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P00791 (PEPA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pepsin A

EC=3.4.23.1
Gene names
Name:PGA
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Post-translational modification

Minor amounts of the active enzyme occur with 'Ala-58' at the amino end.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.1 Ref.2 Ref.4 Ref.5
Propeptide16 – 5944Activation peptide
PRO_0000026026
Chain60 – 385326Pepsin A
PRO_0000026027

Sites

Active site911 Ref.6 Ref.8
Active site2741 Ref.6 Ref.8

Amino acid modifications

Disulfide bond104 ↔ 109 Ref.3 Ref.6
Disulfide bond265 ↔ 269 Ref.3 Ref.6
Disulfide bond308 ↔ 341 Ref.3

Experimental info

Mutagenesis911D → A: Loss of activity. Ref.2
Sequence conflict341N → D AA sequence Ref.4
Sequence conflict341N → D AA sequence Ref.5
Sequence conflict119 – 1202DS → SD AA sequence Ref.3
Sequence conflict1281Q → E AA sequence Ref.3
Sequence conflict2881A → AI in AAA31095. Ref.1
Sequence conflict3011D → Y in AAA31096. Ref.2
Sequence conflict3131S → Q AA sequence Ref.6
Sequence conflict3221N → D AA sequence Ref.6

Secondary structure

........................................................................................ 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00791 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: 27908D6AC0489D2D

FASTA38541,262
        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 

« Hide

References

[1]"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."
Tsukagoshi N., Ando Y., Tomita Y., Uchida R., Takemura T., Sasaki T., Yamagata H., Udaka S., Ichihara Y., Takahashi K.
Gene 65:285-292(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Synthesis, purification, and active-site mutagenesis of recombinant porcine pepsinogen."
Lin X.-L., Wong R.N.S., Tang J.
J. Biol. Chem. 264:4482-4489(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-20 AND 60-65, MUTAGENESIS OF ASP-91.
[3]"Complete amino acid sequence of hog pepsin."
Moravek L., Kostka V.
FEBS Lett. 43:207-211(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-385, DISULFIDE BONDS.
[4]"N-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation."
Stepanov V.M., Baratova L.A., Pugacheva I.B., Belyanova L.P., Revina L.P., Timokhina E.A.
Biochem. Biophys. Res. Commun. 54:1164-1170(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-134.
[5]"The amino-terminal sequence of porcine pepsinogen."
Ong E.B., Perlmann G.E.
J. Biol. Chem. 243:6104-6109(1968) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-56.
[6]"Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin."
Sepulveda P., Marciniszyn J.P. Jr., Liu D., Tang J.
J. Biol. Chem. 250:5082-5088(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-347.
[7]"Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences."
Ichihara Y., Sogawa K., Takahashi K.
J. Biochem. 98:483-492(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 1-26.
[8]"An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide."
Bayliss R.S., Knowles J.R., Wybrandt G.B.
Biochem. J. 113:377-386(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[9]"X-ray crystallographic studies of pepsin."
Andreeva N.S., Gustchina A.E., Fedorov A.A., Shutzkever N.E., Volnova T.V.
Adv. Exp. Med. Biol. 95:23-31(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[10]"X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3-A resolution."
Cooper J.B., Khan G., Taylor G., Tickle I.J., Blundell T.L.
J. Mol. Biol. 214:199-222(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[11]"Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain."
Abad-Zapatero C., Rydel T.J., Erickson J.
Proteins 8:62-81(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[12]"Refined structure of porcine pepsinogen at 1.8-A resolution."
Sielecki A.R., Fujinaga M., Read R.J., James M.N.G.
J. Mol. Biol. 219:671-692(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[13]"The high-resolution crystal structure of porcine pepsinogen."
Hartsuck J.E., Koelsch G., Remington S.J.
Proteins 13:1-25(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20920 mRNA. Translation: AAA31095.1.
J04601 mRNA. Translation: AAA31096.1.
PIRPEPG. JT0307.
UniGeneSsc.219.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F34X-ray2.45A60-385[»]
1PSAX-ray2.90A/B60-385[»]
1YX9X-ray3.00A60-385[»]
2PSGX-ray1.80A16-385[»]
3PEPX-ray2.30A60-385[»]
3PSGX-ray1.65A16-385[»]
4PEPX-ray1.80A60-385[»]
5PEPX-ray2.34A60-385[»]
ProteinModelPortalP00791.
SMRP00791. Positions 16-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-142105.
STRING9823.ENSSSCP00000013926.

Chemistry

BindingDBP00791.
ChEMBLCHEMBL2714.

Protein family/group databases

Allergome2924. Sus s Pepsin.
MEROPSA01.001.

Proteomic databases

PRIDEP00791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000014312; ENSSSCP00000013926; ENSSSCG00000013092.

Phylogenomic databases

eggNOGNOG248684.
GeneTreeENSGT00670000097830.
HOGENOMHOG000197681.
HOVERGENHBG000482.
OMAGMNLPTA.
OrthoDBEOG7HQN88.
TreeFamTF314990.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00791.

Entry information

Entry namePEPA_PIG
AccessionPrimary (citable) accession number: P00791
Secondary accession number(s): Q29080
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 28, 2006
Last modified: February 19, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references