P00791Q29080PEPA_PIGPepsin A3.4.23.1PGASus scrofaPigEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSusNucleotide sequence and expression in Escherichia coli of cDNA of swine pepsinogen: involvement of the amino-terminal portion of the activation peptide segment in restoration of the functional protein.NUCLEOTIDE SEQUENCE [MRNA]Synthesis, purification, and active-site mutagenesis of recombinant porcine pepsinogen.NUCLEOTIDE SEQUENCE [MRNA]PROTEIN SEQUENCE OF 16-20 AND 60-65MUTAGENESIS OF ASP-91Complete amino acid sequence of hog pepsin.PROTEIN SEQUENCE OF 60-385DISULFIDE BONDSN-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation.PROTEIN SEQUENCE OF 16-134The amino-terminal sequence of porcine pepsinogen.PROTEIN SEQUENCE OF 16-56Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin.PROTEIN SEQUENCE OF 58-347Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences.PARTIAL PROTEIN SEQUENCE OF 1-26An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.ACTIVE SITEX-ray crystallographic studies of pepsin.CRYSTALLIZATIONX-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3-A resolution.X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)Refined structure of porcine pepsinogen at 1.8-A resolution.X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)The high-resolution crystal structure of porcine pepsinogen.X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.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.SecretedMinor amounts of the active enzyme occur with 'Ala-58' at the amino end.Belongs to the peptidase A1 family.3D-structureAspartyl proteaseDigestionDirect protein sequencingDisulfide bondHydrolasePhosphoproteinProteaseReference proteomeSecretedSignalZymogenDANDDSSDQEAAIDYSQNDMKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA
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