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P00791

- PEPA_PIG

UniProt

P00791 - PEPA_PIG

Protein

Pepsin A

Gene

PGA

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.

    Catalytic activityi

    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 9112 PublicationsPROSITE-ProRule annotation
    Active sitei274 – 27412 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Keywords - Biological processi

    Digestion

    Protein family/group databases

    MEROPSiA01.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pepsin A (EC:3.4.23.1)
    Gene namesi
    Name:PGA
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 2

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911D → A: Loss of activity. 1 Publication

    Protein family/group databases

    Allergomei2924. Sus s Pepsin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15154 PublicationsAdd
    BLAST
    Propeptidei16 – 5944Activation peptide2 PublicationsPRO_0000026026Add
    BLAST
    Chaini60 – 385326Pepsin APRO_0000026027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi104 ↔ 1092 Publications
    Disulfide bondi265 ↔ 2692 Publications
    Disulfide bondi308 ↔ 3411 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiP00791.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-142105.
    STRINGi9823.ENSSSCP00000013926.

    Structurei

    Secondary structure

    1
    385
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 237
    Helixi27 – 337
    Helixi37 – 437
    Helixi48 – 514
    Helixi54 – 563
    Beta strandi61 – 644
    Helixi66 – 683
    Turni69 – 713
    Beta strandi73 – 797
    Turni80 – 834
    Beta strandi84 – 918
    Beta strandi97 – 1015
    Helixi107 – 1093
    Helixi117 – 1193
    Beta strandi124 – 13613
    Beta strandi138 – 15013
    Beta strandi153 – 16311
    Helixi169 – 1735
    Beta strandi177 – 1815
    Helixi185 – 1873
    Helixi189 – 1913
    Helixi195 – 2017
    Beta strandi205 – 21410
    Beta strandi216 – 2183
    Beta strandi222 – 2265
    Helixi231 – 2333
    Beta strandi234 – 2363
    Beta strandi239 – 2424
    Turni246 – 2494
    Beta strandi250 – 2534
    Beta strandi255 – 26410
    Beta strandi269 – 2735
    Beta strandi279 – 2835
    Helixi284 – 29310
    Beta strandi300 – 3023
    Beta strandi304 – 3063
    Helixi308 – 3136
    Beta strandi317 – 3215
    Beta strandi324 – 3285
    Helixi330 – 3334
    Beta strandi334 – 3363
    Beta strandi341 – 3488
    Beta strandi352 – 3543
    Beta strandi357 – 3604
    Helixi362 – 3654
    Beta strandi368 – 3736
    Turni374 – 3774
    Beta strandi378 – 3847

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00791.
    SMRiP00791. Positions 16-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00791.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG248684.
    GeneTreeiENSGT00670000097830.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    OMAiGMNLPTA.
    OrthoDBiEOG7HQN88.
    TreeFamiTF314990.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00791-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKWLLLLSLV VLSECLVKVP LVRKKSLRQN LIKNGKLKDF LKTHKHNPAS    50
    KYFPEAAALI GDEPLENYLD TEYFGTIGIG TPAQDFTVIF DTGSSNLWVP 100
    SVYCSSLACS DHNQFNPDDS STFEATSQEL SITYGTGSMT GILGYDTVQV 150
    GGISDTNQIF GLSETEPGSF LYYAPFDGIL GLAYPSISAS GATPVFDNLW 200
    DQGLVSQDLF SVYLSSNDDS GSVVLLGGID SSYYTGSLNW VPVSVEGYWQ 250
    ITLDSITMDG ETIACSGGCQ AIVDTGTSLL TGPTSAIANI QSDIGASENS 300
    DGEMVISCSS IDSLPDIVFT INGVQYPLSP SAYILQDDDS CTSGFEGMDV 350
    PTSSGELWIL GDVFIRQYYT VFDRANNKVG LAPVA 385
    Length:385
    Mass (Da):41,262
    Last modified:November 28, 2006 - v3
    Checksum:i27908D6AC0489D2D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341N → D AA sequence (PubMed:4584879)Curated
    Sequence conflicti34 – 341N → D AA sequence (PubMed:4881358)Curated
    Sequence conflicti119 – 1202DS → SD AA sequence (PubMed:4604255)Curated
    Sequence conflicti128 – 1281Q → E AA sequence (PubMed:4604255)Curated
    Sequence conflicti288 – 2881A → AI in AAA31095. (PubMed:3044927)Curated
    Sequence conflicti301 – 3011D → Y in AAA31096. (PubMed:2494172)Curated
    Sequence conflicti313 – 3131S → Q AA sequence (PubMed:1097438)Curated
    Sequence conflicti322 – 3221N → D AA sequence (PubMed:1097438)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20920 mRNA. Translation: AAA31095.1.
    J04601 mRNA. Translation: AAA31096.1.
    PIRiJT0307. PEPG.
    UniGeneiSsc.219.

    Genome annotation databases

    EnsembliENSSSCT00000014312; ENSSSCP00000013926; ENSSSCG00000013092.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20920 mRNA. Translation: AAA31095.1 .
    J04601 mRNA. Translation: AAA31096.1 .
    PIRi JT0307. PEPG.
    UniGenei Ssc.219.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F34 X-ray 2.45 A 60-385 [» ]
    1PSA X-ray 2.90 A/B 60-385 [» ]
    1YX9 X-ray 3.00 A 60-385 [» ]
    2PSG X-ray 1.80 A 16-385 [» ]
    3PEP X-ray 2.30 A 60-385 [» ]
    3PSG X-ray 1.65 A 16-385 [» ]
    4PEP X-ray 1.80 A 60-385 [» ]
    5PEP X-ray 2.34 A 60-385 [» ]
    ProteinModelPortali P00791.
    SMRi P00791. Positions 16-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-142105.
    STRINGi 9823.ENSSSCP00000013926.

    Chemistry

    BindingDBi P00791.
    ChEMBLi CHEMBL2714.

    Protein family/group databases

    Allergomei 2924. Sus s Pepsin.
    MEROPSi A01.001.

    Proteomic databases

    PRIDEi P00791.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000014312 ; ENSSSCP00000013926 ; ENSSSCG00000013092 .

    Phylogenomic databases

    eggNOGi NOG248684.
    GeneTreei ENSGT00670000097830.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    OMAi GMNLPTA.
    OrthoDBi EOG7HQN88.
    TreeFami TF314990.

    Miscellaneous databases

    EvolutionaryTracei P00791.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiPEPA_PIG
    AccessioniPrimary (citable) accession number: P00791
    Secondary accession number(s): Q29080
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 123 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3