AMFR

AMFR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAMFR, GP78, RNF45, autocrine motility factor receptor
External IDsMGI: 1345634 HomoloGene: 888 GeneCards: AMFR
Gene location (Human)
Chr.Chromosome 16 (human)[1]
Band16q13Start56,361,452 bp[1]
End56,425,538 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

267

23802

Ensembl

ENSG00000159461

ENSMUSG00000031751

UniProt

Q9UKV5

Q9R049

RefSeq (mRNA)

NM_001144
NM_138958
NM_001323511
NM_001323512

NM_011787

RefSeq (protein)

NP_001135
NP_001310440
NP_001310441

NP_035917

Location (UCSC)Chr 16: 56.36 – 56.43 MbChr 8: 93.97 – 94.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Autocrine motility factor receptor, isoform 2 is a protein that in humans is encoded by the AMFR gene.[5][6]

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.[6]

Model organisms

Model organisms have been used in the study of AMFR function. A conditional knockout mouse line, called Amfrtm1a(KOMP)Wtsi[11][12] 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.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty six tests were carried out on mutant mice and one significant abnormality was observed: Fewer than expected homozygous mutant mice survived until weaning.[9]

Interactions

AMFR has been shown to interact with Valosin-containing protein.[17][18]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000159461 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031751 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. 1 2 "Entrez Gene: AMFR autocrine motility factor receptor".
  7. ↑ "Salmonella infection data for Amfr". Wellcome Trust Sanger Institute.
  8. ↑ "Citrobacter infection data for Amfr". Wellcome Trust Sanger Institute.
  9. 1 2 3 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.
  10. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  11. ↑ "International Knockout Mouse Consortium".
  12. ↑ "Mouse Genome Informatics".
  13. ↑ 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.
  14. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  15. ↑ 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.
  16. ↑ 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.
  17. ↑ 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.
  18. ↑ 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

  • Huang B, Xie Y, Raz A (1995). "Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor". Biochem. Biophys. Res. Commun. 212 (3): 727–42. doi:10.1006/bbrc.1995.2031. PMID 7626106.
  • Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
  • Shimizu K, Tani M, Watanabe H, et al. (1999). "The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein". FEBS Lett. 456 (2): 295–300. doi:10.1016/S0014-5793(99)00966-7. PMID 10456327.
  • Fang S, Ferrone M, Yang C, et al. (2002). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14422–7. Bibcode:2001PNAS...9814422F. doi:10.1073/pnas.251401598. PMC 64697. PMID 11724934.
  • Luo Y, Long JM, Lu C, et al. (2002). "A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78". J. Neurochem. 80 (2): 354–61. doi:10.1046/j.0022-3042.2001.00707.x. PMID 11902125.
  • Tímár J, Rásó E, Döme B, et al. (2002). "Expression and function of the AMF receptor by human melanoma in experimental and clinical systems". Clin. Exp. Metastasis. 19 (3): 225–32. doi:10.1023/A:1015595708241. PMID 12067203.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Liang JS, Kim T, Fang S, et al. (2003). "Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells". J. Biol. Chem. 278 (26): 23984–8. doi:10.1074/jbc.M302683200. PMID 12670940.
  • Takanami I, Takeuchi K (2003). "Autocrine motility factor-receptor gene expression in lung cancer". Jpn. J. Thorac. Cardiovasc. Surg. 51 (8): 368–73. doi:10.1007/BF02719469. PMID 12962414.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Registre M, Goetz JG, St Pierre P, et al. (2004). "The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum". Biochem. Biophys. Res. Commun. 320 (4): 1316–22. doi:10.1016/j.bbrc.2004.06.089. PMID 15303277.
  • Zhong X, Shen Y, Ballar P, et al. (2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation". J. Biol. Chem. 279 (44): 45676–84. doi:10.1074/jbc.M409034200. PMID 15331598.
  • 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. PMC 528928. PMID 15489334.
  • Song BL, Sever N, DeBose-Boyd RA (2005). "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase". Mol. Cell. 19 (6): 829–40. doi:10.1016/j.molcel.2005.08.009. PMID 16168377.
  • Kaynak K, Kara M, Oz B, et al. (2006). "Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas". Acta Chir. Belg. 105 (4): 378–82. PMID 16184720.
  • Ye Y, Shibata Y, Kikkert M, et al. (2006). "Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. Bibcode:2005PNAS..10214132Y. doi:10.1073/pnas.0505006102. PMC 1242302. PMID 16186510.
  • Chen B, Mariano J, Tsai YC, et al. (2006). "The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site". Proc. Natl. Acad. Sci. U.S.A. 103 (2): 341–6. Bibcode:2006PNAS..103..341C. doi:10.1073/pnas.0506618103. PMC 1326157. PMID 16407162.
  • Haga A, Tanaka N, Funasaka T, et al. (2006). "The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF". J. Mol. Biol. 358 (3): 741–53. doi:10.1016/j.jmb.2006.02.046. PMID 16563432.
  • Shen Y, Ballar P, Fang S (2006). "Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin". Biochem. Biophys. Res. Commun. 349 (4): 1285–93. doi:10.1016/j.bbrc.2006.08.173. PMID 16979136.
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