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{{Infobox_gene}}
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'''Autocrine motility factor receptor, isoform 2''' is a [[protein]] that in humans is encoded by the ''AMFR'' [[gene]].<ref name="pmid1649192">{{cite journal | vauthors = Watanabe H, Carmi P, Hogan V, Raz T, Silletti S, Nabi IR, Raz A | title = Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor | journal = J Biol Chem | volume = 266 | issue = 20 | pages = 13442–8 |date=Aug 1991 | pmid = 1649192 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AMFR autocrine motility factor receptor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=267| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Autocrine motility factor receptor
| HGNCid = 463
| Symbol = AMFR
| AltSymbols =; GP78; RNF45
| OMIM = 603243
| ECnumber = 
| Homologene = 888
| MGIid = 1345634
| GeneAtlas_image1 = PBB_GE_AMFR_202203_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AMFR_202204_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030176 |text = integral to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0030433 |text = ER-associated protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 267
    | Hs_Ensembl = ENSG00000159461
    | Hs_RefseqProtein = NP_001135
    | Hs_RefseqmRNA = NM_001144
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 54952865
    | Hs_GenLoc_end = 55016804
    | Hs_Uniprot = Q9UKV5
    | Mm_EntrezGene = 23802
    | Mm_Ensembl = ENSMUSG00000031751
    | Mm_RefseqmRNA = XM_990903
    | Mm_RefseqProtein = XP_995997
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 96861055
    | Mm_GenLoc_end = 96901971
    | Mm_Uniprot = Q3TCI2
  }}
}}
'''Autocrine motility factor receptor''', also known as '''AMFR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMFR autocrine motility factor receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=267| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: AMFR autocrine motility factor receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=267| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}
==Model organisms==
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
|+ ''Amfr'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal
|-
| [[Recessive]] lethal study || bgcolor="#488ED3"|Normal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#488ED3"|Normal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#488ED3"|Normal
|-
| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBPL/salmonella-challenge/ |title=''Salmonella'' infection data for Amfr |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBPL/citrobacter-challenge/ |title=''Citrobacter'' infection data for Amfr |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of AMFR function. A conditional [[knockout mouse]] line, called ''Amfr<sup>tm1a(KOMP)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Amfr |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362704 |title=Mouse Genome Informatics}}</ref> 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.<ref name="pmid21677750">{{Cite journal
| last1 = Skarnes |first1 =W. C.
| doi = 10.1038/nature10163
| last2 = Rosen | first2 = B.
| last3 = West | first3 = A. P.
| last4 = Koutsourakis | first4 = M.
| last5 = Bushell | first5 = W.
| last6 = Iyer | first6 = V.
| last7 = Mujica | first7 = A. O.
| last8 = Thomas | first8 = M.
| last9 = Harrow | first9 = J.
| last10 = Cox | first10 = T.
| last11 = Jackson | first11 = D.
| last12 = Severin | first12 = J.
| last13 = Biggs | first13 = P.
| last14 = Fu | first14 = J.
| last15 = Nefedov | first15 = M.
| last16 = De Jong | first16 = P. J.
| last17 = Stewart | first17 = A. F.
| last18 = Bradley | first18 = A.
| title = A conditional knockout resource for the genome-wide study of mouse gene function
| journal = Nature
| volume = 474
| issue = 7351
| pages = 337–342
| year = 2011
| pmid = 21677750
| pmc =3572410
}}</ref><ref name="mouse_library">{{cite journal | doi = 10.1038/474262a | title = Mouse library set to be knockout | year = 2011 | author = Dolgin E | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | pmid = 21677718 }}</ref><ref name="mouse_for_all_reasons">{{cite journal | doi = 10.1016/j.cell.2006.12.018 | title = A Mouse for All Reasons | year = 2007 | journal = Cell | volume = 128 | pages = 9–13 | pmid = 17218247 |vauthors=Collins FS, Rossant J, Wurst W| issue = 1 }}</ref>
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal| vauthors=van der Weyden L, White JK, Adams DJ, Logan DW| title=The mouse genetics toolkit: revealing function and mechanism. | journal=Genome Biol | year= 2011 | volume= 12 | issue= 6 | pages= 224 | pmid=21722353 | doi=10.1186/gb-2011-12-6-224  | pmc=3218837}}</ref> Twenty six tests were carried out on [[mutant]] mice and one significant abnormality was observed: [[Mendelian ratio|Fewer than expected homozygous]] mutant mice survived until [[weaning]].<ref name="mgp_reference" />
