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UniProtKB/Swiss-Prot entry P00791


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PEPA_PIG
Primary accession number P00791
Secondary accession number Q29080
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 28, 2006 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Pepsin A [Precursor]
Synonym EC 3.4.23.1
Gene name
Name: PGA
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(88)90465-9; PubMed=3044927 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukagoshi N., Ando Y., Tomita Y., Uchida R., Takemura T., Sasaki T., Yamagata H., Udaka S., Ichihara Y., Takahashi K.;
"Nucleotide 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.";
Gene 65:285-292(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-20 AND 60-65, AND MUTAGENESIS OF ASP-91.
PubMed=2494172 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X.-L., Wong R.N.S., Tang J.;
"Synthesis, purification, and active-site mutagenesis of recombinant porcine pepsinogen.";
J. Biol. Chem. 264:4482-4489(1989).
[3]
PROTEIN SEQUENCE OF 60-385.
DOI=10.1016/0014-5793(74)81001-X; PubMed=4604255 [NCBI, ExPASy, EBI, Israel, Japan]
Moravek L., Kostka V.;
"Complete amino acid sequence of hog pepsin.";
FEBS Lett. 43:207-211(1974).
[4]
PROTEIN SEQUENCE OF 16-134.
DOI=10.1016/0006-291X(73)90814-0; PubMed=4584879 [NCBI, ExPASy, EBI, Israel, Japan]
Stepanov V.M., Baratova L.A., Pugacheva I.B., Belyanova L.P., Revina L.P., Timokhina E.A.;
"N-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation.";
Biochem. Biophys. Res. Commun. 54:1164-1170(1973).
[5]
PROTEIN SEQUENCE OF 16-56.
PubMed=4881358 [NCBI, ExPASy, EBI, Israel, Japan]
Ong E.B., Perlmann G.E.;
"The amino-terminal sequence of porcine pepsinogen.";
J. Biol. Chem. 243:6104-6109(1968).
[6]
PROTEIN SEQUENCE OF 58-347.
PubMed=1097438 [NCBI, ExPASy, EBI, Israel, Japan]
Sepulveda P., Marciniszyn J.P. Jr., Liu D., Tang J.;
"Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin.";
J. Biol. Chem. 250:5082-5088(1975).
[7]
PARTIAL PROTEIN SEQUENCE OF 1-26.
PubMed=2415509 [NCBI, ExPASy, EBI, Israel, Japan]
Ichihara Y., Sogawa K., Takahashi K.;
"Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences.";
J. Biochem. 98:483-492(1985).
[8]
ACTIVE SITE.
PubMed=4897201 [NCBI, ExPASy, EBI, Israel, Japan]
Bayliss R.S., Knowles J.R., Wybrandt G.B.;
"An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.";
Biochem. J. 113:377-386(1969).
[9]
CRYSTALLIZATION.
PubMed=339692 [NCBI, ExPASy, EBI, Israel, Japan]
Andreeva N.S., Gustchina A.E., Fedorov A.A., Shutzkever N.E., Volnova T.V.;
"X-ray crystallographic studies of pepsin.";
Adv. Exp. Med. Biol. 95:23-31(1977).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/0022-2836(90)90156-G; PubMed=2115088 [NCBI, ExPASy, EBI, Israel, Japan]
Cooper J.B., Khan G., Taylor G., Tickle I.J., Blundell T.L.;
"X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3-A resolution.";
J. Mol. Biol. 214:199-222(1990).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1002/prot.340080109; PubMed=2217165 [NCBI, ExPASy, EBI, Israel, Japan]
Abad-Zapatero C., Rydel T.J., Erickson J.;
"Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.";
Proteins 8:62-81(1990).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1016/0022-2836(91)90664-R; PubMed=2056534 [NCBI, ExPASy, EBI, Israel, Japan]
Sielecki A.R., Fujinaga M., Read R.J., James M.N.G.;
"Refined structure of porcine pepsinogen at 1.8-A resolution.";
J. Mol. Biol. 219:671-692(1991).
[13]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
DOI=10.1002/prot.340130102; PubMed=1594574 [NCBI, ExPASy, EBI, Israel, Japan]
Hartsuck J.E., Koelsch G., Remington S.J.;
"The high-resolution crystal structure of porcine pepsinogen.";
Proteins 13:1-25(1992).
Comments
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
M20920; AAA31095.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04601; AAA31096.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JT0307; PEPG.
RefSeq NP_999038.1; -.
UniGene Ssc.219
3D structure databases
PDB
1F34; X-ray; 2.45 A; A=60-385.[ExPASy / RCSB / EBI]
