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{{Infobox_gene}}
{{PBB_Controls
'''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]].<ref name="entrez">{{EntrezGene|51752}}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
| HGNCid = 
| Symbol = ARTS-1
| AltSymbols =; A-LAP; ALAP; APPILS; ARTS1; ERAAP; ERAP1; KIAA0525; PILSAP
| OMIM = 606832
| ECnumber = 
| Homologene = 56754
| MGIid = 1933403
| GeneAtlas_image1 = PBB_GE_ARTS-1_214012_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARTS-1_214034_at_tn.png
| Function = {{GNF_GO|id=GO:0004178 |text = leucyl aminopeptidase activity}} {{GNF_GO|id=GO:0004179 |text = membrane alanyl aminopeptidase activity}} {{GNF_GO|id=GO:0004239 |text = methionyl aminopeptidase activity}} {{GNF_GO|id=GO:0005138 |text = interleukin-6 receptor binding}} {{GNF_GO|id=GO:0005151 |text = interleukin-1, Type II receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005788 |text = endoplasmic reticulum lumen}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006509 |text = membrane protein ectodomain proteolysis}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0019885 |text = antigen processing and presentation of endogenous peptide antigen via MHC class I}} {{GNF_GO|id=GO:0045088 |text = regulation of innate immune response}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} {{GNF_GO|id=GO:0045766 |text = positive regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51752
    | Hs_Ensembl = ENSG00000164307
    | Hs_RefseqProtein = NP_001035548
    | Hs_RefseqmRNA = NM_001040458
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 96122277
    | Hs_GenLoc_end = 96169559
    | Hs_Uniprot = Q9NZ08
    | Mm_EntrezGene = 80898
    | Mm_Ensembl = ENSMUSG00000021583
    | Mm_RefseqmRNA = NM_030711
    | Mm_RefseqProtein = NP_109636
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 75105875
    | Mm_GenLoc_end = 75158537
    | Mm_Uniprot = Q6GTP5
  }}
}}
'''Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator''', also known as '''ARTS-1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARTS-1 type 1 tumor necrosis factor receptor shedding aminopeptidase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51752| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Nomenclature ==
{{PBB_Summary
ARTS1 is also known as:  
| section_title =
* ER aminopeptidase 1 (ERAP1) the name accepted by the Hugo Gene Nomenclature Committee<ref name="HGNC ERAP1">{{cite web|url=http://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=18173  |title=HGNC |publisher=HGNC|accessdate=27 March 2014}}</ref>
| summary_text = Aminopeptidases play a role in the metabolism of several peptides that may be involved in blood pressure and the pathogenesis of essential hypertension (MIM 145500). Adipocyte-derived leucine aminopeptidase (ALAP) is a member of the M1 family of zinc metallopeptidases.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: ARTS-1 type 1 tumor necrosis factor receptor shedding aminopeptidase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51752| accessdate = }}</ref>
* ER aminopeptidase associated with antigen processing (ERAAP)
}}
* Adipocyte-derived leucine aminopeptidase (ALAP)
* Puromycin-insensitive leucine aminopeptidase (PILS-AP)


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
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.<ref name="urlERAP1 - endoplasmic reticulum aminopeptidase 1 - Genetics Home Reference">{{cite web |url=http://ghr.nlm.nih.gov/gene/ERAP1 |title=ERAP1 - endoplasmic reticulum aminopeptidase 1 - Genetics Home Reference |format= |work= |accessdate=}}</ref>
 
ARTS-1  is a member of the M1 family of zinc [[metalloproteinase|metallopeptidase]]s which acts as an [[aminopeptidase]] that degrades oligopeptides by cleavage starting at the [[N-terminus|amino terminus]].  One of the functions of aminopeptidases is to degrade potentially toxic peptides in the [[cytosol]].<ref name="entrez"/>
 
ARTS-1 is a transmembrane protein that is localized to the [[endoplasmic reticulum]].  It has been implicated in the following functions:
* Shedding of various [[cytokine receptor]]s and decoy receptors
* Trimming of antigenic peptides before binding to [[MHC class I]], affecting antigen presentation to [[cytotoxic T cell|cytotoxic T lymphocyte]]s
 
== Clinical significance ==
 
Aminopeptidases play a role in the metabolism of several peptides that may be involved in [[blood pressure]] and the [[pathogenesis]] of [[Hypertension#Essential .28primary.29 hypertension|essential hypertension]].<ref name="entrez"/> Mutations in the ARTS-1 have been linked to an increased risk of [[ankylosing spondylitis]] but only in [[HLA-B27]] positive patients .<ref name="pmid18525349">{{cite journal | vauthors = Brionez TF, Reveille JD | title = The contribution of genes outside the major histocompatibility complex to susceptibility to ankylosing spondylitis | journal = Current Opinion in Rheumatology | volume = 20 | issue = 4 | pages = 384–91 | year = 2008 | pmid = 18525349 | doi = 10.1097/BOR.0b013e32830460fe }}</ref>
 