==Interactions==
AMFR has been shown to [[Protein-protein interaction|interact]] with [[Valosin-containing protein]].<ref name=pmid15331598>{{cite journal |last=Zhong |first=Xiaoyan |author2=Shen Yuxian |author3=Ballar Petek |author4=Apostolou Andria |author5=Agami Reuven |author6=Fang Shengyun  |date=Oct 2004 |title=AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation |journal=J. Biol. Chem. |volume=279 |issue=44 |pages=45676–84 |publisher= |location = United States| issn = 0021-9258| pmid = 15331598 |doi = 10.1074/jbc.M409034200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid18835813>{{cite journal |last=Lee |first=Joon No |author2=Zhang Xiangyu |author3=Feramisco Jamison D |author4=Gong Yi |author5=Ye Jin  |date=Nov 2008 |title=Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step |journal=J. Biol. Chem. |volume=283 |issue=48 |pages=33772–83 |publisher= |location = United States| issn = 0021-9258| pmid = 18835813 |doi = 10.1074/jbc.M806108200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=2586246 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|AMFR}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Watanabe H, Carmi P, Hogan V, ''et al.'' |title=Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 13442-8 |year= 1991 |pmid= 1649192 |doi=  }}
*{{cite journal  | vauthors=Huang B, Xie Y, Raz A |title=Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor. |journal=Biochem. Biophys. Res. Commun. |volume=212 |issue= 3 |pages= 727–42 |year= 1995 |pmid= 7626106 |doi=10.1006/bbrc.1995.2031 }}
*{{cite journal  | author=Huang B, Xie Y, Raz A |title=Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor. |journal=Biochem. Biophys. Res. Commun. |volume=212 |issue= 3 |pages= 727-42 |year= 1995 |pmid= 7626106 |doi=  }}
*{{cite journal  | vauthors=Hillier LD, Lennon G, Becker M |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1997 |pmid= 8889549 |doi=10.1101/gr.6.9.807 |display-authors=etal}}
*{{cite journal  | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal  | vauthors=Shimizu K, Tani M, Watanabe H |title=The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein. |journal=FEBS Lett. |volume=456 |issue= 2 |pages= 295–300 |year= 1999 |pmid= 10456327 |doi=10.1016/S0014-5793(99)00966-7  |display-authors=etal}}
*{{cite journal  | author=Shimizu K, Tani M, Watanabe H, ''et al.'' |title=The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein. |journal=FEBS Lett. |volume=456 |issue= 2 |pages= 295-300 |year= 1999 |pmid= 10456327 |doi= }}
*{{cite journal  | vauthors=Fang S, Ferrone M, Yang C |title=The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 25 |pages= 14422–7 |year= 2002 |pmid= 11724934 |doi= 10.1073/pnas.251401598  | pmc=64697 |display-authors=etal|bibcode=2001PNAS...9814422F }}
*{{cite journal  | author=Fang S, Ferrone M, Yang C, ''et al.'' |title=The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 25 |pages= 14422-7 |year= 2002 |pmid= 11724934 |doi= 10.1073/pnas.251401598 }}
*{{cite journal  | vauthors=Luo Y, Long JM, Lu C |title=A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78. |journal=J. Neurochem. |volume=80 |issue= 2 |pages= 354–61 |year= 2002 |pmid= 11902125 |doi=10.1046/j.0022-3042.2001.00707.x  |display-authors=etal}}
*{{cite journal  | author=Luo Y, Long JM, Lu C, ''et al.'' |title=A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78. |journal=J. Neurochem. |volume=80 |issue= 2 |pages= 354-61 |year= 2002 |pmid= 11902125 |doi=  }}
*{{cite journal  | vauthors=Tímár J, Rásó E, Döme B |title=Expression and function of the AMF receptor by human melanoma in experimental and clinical systems. |journal=Clin. Exp. Metastasis |volume=19 |issue= 3 |pages= 225–32 |year= 2002 |pmid= 12067203 |doi=10.1023/A:1015595708241 |display-authors=etal}}
*{{cite journal  | author=Tímár J, Rásó E, Döme B, ''et al.'' |title=Expression and function of the AMF receptor by human melanoma in experimental and clinical systems. |journal=Clin. Exp. Metastasis |volume=19 |issue= 3 |pages= 225-32 |year= 2002 |pmid= 12067203 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal|bibcode=2002PNAS...9916899M }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Liang JS, Kim T, Fang S |title=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. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23984–8 |year= 2003 |pmid= 12670940 |doi= 10.1074/jbc.M302683200 |display-authors=etal}}
*{{cite journal  | author=Liang JS, Kim T, Fang S, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23984-8 |year= 2003 |pmid= 12670940 |doi= 10.1074/jbc.M302683200 }}
*{{cite journal  | vauthors=Takanami I, Takeuchi K |title=Autocrine motility factor-receptor gene expression in lung cancer. |journal=Jpn. J. Thorac. Cardiovasc. Surg. |volume=51 |issue= 8 |pages= 368–73 |year= 2003 |pmid= 12962414 |doi=10.1007/BF02719469  }}
