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PGA5 pepsinogen 5, group I (pepsinogen A) [ Sus scrofa (pig) ]

Gene ID: 396892, updated on 16-Nov-2023

Summary

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Gene symbol
PGA5
Gene description
pepsinogen 5, group I (pepsinogen A)
See related
Ensembl:ENSSSCG00000013092
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Sus scrofa
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus
Also known as
PGA
Expression
Low expression observed in reference dataset See more
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Genomic context

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See PGA5 in Genome Data Viewer
Location:
chromosome: 2
Exon count:
9
Annotation release Status Assembly Chr Location
106 current Sscrofa11.1 (GCF_000003025.6) 2 NC_010444.4 (10244300..10252644, complement)
105 previous assembly Sscrofa10.2 (GCF_000003025.5) 2 NC_010444.3 (9792085..9800451, complement)

Chromosome 2 - NC_010444.4Genomic Context describing neighboring genes Neighboring gene damage specific DNA binding protein 1 Neighboring gene uncharacterized LOC110259248 Neighboring gene von Willebrand factor C and EGF domains Neighboring gene pregnancy-associated glycoprotein 2-like Neighboring gene pregnancy-associated glycoprotein 6 Neighboring gene pregnancy-associated glycoprotein 2-like

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: Transcriptome data used for gene annotation Transcriptome data used for gene annotation
  • Description: Nine kinds of tissues and a mixture of multiple tissues were sequenced for genome annotation
  • BioProject: PRJNA311523
  • Publication: PMID 27646534
  • Analysis date: Thu Dec 14 17:10:49 2017

Bibliography

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Related articles in PubMed

  1. N-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation. Stepanov VM, et al. Biochem Biophys Res Commun, 1973 Oct 1. PMID 4584879
  2. X-ray crystallographic studies of pepsin. Andreeva NS, et al. Adv Exp Med Biol, 1977. PMID 339692
  3. Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin. Sepulveda P, et al. J Biol Chem, 1975 Jul 10. PMID 1097438
  4. The high-resolution crystal structure of porcine pepsinogen. Hartsuck JA, et al. Proteins, 1992 May. PMID 1594574
  5. Refined structure of porcine pepsinogen at 1.8 A resolution. Sielecki AR, et al. J Mol Biol, 1991 Jun 20. PMID 2056534

See all (19) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Docking interactions determine early cleavage events in insulin proteolysis by pepsin: Experiment and simulation.
    Title: Docking interactions determine early cleavage events in insulin proteolysis by pepsin: Experiment and simulation.
  2. The observation that the mutant prosegment peptides retained their inhibition and folding-catalyst functionality suggests a high level of resilience to mutations of the pepsin prosegment domain.
    Title: Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin.
  3. Acetonitrile was found to induce non-coincident disruption of the secondary and tertiary structural features of pepsin A.
    Title: Acetonitrile-induced unfolding of porcine pepsin A: A proposal for a critical role of hydration structures in conformational stability.
  4. structural evidence presented here may have important implications for understanding the relationship between the structure of porcine pepsin and enzymatic function
    Title: Synchrotron small-angle X-ray scattering studies of the structure of porcine pepsin under various pH conditions.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables aspartic-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
pepsin A
Names
pepsinogen A
NP_999038.2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_213873.2 → NP_999038.2  pepsin A preproprotein

    See identical proteins and their annotated locations for NP_999038.2

    Status: VALIDATED

    Source sequence(s)
    EF108301
    UniProtKB/Swiss-Prot
    P00791, Q29080
    UniProtKB/TrEMBL
    A1YM35
    Related
    ENSSSCP00000013926.1, ENSSSCT00000014312.3
    Conserved Domains (3) summary
    cd05478
    Location:63 → 383
    pepsin_A; Pepsin A, aspartic protease produced in gastric mucosa of mammals
    pfam00026
    Location:72 → 384
    Asp; Eukaryotic aspartyl protease
    pfam07966
    Location:16 → 44
    A1_Propeptide; A1 Propeptide

RefSeqs of Annotated Genomes: Sus scrofa Annotation Release 106 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Sscrofa11.1 Primary Assembly

Genomic

  1. NC_010444.4 Reference Sscrofa11.1 Primary Assembly

    Range
    10244300..10252644 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00791.3 GenPept UniProtKB/Swiss-Prot:P00791

Gene LinkOut

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