Adverts

Open Access Articles- Top Results for ARTS-1

ARTS-1

Template:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/row
Identifiers
SymbolsERAP1 ; A-LAP; ALAP; APPILS; ARTS-1; ARTS1; ERAAP; ERAAP1; PILS-AP; PILSAP
External IDsOMIM606832 MGI1933403 HomoloGene56754 IUPHAR: 1566 ChEMBL: 5939 GeneCards: ERAP1 Gene
RNA expression pattern
File:PBB GE ARTS-1 214012 at tn.png
File:PBB GE ARTS-1 214034 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez5175280898
EnsemblENSG00000164307ENSMUSG00000021583
UniProtQ9NZ08Q9EQH2
RefSeq (mRNA)NM_001040458NM_030711
RefSeq (protein)NP_001035548NP_109636
Location (UCSC)Chr 5:
96.1 – 96.14 Mb
Chr 13:
74.64 – 74.69 Mb
PubMed search[1][2]


Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, also known as endoplasmic reticulum aminopeptidase 1 (ARTS-1), is a protein which in humans is encoded by the ARTS-1 gene.[1]

Endoplasmic reticulum amino peptidase 1 is active in the endoplasmic reticulum, which is involved in protein processing and transport. This protein is an aminopeptidase, which is an enzyme that cleaves other proteins into smaller fragments called peptides.

Nomenclature

ARTS1 is also known as:

  • ER aminopeptidase 1 (ERAP1) the name accepted by the Hugo Gene Nomenclature Committee[2]
  • ER aminopeptidase associated with antigen processing (ERAAP)
  • Adipocyte-derived leucine aminopeptidase (ALAP)
  • Puromycin-insensitive leucine aminopeptidase (PILS-AP)

Function

ERAP1 has two major functions in the immune system:

  • First, ERAP1 cleaves several proteins called cytokine receptors on the surface of cells. Cleaving these receptors reduces their ability to transmit chemical signals into the cell, which affects the process of inflammation.
  • Second, ERAP1 trims peptides within the endoplasmic reticulum so that they can be loaded onto major histocompatibility complex (MHC) class I. These peptides are attached to MHC class I in the endoplasmic reticulum and exported to the cell surface, where they are displayed to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by triggering the infected cell to self-destruct.[3]

ARTS-1 is a member of the M1 family of zinc metallopeptidases which acts as an aminopeptidase that degrades oligopeptides by cleavage starting at the amino terminus. One of the functions of aminopeptidases is to degrade potentially toxic peptides in the cytosol.[1]

ARTS-1 is a transmembrane protein that is localized to the endoplasmic reticulum. It has been implicated in the following functions:

Clinical significance

Aminopeptidases play a role in the metabolism of several peptides that may be involved in blood pressure and the pathogenesis of essential hypertension.[1] Mutations in the ARTS-1 have been linked to an increased risk of ankylosing spondylitis but only in HLA-B27 positive patients .[4]

The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.[1]

References

  1. ^ a b c d EntrezGene 51752
  2. ^ "HGNC publisher=HGNC". Retrieved 27 March 2014. 
  3. ^ "ERAP1 - endoplasmic reticulum aminopeptidase 1 - Genetics Home Reference". 
  4. ^ Brionez TF, Reveille JD (2008). "The contribution of genes outside the major histocompatibility complex to susceptibility to ankylosing spondylitis". Current Opinion in Rheumatology 20 (4): 384–91. PMID 18525349. doi:10.1097/BOR.0b013e32830460fe. 

Further reading

</dl>

Lua error in package.lua at line 80: module 'Module:Buffer' not found.