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.<ref name="entrez"/>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ERAP1}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T | title = Construction of Expression-ready cDNA Clones for KIAA Genes: Manual Curation of 330 KIAA cDNA Clones | journal = DNA Research | volume = 9 | issue = 3 | pages = 99–106 | year = 2002 | pmid = 12168954 | doi = 10.1093/dnares/9.3.99 }}
| citations =
* {{cite journal | vauthors = Tsujimoto M, Hattori A | title = The oxytocinase subfamily of M1 aminopeptidases | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1751 | pages = 9–18 | year = 2005 | pmid = 16054015 | doi = 10.1016/j.bbapap.2004.09.011 }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Tsujimoto M, Hattori A |title=The oxytocinase subfamily of M1 aminopeptidases. |journal=Biochim. Biophys. Acta |volume=1751 |issue= 1 |pages= 9-18 |year= 2005 |pmid= 16054015 |doi= 10.1016/j.bbapap.2004.09.011 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the Coding Sequences of Unidentified Human Genes. IX. The Complete Sequences of 100 New cDNA Clones from Brain Which Can Code for Large Proteins in vitro | journal = DNA Research | volume = 5 | issue = 1 | pages = 31–9 | year = 1998 | pmid = 9628581 | doi = 10.1093/dnares/5.1.31 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Hattori A, Matsumoto H, Mizutani S, Tsujimoto M | title = Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase | journal = Journal of Biochemistry | volume = 125 | issue = 5 | pages = 931–8 | year = 1999 | pmid = 10220586 | doi = 10.1093/oxfordjournals.jbchem.a022371 }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
* {{cite journal | vauthors = Hattori A, Kitatani K, Matsumoto H, Miyazawa S, Rogi T, Tsuruoka N, Mizutani S, Natori Y, Tsujimoto M | title = Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells | journal = Journal of Biochemistry | volume = 128 | issue = 5 | pages = 755–62 | year = 2000 | pmid = 11056387 | doi = 10.1093/oxfordjournals.jbchem.a022812 }}
*{{cite journal | author=Hattori A, Matsumoto H, Mizutani S, Tsujimoto M |title=Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase. |journal=J. Biochem. |volume=125 |issue= 5 |pages= 931-8 |year= 1999 |pmid= 10220586 |doi= }}
* {{cite journal | vauthors = Hattori A, Matsumoto K, Mizutani S, Tsujimoto M | title = Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene | journal = Journal of Biochemistry | volume = 130 | issue = 2 | pages = 235–41 | year = 2001 | pmid = 11481040 | doi = 10.1093/oxfordjournals.jbchem.a002977 }}
*{{cite journal | author=Hattori A, Kitatani K, Matsumoto H, ''et al.'' |title=Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells. |journal=J. Biochem. |volume=128 |issue= 5 |pages= 755-62 |year= 2001 |pmid= 11056387 |doi= }}
* {{cite journal | vauthors = Yamamoto N, Nakayama J, Yamakawa-Kobayashi K, Hamaguchi H, Miyazaki R, Arinami T | title = Identification of 33 polymorphisms in the adipocyte-derived leucine aminopeptidase (ALAP) gene and possible association with hypertension | journal = Human Mutation | volume = 19 | issue = 3 | pages = 251–7 | year = 2002 | pmid = 11857741 | doi = 10.1002/humu.10047 }}
*{{cite journal | author=Hattori A, Matsumoto K, Mizutani S, Tsujimoto M |title=Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene. |journal=J. Biochem. |volume=130 |issue= 2 |pages= 235-41 |year= 2001 |pmid= 11481040 |doi= }}
* {{cite journal | vauthors = Cui X, Hawari F, Alsaaty S, Lawrence M, Combs CA, Geng W, Rouhani FN, Miskinis D, Levine SJ | title = Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding | journal = Journal of Clinical Investigation | volume = 110 | issue = 4 | pages = 515–26 | year = 2002 | pmid = 12189246 | pmc = 150410 | doi = 10.1172/JCI13847 }}
*{{cite journal | author=Yamamoto N, Nakayama J, Yamakawa-Kobayashi K, ''et al.'' |title=Identification of 33 polymorphisms in the adipocyte-derived leucine aminopeptidase (ALAP) gene and possible association with hypertension. |journal=Hum. Mutat. |volume=19 |issue= 3 |pages= 251-7 |year= 2002 |pmid= 11857741 |doi= 10.1002/humu.10047 }}
* {{cite journal | vauthors = Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N | title = ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum | journal = Nature | volume = 419 | issue = 6906 | pages = 480–3 | year = 2002 | pmid = 12368856 | doi = 10.1038/nature01074 }}
