ARTS-1

From Wikipedia, the free encyclopedia

Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator

Identifiers

ARTS-1; A-LAP; ALAP; APPILS; ARTS1; ERAAP; ERAP1; KIAA0525; PILSAP

External IDs

OMIM: 606832 MGI: 1933403 HomoloGene: 56754

Gene ontology
Molecular Function:	• leucyl aminopeptidase activity • membrane alanyl aminopeptidase activity • methionyl aminopeptidase activity • interleukin-6 receptor binding • interleukin-1, Type II receptor binding • protein binding • metallopeptidase activity • zinc ion binding • metal ion binding
Cellular Component:	• extracellular region • cytoplasm • endoplasmic reticulum • endoplasmic reticulum lumen • cytosol • integral to membrane
Biological Process:	• angiogenesis • membrane protein ectodomain proteolysis • blood pressure regulation • antigen processing and presentation of endogenous peptide antigen via MHC class I • regulation of innate immune response • fat cell differentiation • positive regulation of angiogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001040458 (mRNA)
NP_001035548 (protein)

NM_030711 (mRNA)
NP_109636 (protein)

Location

Chr 5: 96.12 - 96.17 Mb

Chr 13: 75.11 - 75.16 Mb

Pubmed search

[1]

[2]

Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, also known as ARTS-1, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: ARTS-1 type 1 tumor necrosis factor receptor shedding aminopeptidase regulator.

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Tsujimoto M, Hattori A (2005). "The oxytocinase subfamily of M1 aminopeptidases.". Biochim. Biophys. Acta 1751 (1): 9–18. doi:10.1016/j.bbapap.2004.09.011. PMID 16054015.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Nagase T, Ishikawa K, Miyajima N, et al. (1998). "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.". DNA Res. 5 (1): 31–9. PMID 9628581.
Hattori A, Matsumoto H, Mizutani S, Tsujimoto M (1999). "Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase.". J. Biochem. 125 (5): 931–8. PMID 10220586.
Hattori A, Kitatani K, Matsumoto H, et al. (2001). "Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells.". J. Biochem. 128 (5): 755–62. PMID 11056387.
Hattori A, Matsumoto K, Mizutani S, Tsujimoto M (2001). "Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene.". J. Biochem. 130 (2): 235–41. PMID 11481040.
Yamamoto N, Nakayama J, Yamakawa-Kobayashi K, et al. (2002). "Identification of 33 polymorphisms in the adipocyte-derived leucine aminopeptidase (ALAP) gene and possible association with hypertension.". Hum. Mutat. 19 (3): 251–7. doi:10.1002/humu.10047. PMID 11857741.
Cui X, Hawari F, Alsaaty S, et al. (2002). "Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding.". J. Clin. Invest. 110 (4): 515–26. PMID 12189246.
Serwold T, Gonzalez F, Kim J, et al. (2002). "ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum.". Nature 419 (6906): 480–3. doi:10.1038/nature01074. PMID 12368856.
Saric T, Chang SC, Hattori A, et al. (2002). "An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides.". Nat. Immunol. 3 (12): 1169–76. doi:10.1038/ni859. PMID 12436109.
York IA, Chang SC, Saric T, et al. (2002). "The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues.". Nat. Immunol. 3 (12): 1177–84. doi:10.1038/ni860. PMID 12436110.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Cui X, Rouhani FN, Hawari F, Levine SJ (2003). "An aminopeptidase, ARTS-1, is required for interleukin-6 receptor shedding.". J. Biol. Chem. 278 (31): 28677–85. doi:10.1074/jbc.M300456200. PMID 12748171.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
Cui X, Rouhani FN, Hawari F, Levine SJ (2004). "Shedding of the type II IL-1 decoy receptor requires a multifunctional aminopeptidase, aminopeptidase regulator of TNF receptor type 1 shedding.". J. Immunol. 171 (12): 6814–9. PMID 14662887.
Shibata D, Ando H, Iwase A, et al. (2004). "Distribution of adipocyte-derived leucine aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in human uterine endometrium.". J. Histochem. Cytochem. 52 (9): 1169–75. doi:10.1369/jhc.3A6216.2004. PMID 15314084.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.