Propeptide	429
Signatures in BioMart

GO Term annotation Help

Process

GO:0006508 proteolysis

Function

GO:0004190 aspartic-type endopeptidase activity

InterPro annotation

Entry Details in BioMart

Abstract

Most eukaryotic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long. In pepsinogen A, the first 11 residues of the mature pepsin sequence are displaced by residues of the propeptide. The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residue in the propeptide. This hydrogen bond stabilises the propeptide conformation and is probably responsible for triggering the conversion of pepsinogen to pepsin under acidic conditions [1, 2].

Structural links Help

PDB - click here

SCOP: b.50.1.2

CATH: 2.40.70.10

Database links Help

Enzyme: EC:3.4.23

PANDIT: PF07966

Blocks: IPB012848

CluSTr: ALLvsALL:797:106.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012848

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00790 Pepsin A

P00791 Pepsin A

P00796 Renin-2

Q03168 Lysosomal aspartic protease

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012848	Propeptide, peptidase A1
IPR001461	Peptidase A1
IPR001969	Peptidase aspartic, active site
IPR009007	Peptidase aspartic, catalytic
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Hartsuck JA, Koelsch G, Remington SJ. The high-resolution crystal structure of porcine pepsinogen. Proteins 13 1-25 1992 [PubMed: 1594574] http://dx.doi.org/10.1002/prot.340130102
2.	Sielecki AR, Fujinaga M, Read RJ, James MN. Refined structure of porcine pepsinogen at 1.8 A resolution. J. Mol. Biol. 219 671-92 1991 [PubMed: 2056534] http://dx.doi.org/10.1016/0022-2836(91)90664-R

Additional Reading Open in usermanual
	Khan AR, Cherney MM, Tarasova NI, James MN. Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin. Nat. Struct. Biol. 4 1997 1010-5 [PubMed: 9406551] http://dx.doi.org/10.1038/nsb1297-1010
	Moore SA, Sielecki AR, Chernaia MM, Tarasova NI, James MN. Crystal and molecular structures of human progastricsin at 1.62 A resolution. J. Mol. Biol. 247 1995 466-85 [PubMed: 7714902] http://dx.doi.org/10.1006/jmbi.1994.0154
	Kesavulu MM, Ramasubramanian S, Suguna K. Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin. Biochem. Biophys. Res. Commun. 331 2005 1510-4 [PubMed: 15883044] http://dx.doi.org/10.1016/j.bbrc.2005.03.247
	Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN. Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3. Nat. Struct. Biol. 7 2000 653-7 [PubMed: 10932249] http://dx.doi.org/10.1038/77950

InterPro 23.1