MFAP5

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Microfibrillar associated protein 5
Identifiers
Symbol(s) MFAP5; MAGP2; MP25
External IDs OMIM: 601103 MGI: 1354387 HomoloGene: 2599
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 8076 50530
Ensembl ENSG00000197614 ENSMUSG00000030116
Uniprot Q13361 Q9QZJ6
Refseq NM_003480 (mRNA)
NP_003471 (protein)		 NM_015776 (mRNA)
NP_056591 (protein)
Location Chr 12: 8.69 - 8.71 Mb Chr 6: 122.48 - 122.49 Mb
Pubmed search [1] [2]

Microfibrillar associated protein 5, also known as MFAP5, is a human gene.[1]

This gene encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. It lacks a hydrophobic carboxyl terminus and proline-, glutamine-, and tyrosine-rich regions, which are characteristics of a related 31-kDa microfibril-associated glycoprotein (MFAP2). The close similarity between these two proteins is confined to a central region of 60 aa where precise alignment of 7 cysteine residues occurs. The structural differences suggest that this encoded protein has some functions that are distinct from those of MFAP2.[1]

[edit] References

  1. ^ a b Entrez Gene: MFAP5 microfibrillar associated protein 5.

[edit] Further reading

  • Miyamoto A, Lau R, Hein PW, et al. (2006). "Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation.". J. Biol. Chem. 281 (15): 10089-97. doi:10.1074/jbc.M600298200. PMID 16492672. 
  • 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. 
  • Imabayashi H, Mori T, Gojo S, et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis.". Exp. Cell Res. 288 (1): 35-50. PMID 12878157. 
  • 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. 
  • Penner AS, Rock MJ, Kielty CM, Shipley JM (2002). "Microfibril-associated glycoprotein-2 interacts with fibrillin-1 and fibrillin-2 suggesting a role for MAGP-2 in elastic fiber assembly.". J. Biol. Chem. 277 (38): 35044-9. doi:10.1074/jbc.M206363200. PMID 12122015. 
  • Hatzinikolas G, Gibson MA (1998). "The exon structure of the human MAGP-2 gene. Similarity with the MAGP-1 gene is confined to two exons encoding a cysteine-rich region.". J. Biol. Chem. 273 (45): 29309-14. PMID 9792630. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548. 
  • Gibson MA, Hatzinikolas G, Kumaratilake JS, et al. (1996). "Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)". J. Biol. Chem. 271 (2): 1096-103. PMID 8557636. 
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