MATN3

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Matrilin 3
Identifiers
Symbols	MATN3 ; DIPOA; EDM5; HOA; OADIP; OS2
External IDs	OMIM: 602109 MGI: 1328350 HomoloGene: 1785 GeneCards: MATN3 Gene
Gene ontology Molecular function • extracellular matrix structural constituent • calcium ion binding • protein binding Cellular component • extracellular region • proteinaceous extracellular matrix Biological process • skeletal system development • chondrocyte differentiation • extracellular matrix organization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4148	17182
Ensembl	ENSG00000132031	ENSMUSG00000020583
UniProt	O15232	O35701
RefSeq (mRNA)	NM_002381	NM_010770
RefSeq (protein)	NP_002372	NP_034900
Location (UCSC)	Chr 2: 19.99 – 20.01 Mb	Chr 12: 8.95 – 8.97 Mb
PubMed search

Matrilin-3 is a protein that in humans is encoded by the MATN3 gene.^[1][2][3]

This gene encodes a member of von Willebrand factor A domain containing protein family. This family of proteins is thought to be involved in the formation of filamentous networks in the extracellular matrices of various tissues. This protein contains two von Willebrand factor A domains; it is present in the cartilage extracellular matrix and has a role in the development and homeostasis of cartilage and bone. Mutations in this gene result in multiple epiphyseal dysplasia.^[3]

References

1. Wagener R, Kobbe B, Paulsson M (Oct 1997). "Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor". FEBS Lett 413 (1): 129–34. doi:10.1016/S0014-5793(97)00895-8. PMID 9287130.
2. Belluoccio D, Trueb B (Nov 1997). "Matrilin-3 from chicken cartilage". FEBS Lett 415 (2): 212–6. doi:10.1016/S0014-5793(97)01126-5. PMID 9350998.
3. "Entrez Gene: MATN3 matrilin 3".

External links

• GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant

Further reading

• Belluoccio D, Schenker T, Baici A, Trueb B (1998). "Characterization of human matrilin-3 (MATN3).". Genomics 53 (3): 391–4. doi:10.1006/geno.1998.5519. PMID 9799608.
• "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Chapman KL, Mortier GR, Chapman K, et al. (2001). "Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia.". Nat. Genet. 28 (4): 393–6. doi:10.1038/ng573. PMID 11479597.
• Frank S, Schulthess T, Landwehr R, et al. (2002). "Characterization of the matrilin coiled-coil domains reveals seven novel isoforms.". J. Biol. Chem. 277 (21): 19071–9. doi:10.1074/jbc.M202146200. PMID 11896063.
• Stefánsson SE, Jónsson H, Ingvarsson T, et al. (2003). "Genomewide scan for hand osteoarthritis: a novel mutation in matrilin-3.". Am. J. Hum. Genet. 72 (6): 1448–59. doi:10.1086/375556. PMC 1180305. PMID 12736871.
• Jackson GC, Barker FS, Jakkula E, et al. (2004). "Missense mutations in the beta strands of the single A-domain of matrilin-3 result in multiple epiphyseal dysplasia.". J. Med. Genet. 41 (1): 52–9. doi:10.1136/jmg.2003.011429. PMC 1757268. PMID 14729835.
• Mäkitie O, Mortier GR, Czarny-Ratajczak M, et al. (2004). "Clinical and radiographic findings in multiple epiphyseal dysplasia caused by MATN3 mutations: description of 12 patients.". Am. J. Med. Genet. A 125 (3): 278–84. doi:10.1002/ajmg.a.20486. PMID 14994237.
• Borochowitz ZU, Scheffer D, Adir V, et al. (2004). "Spondylo-epi-metaphyseal dysplasia (SEMD) matrilin 3 type: homozygote matrilin 3 mutation in a novel form of SEMD.". J. Med. Genet. 41 (5): 366–72. doi:10.1136/jmg.2003.013342. PMC 1735768. PMID 15121775.
• Mabuchi A, Haga N, Maeda K, et al. (2005). "Novel and recurrent mutations clustered in the von Willebrand factor A domain of MATN3 in multiple epiphyseal dysplasia.". Hum. Mutat. 24 (5): 439–40. doi:10.1002/humu.9286. PMID 15459972.
• Hecht JT, Hayes E, Haynes R, Cole WG (2005). "COMP mutations, chondrocyte function and cartilage matrix.". Matrix Biol. 23 (8): 525–33. doi:10.1016/j.matbio.2004.09.006. PMID 15694129.
• Otten C, Wagener R, Paulsson M, Zaucke F (2006). "Matrilin-3 mutations that cause chondrodysplasias interfere with protein trafficking while a mutation associated with hand osteoarthritis does not.". J. Med. Genet. 42 (10): 774–9. doi:10.1136/jmg.2004.029462. PMC 1735938. PMID 16199550.
• Cotterill SL, Jackson GC, Leighton MP, et al. (2006). "Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3.". Hum. Mutat. 26 (6): 557–65. doi:10.1002/humu.20263. PMC 2726956. PMID 16287128.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Eliasson GJ, Verbruggen G, Stefansson SE, et al. (2006). "Hand radiology characteristics of patients carrying the T(303)M mutation in the gene for matrilin-3.". Scand. J. Rheumatol. 35 (2): 138–42. doi:10.1080/03009740500303215. PMID 16641049.
• Maeda K, Horikoshi T, Nakashima E, et al. (2007). "MATN and LAPTM are parts of larger transcription units produced by intergenic splicing: intergenic splicing may be a common phenomenon.". DNA Res. 12 (5): 365–72. doi:10.1093/dnares/dsi017. PMID 16769693.
• Hills R, Mazzarella R, Fok K, et al. (2007). "Identification of an ADAMTS-4 cleavage motif using phage display leads to the development of fluorogenic peptide substrates and reveals matrilin-3 as a novel substrate.". J. Biol. Chem. 282 (15): 11101–9. doi:10.1074/jbc.M611588200. PMID 17311924.
• Leighton MP, Nundlall S, Starborg T, et al. (2007). "Decreased chondrocyte proliferation and dysregulated apoptosis in the cartilage growth plate are key features of a murine model of epiphyseal dysplasia caused by a matn3 mutation.". Hum. Mol. Genet. 16 (14): 1728–41. doi:10.1093/hmg/ddm121. PMC 2674230. PMID 17517694.