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Protein

Pepsin A

Gene

PGA

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei91PROSITE-ProRule annotation2 Publications1
Active sitei274PROSITE-ProRule annotation2 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Digestion

Enzyme and pathway databases

ReactomeiR-SSC-5683826. Surfactant metabolism.

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
Proteomesi
  • UP000008227 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91D → A: Loss of activity. 1 Publication1

Protein family/group databases

Allergomei2924. Sus s Pepsin.

Chemistry databases

ChEMBLiCHEMBL2714.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 154 PublicationsAdd BLAST15
PropeptideiPRO_000002602616 – 59Activation peptide2 PublicationsAdd BLAST44
ChainiPRO_000002602760 – 385Pepsin AAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104 ↔ 1092 Publications
Modified residuei127PhosphoserineBy similarity1
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, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP00791.
PeptideAtlasiP00791.
PRIDEiP00791.

Expressioni

Gene expression databases

GenevisibleiP00791. SS.

Interactioni

Protein-protein interaction databases

MINTiMINT-142105.
STRINGi9823.ENSSSCP00000013926.

Chemistry databases

BindingDBiP00791.

Structurei

Secondary structure

1385
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 23Combined sources7
Helixi27 – 33Combined sources7
Helixi37 – 43Combined sources7
Helixi48 – 51Combined sources4
Helixi54 – 56Combined sources3
Beta strandi61 – 64Combined sources4
Helixi66 – 68Combined sources3
Turni69 – 71Combined sources3
Beta strandi73 – 79Combined sources7
Turni80 – 83Combined sources4
Beta strandi84 – 91Combined sources8
Beta strandi97 – 101Combined sources5
Helixi107 – 109Combined sources3
Helixi117 – 119Combined sources3
Beta strandi124 – 136Combined sources13
Beta strandi138 – 150Combined sources13
Beta strandi153 – 163Combined sources11
Helixi169 – 173Combined sources5
Beta strandi177 – 181Combined sources5
Helixi185 – 187Combined sources3
Helixi189 – 191Combined sources3
Helixi195 – 201Combined sources7
Beta strandi205 – 214Combined sources10
Beta strandi216 – 218Combined sources3
Beta strandi222 – 226Combined sources5
Helixi231 – 233Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi239 – 242Combined sources4
Turni246 – 249Combined sources4
Beta strandi250 – 253Combined sources4
Beta strandi255 – 264Combined sources10
Beta strandi269 – 273Combined sources5
Beta strandi279 – 283Combined sources5
Helixi284 – 293Combined sources10
Beta strandi300 – 302Combined sources3
Beta strandi304 – 306Combined sources3
Helixi308 – 313Combined sources6
Beta strandi317 – 321Combined sources5
Beta strandi324 – 328Combined sources5
Helixi330 – 333Combined sources4
Beta strandi334 – 336Combined sources3
Beta strandi341 – 348Combined sources8
Beta strandi352 – 354Combined sources3
Beta strandi357 – 360Combined sources4
Helixi362 – 365Combined sources4
Beta strandi368 – 373Combined sources6
Turni374 – 377Combined sources4
Beta strandi378 – 384Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00791.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 382Peptidase A1PROSITE-ProRule annotationAdd BLAST310

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP00791.
OMAiFQGMNIP.
OrthoDBiEOG091G0JP7.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti34N → D AA sequence (PubMed:4584879).Curated1
Sequence conflicti34N → D AA sequence (PubMed:4881358).Curated1
Sequence conflicti119 – 120DS → SD AA sequence (PubMed:4604255).Curated2
Sequence conflicti128Q → E AA sequence (PubMed:4604255).Curated1
Sequence conflicti288A → AI in AAA31095 (PubMed:3044927).Curated1
Sequence conflicti301D → Y in AAA31096 (PubMed:2494172).Curated1
Sequence conflicti313S → Q AA sequence (PubMed:1097438).Curated1
Sequence conflicti322N → D AA sequence (PubMed:1097438).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M20920 mRNA. Translation: AAA31095.1.
J04601 mRNA. Translation: AAA31096.1.
PIRiJT0307. PEPG.
UniGeneiSsc.219.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-142105.
STRINGi9823.ENSSSCP00000013926.

Chemistry databases

BindingDBiP00791.
ChEMBLiCHEMBL2714.

Protein family/group databases

Allergomei2924. Sus s Pepsin.
MEROPSiA01.001.

Proteomic databases

PaxDbiP00791.
PeptideAtlasiP00791.
PRIDEiP00791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000014312; ENSSSCP00000013926; ENSSSCG00000013092.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP00791.
OMAiFQGMNIP.
OrthoDBiEOG091G0JP7.
TreeFamiTF314990.

Enzyme and pathway databases

ReactomeiR-SSC-5683826. Surfactant metabolism.

Miscellaneous databases

EvolutionaryTraceiP00791.

Gene expression databases

GenevisibleiP00791. SS.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.