Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00791

- PEPA_PIG

UniProt

P00791 - PEPA_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pepsin A

Gene

PGA

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP00791.
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

        10         20         30         40         50
MKWLLLLSLV VLSECLVKVP LVRKKSLRQN LIKNGKLKDF LKTHKHNPAS
60 70 80 90 100
KYFPEAAALI GDEPLENYLD TEYFGTIGIG TPAQDFTVIF DTGSSNLWVP
110 120 130 140 150
SVYCSSLACS DHNQFNPDDS STFEATSQEL SITYGTGSMT GILGYDTVQV
160 170 180 190 200
GGISDTNQIF GLSETEPGSF LYYAPFDGIL GLAYPSISAS GATPVFDNLW
210 220 230 240 250
DQGLVSQDLF SVYLSSNDDS GSVVLLGGID SSYYTGSLNW VPVSVEGYWQ
260 270 280 290 300
ITLDSITMDG ETIACSGGCQ AIVDTGTSLL TGPTSAIANI QSDIGASENS
310 320 330 340 350
DGEMVISCSS IDSLPDIVFT INGVQYPLSP SAYILQDDDS CTSGFEGMDV
360 370 380
PTSSGELWIL GDVFIRQYYT VFDRANNKVG LAPVA
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 ENSGT00760000118929.
HOGENOMi HOG000197681.
HOVERGENi HBG000482.
InParanoidi P00791.
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 29, 2014
This is version 124 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