*{{cite journal | author=Cui X, Hawari F, Alsaaty S, ''et al.'' |title=Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding. |journal=J. Clin. Invest. |volume=110 |issue= 4 |pages= 515-26 |year= 2002 |pmid= 12189246 |doi= }}
* {{cite journal | vauthors = Saric T, Chang SC, Hattori A, York IA, Markant S, Rock KL, Tsujimoto M, Goldberg AL | title = An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides | journal = Nature Immunology | volume = 3 | issue = 12 | pages = 1169–76 | year = 2002 | pmid = 12436109 | doi = 10.1038/ni859 }}
*{{cite journal | author=Serwold T, Gonzalez F, Kim J, ''et al.'' |title=ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. |journal=Nature |volume=419 |issue= 6906 |pages= 480-3 |year= 2002 |pmid= 12368856 |doi= 10.1038/nature01074 }}
* {{cite journal | vauthors = York IA, Chang SC, Saric T, Keys JA, Favreau JM, Goldberg AL, Rock KL | title = The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8–9 residues | journal = Nature Immunology | volume = 3 | issue = 12 | pages = 1177–84 | year = 2002 | pmid = 12436110 | doi = 10.1038/ni860 }}
*{{cite journal | author=Saric T, Chang SC, Hattori A, ''et al.'' |title=An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. |journal=Nat. Immunol. |volume=3 |issue= 12 |pages= 1169-76 |year= 2002 |pmid= 12436109 |doi= 10.1038/ni859 }}
* {{cite journal | vauthors = Cui X, Rouhani FN, Hawari F, Levine SJ | title = An Aminopeptidase, ARTS-1, Is Required for Interleukin-6 Receptor Shedding | journal = Journal of Biological Chemistry | volume = 278 | issue = 31 | pages = 28677–85 | year = 2003 | pmid = 12748171 | doi = 10.1074/jbc.M300456200 }}
*{{cite journal | author=York IA, Chang SC, Saric T, ''et al.'' |title=The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. |journal=Nat. Immunol. |volume=3 |issue= 12 |pages= 1177-84 |year= 2002 |pmid= 12436110 |doi= 10.1038/ni860 }}
* {{cite journal | vauthors = Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A | title = The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment | journal = Genome Research | volume = 13 | issue = 10 | pages = 2265–70 | year = 2003 | pmid = 12975309 | pmc = 403697 | doi = 10.1101/gr.1293003 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Cui X, Rouhani FN, Hawari F, Levine SJ | title = Shedding of the Type II IL-1 Decoy Receptor Requires a Multifunctional Aminopeptidase, Aminopeptidase Regulator of TNF Receptor Type 1 Shedding | journal = The Journal of Immunology | volume = 171 | issue = 12 | pages = 6814–9 | year = 2003 | pmid = 14662887 | doi = 10.4049/jimmunol.171.12.6814 | url = http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=14662887 }}
*{{cite journal  | author=Cui X, Rouhani FN, Hawari F, Levine SJ |title=An aminopeptidase, ARTS-1, is required for interleukin-6 receptor shedding. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28677-85 |year= 2003 |pmid= 12748171 |doi= 10.1074/jbc.M300456200 }}
* {{cite journal | vauthors = Shibata D, Ando H, Iwase A, Nagasaka T, Hattori A, Tsujimoto M, Mizutani S | title = Distribution of Adipocyte-derived Leucine Aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in Human Uterine Endometrium | journal = Journal of Histochemistry and Cytochemistry | volume = 52 | issue = 9 | pages = 1169–75 | year = 2004 | pmid = 15314084 | doi = 10.1369/jhc.3A6216.2004 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Cui X, Rouhani FN, Hawari F, Levine SJ |title=Shedding of the type II IL-1 decoy receptor requires a multifunctional aminopeptidase, aminopeptidase regulator of TNF receptor type 1 shedding. |journal=J. Immunol. |volume=171 |issue= 12 |pages= 6814-9 |year= 2004 |pmid= 14662887 |doi= }}
*{{cite journal | author=Shibata D, Ando H, Iwase A, ''et al.'' |title=Distribution of adipocyte-derived leucine aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in human uterine endometrium. |journal=J. Histochem. Cytochem. |volume=52 |issue= 9 |pages= 1169-75 |year= 2004 |pmid= 15314084 |doi= 10.1369/jhc.3A6216.2004 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
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Latest revision as of 20:39, 10 May 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 1.0 1.1 1.2 1.3 EntrezGene 51752
  2. ↑ "HGNC". 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. doi:10.1097/BOR.0b013e32830460fe. PMID 18525349.

External links

Further reading

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