1PSA; X-ray; 2.90 A; A/B=60-385.[ExPASy / RCSB / EBI]
1YX9; X-ray; 3.00 A; A=60-385.[ExPASy / RCSB / EBI]
2PSG; X-ray; 1.80 A; A=16-385.[ExPASy / RCSB / EBI]
3PEP; X-ray; 2.30 A; A=60-385.[ExPASy / RCSB / EBI]
3PSG; X-ray; 1.65 A; A=16-385.[ExPASy / RCSB / EBI]
4PEP; X-ray; 1.80 A; A=60-385.[ExPASy / RCSB / EBI]
5PEP; X-ray; 2.34 A; A=60-385.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F34; -.
1PSA; -.
1YX9; -.
2PSG; -.
3PEP; -.
3PSG; -.
4PEP; -.
5PEP; -.
ModBase P00791.
Protein family/group databases
MEROPS A01.001; -.
Ontologies
GO
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 P00791.
Genome annotation databases
GeneID 396892; -.
KEGG ssc:396892; -.
Phylogenomic databases
HOVERGEN P00791; -.
Other
LinkHub P00791; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aspartyl protease; Digestion; Direct protein sequencing; Hydrolase; Phosphoprotein; Protease; Secreted; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15      
PROPEP   16    59  44     Activation peptide. PRO_0000026026
CHAIN   60   385  326     Pepsin A. PRO_0000026027
ACT_SITE   91    91         
ACT_SITE   274   274         
MOD_RES   127   127        Phosphoserine. 
DISULFID   104   109         
DISULFID   265   269         
DISULFID   308   341         
MUTAGEN   91    91        D->A: Loss of activity. 
CONFLICT   34    34        N -> D (in Ref. 4 and 5). 
CONFLICT   119   120        DS -> SD (in Ref. 3; AA sequence). 
CONFLICT   128   128        Q -> E (in Ref. 3; AA sequence). 
CONFLICT   288   288        A -> AI (in Ref. 1; AAA31095). 
CONFLICT   301   301        D -> Y (in Ref. 2; AAA31096). 
CONFLICT   313   313        S -> Q (in Ref. 6; AA sequence). 
CONFLICT   322   322        N -> D (in Ref. 6; AA sequence). 
STRAND   62    64  3      
STRAND   66    68  3      
TURN   69    71  3      
STRAND   72    79  8      
TURN   80    83  4      
STRAND   84    91  8      
STRAND   97   101  5      
HELIX   107   111  5      
HELIX   117   119  3      
STRAND   124   136  13      
STRAND   138   150  13      
STRAND   153   165  13      
HELIX   169   173  5      
STRAND   178   181  4      
HELIX   185   187  3      
HELIX   189   191  3      
HELIX   195   201  7      
STRAND   205   213  9      
STRAND   223   226  4      
HELIX   231   233  3      
STRAND   234   236  3      
STRAND   239   242  4      
TURN   246   249  4      
STRAND   250   253  4      
STRAND   255   258  4      
STRAND   261   264  4      
STRAND   269   273  5      
STRAND   279   282  4      
HELIX   284   292  9      
TURN   293   295  3      
STRAND   302   305  4      
HELIX   310   312  3      
STRAND   317   321  5      
STRAND   324   328  5      
TURN   330   332  3      
STRAND   333   339  7      
STRAND   341   347  7      
STRAND   358   360  3      
HELIX   362   365  4      
STRAND   368   373  6      
TURN   374   377  4      
STRAND   378   384  7      
Sequence information
Length: 385 AA [This is the length of the unprocessed precursor] Molecular weight: 41262 Da [This is the MW of the unprocessed precursor] CRC64: 27908D6AC0489D2D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKWLLLLSLV VLSECLVKVP LVRKKSLRQN LIKNGKLKDF LKTHKHNPAS KYFPEAAALI 

        70         80         90        100        110        120 
GDEPLENYLD TEYFGTIGIG TPAQDFTVIF DTGSSNLWVP SVYCSSLACS DHNQFNPDDS 

       130        140        150        160        170        180 
STFEATSQEL SITYGTGSMT GILGYDTVQV GGISDTNQIF GLSETEPGSF LYYAPFDGIL 

       190        200        210        220        230        240 
GLAYPSISAS GATPVFDNLW DQGLVSQDLF SVYLSSNDDS GSVVLLGGID SSYYTGSLNW 

       250        260        270        280        290        300 
VPVSVEGYWQ ITLDSITMDG ETIACSGGCQ AIVDTGTSLL TGPTSAIANI QSDIGASENS 

       310        320        330        340        350        360 
DGEMVISCSS IDSLPDIVFT INGVQYPLSP SAYILQDDDS CTSGFEGMDV PTSSGELWIL 

       370        380 
GDVFIRQYYT VFDRANNKVG LAPVA 

P00791 in FASTA format

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View entry in raw text format (no links)
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