*{{cite journal  | author=Takanami I, Takeuchi K |title=Autocrine motility factor-receptor gene expression in lung cancer. |journal=Jpn. J. Thorac. Cardiovasc. Surg. |volume=51 |issue= 8 |pages= 368-73 |year= 2003 |pmid= 12962414 |doi= }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Registre M, Goetz JG, St Pierre P |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=320 |issue= 4 |pages= 1316–22 |year= 2004 |pmid= 15303277 |doi=10.1016/j.bbrc.2004.06.089  |display-authors=etal}}
*{{cite journal  | author=Registre M, Goetz JG, St Pierre P, ''et al.'' |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=320 |issue= 4 |pages= 1316-22 |year= 2004 |pmid= 15303277 |doi= }}
*{{cite journal  | vauthors=Zhong X, Shen Y, Ballar P |title=AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. |journal=J. Biol. Chem. |volume=279 |issue= 44 |pages= 45676–84 |year= 2004 |pmid= 15331598 |doi= 10.1074/jbc.M409034200 |display-authors=etal}}
*{{cite journal  | author=Zhong X, Shen Y, Ballar P, ''et al.'' |title=AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. |journal=J. Biol. Chem. |volume=279 |issue= 44 |pages= 45676-84 |year= 2004 |pmid= 15331598 |doi= 10.1074/jbc.M409034200 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Song BL, Sever N, DeBose-Boyd RA |title=Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. |journal=Mol. Cell |volume=19 |issue= 6 |pages= 829–40 |year= 2005 |pmid= 16168377 |doi= 10.1016/j.molcel.2005.08.009 }}
*{{cite journal  | author=Song BL, Sever N, DeBose-Boyd RA |title=Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. |journal=Mol. Cell |volume=19 |issue= 6 |pages= 829-40 |year= 2005 |pmid= 16168377 |doi= 10.1016/j.molcel.2005.08.009 }}
*{{cite journal  | vauthors=Kaynak K, Kara M, Oz B |title=Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas. |journal=Acta Chir. Belg. |volume=105 |issue= 4 |pages= 378–82 |year= 2006 |pmid= 16184720 |doi= |display-authors=etal}}
*{{cite journal  | author=Kaynak K, Kara M, Oz B, ''et al.'' |title=Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas. |journal=Acta Chir. Belg. |volume=105 |issue= 4 |pages= 378-82 |year= 2006 |pmid= 16184720 |doi=  }}
*{{cite journal  | vauthors=Ye Y, Shibata Y, Kikkert M |title=Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14132–8 |year= 2006 |pmid= 16186510 |doi= 10.1073/pnas.0505006102 | pmc=1242302 |display-authors=etal|bibcode=2005PNAS..10214132Y }}
*{{cite journal  | author=Ye Y, Shibata Y, Kikkert M, ''et al.'' |title=Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 40 |pages= 14132-8 |year= 2006 |pmid= 16186510 |doi= 10.1073/pnas.0505006102 }}
*{{cite journal  | vauthors=Chen B, Mariano J, Tsai YC |title=The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 2 |pages= 341–6 |year= 2006 |pmid= 16407162 |doi= 10.1073/pnas.0506618103  | pmc=1326157 |display-authors=etal|bibcode=2006PNAS..103..341C }}
*{{cite journal  | author=Chen B, Mariano J, Tsai YC, ''et al.'' |title=The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 2 |pages= 341-6 |year= 2006 |pmid= 16407162 |doi= 10.1073/pnas.0506618103 }}
*{{cite journal  | vauthors=Haga A, Tanaka N, Funasaka T |title=The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF. |journal=J. Mol. Biol. |volume=358 |issue= 3 |pages= 741–53 |year= 2006 |pmid= 16563432 |doi= 10.1016/j.jmb.2006.02.046 |display-authors=etal}}
*{{cite journal  | author=Haga A, Tanaka N, Funasaka T, ''et al.'' |title=The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF. |journal=J. Mol. Biol. |volume=358 |issue= 3 |pages= 741-53 |year= 2006 |pmid= 16563432 |doi= 10.1016/j.jmb.2006.02.046 }}
*{{cite journal  | vauthors=Shen Y, Ballar P, Fang S |title=Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin. |journal=Biochem. Biophys. Res. Commun. |volume=349 |issue= 4 |pages= 1285–93 |year= 2006 |pmid= 16979136 |doi= 10.1016/j.bbrc.2006.08.173 }}
*{{cite journal  | author=Shen Y, Ballar P, Fang S |title=Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin. |journal=Biochem. Biophys. Res. Commun. |volume=349 |issue= 4 |pages= 1285-93 |year= 2006 |pmid= 16979136 |doi= 10.1016/j.bbrc.2006.08.173 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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[[Category:Genes mutated in mice]]

Latest revision as of 09:16, 10 January 2019

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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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

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

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

References

  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. ↑ 2.0 2.1 "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. ↑ 5.0 5.1 5.2 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.
  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.

External links

Further reading

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