AMFR

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Autocrine motility factor receptor, E3 ubiquitin protein ligase
Protein AMFR PDB 2EJS.png
Rendering based on PDB 2EJS.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols AMFR ; GP78; RNF45
External IDs OMIM603243 MGI1345634 HomoloGene888 GeneCards: AMFR Gene
EC number 6.3.2.19
RNA expression pattern
PBB GE AMFR 202203 s at tn.png
PBB GE AMFR 202204 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 267 23802
Ensembl ENSG00000159461 ENSMUSG00000031751
UniProt Q9UKV5 Q9R049
RefSeq (mRNA) NM_001144 NM_011787
RefSeq (protein) NP_001135 NP_035917
Location (UCSC) Chr 16:
56.4 – 56.46 Mb
Chr 8:
93.97 – 94.01 Mb
PubMed search [1] [2]

Autocrine motility factor receptor, isoform 2 is a protein that in humans is encoded by the AMFR gene.[1][2]

Autocrine motility factor is a tumor motility-stimulating protein secreted by tumor cells. The protein encoded by this gene is a glycosylated transmembrane protein and a receptor for autocrine motility factor. The receptor, which shows some sequence similarity to tumor protein p53, is localized to the leading and trailing edges of carcinoma cells.[2]

Model organisms[edit]

Model organisms have been used in the study of AMFR function. A conditional knockout mouse line, called Amfrtm1a(KOMP)Wtsi[7][8] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[9][10][11]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[5][12] Twenty six tests were carried out on mutant mice and one significant abnormality was observed: Fewer than expected homozygous mutant mice survived until weaning.[5]

Interactions[edit]

AMFR has been shown to interact with Valosin-containing protein.[13][14]

References[edit]

  1. ^ Watanabe H, Carmi P, Hogan V, Raz T, Silletti S, Nabi IR, Raz A (Aug 1991). "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor". J Biol Chem 266 (20): 13442–8. PMID 1649192. 
  2. ^ a b "Entrez Gene: AMFR autocrine motility factor receptor". 
  3. ^ "Salmonella infection data for Amfr". Wellcome Trust Sanger Institute. 
  4. ^ "Citrobacter infection data for Amfr". Wellcome Trust Sanger Institute. 
  5. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  6. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  7. ^ "International Knockout Mouse Consortium". 
  8. ^ "Mouse Genome Informatics". 
  9. ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.  edit
  10. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  11. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  12. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  13. ^ Zhong, Xiaoyan; Shen Yuxian; Ballar Petek; Apostolou Andria; Agami Reuven; Fang Shengyun (Oct 2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation". J. Biol. Chem. (United States) 279 (44): 45676–84. doi:10.1074/jbc.M409034200. ISSN 0021-9258. PMID 15331598. 
  14. ^ Lee, Joon No; Zhang Xiangyu; Feramisco Jamison D; Gong Yi; Ye Jin (Nov 2008). "Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step". J. Biol. Chem. (United States) 283 (48): 33772–83. doi:10.1074/jbc.M806108200. ISSN 0021-9258. PMC 2586246. PMID 18835813. 

Further reading[edit]