AMFR

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

AMFR
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2EJS, 2LVN, 2LVO, 2LVP, 2LVQ, 2LXH, 2LXP, 3FSH, 3H8K, 3TIW, 4G3O, 4LAD
Identifiers
Aliases	AMFR, GP78, RNF45, autocrine motility factor receptor
External IDs	OMIM: 603243 MGI: 1345634 HomoloGene: 888 GeneCards: AMFR
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q13 Start 56,361,452 bp[1] End 56,425,545 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 C5|8 45.96 cM Start 93,971,588 bp[2] End 94,012,842 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein binding, bridging • chaperone binding • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • metal ion binding • ubiquitin-protein transferase activity • ubiquitin-ubiquitin ligase activity • GO:0001948 protein binding • ubiquitin-specific protease binding • receptor activity • transferase activity • identical protein binding • BAT3 complex binding • signaling receptor activity Cellular component • cytoplasm • integral component of membrane • membrane • growth cone • integral component of endoplasmic reticulum membrane • neuronal cell body • dendrite • Derlin-1 retrotranslocation complex • perinuclear region of cytoplasm • cell nucleus • endoplasmic reticulum • endoplasmic reticulum membrane • Golgi apparatus • endoplasmic reticulum quality control compartment • macromolecular complex • ubiquitin ligase complex • cytosol Biological process • movement of cell or subcellular component • ERAD pathway • ubiquitin-dependent protein catabolic process • aging • protein polyubiquitination • endoplasmic reticulum unfolded protein response • protein K48-linked ubiquitination • protein oligomerization • protein ubiquitination • ubiquitin-dependent ERAD pathway • learning or memory • positive regulation of protein binding • signal transduction • protein autoubiquitination • protein folding • endoplasmic reticulum mannose trimming Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
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 Mb	Chr 8: 93.97 – 94.01 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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

Amfr knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[7]
Citrobacter infection	Normal[8]
All tests and analysis from[9][10]

Model organisms have been used in the study of AMFR function. A conditional knockout mouse line, called Amfr^{tm1a(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. GRCh38: Ensembl release 89: ENSG00000159461 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031751 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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. "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. 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.

External links

• Human AMFR genome location and AMFR gene details page in the UCSC Genome Browser.

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.