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Q9R049 (AMFR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase AMFR

EC=6.3.2.-
Alternative name(s):
Autocrine motility factor receptor
Short name=AMF receptor
Gene names
Name:Amfr
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which can target both itself and other proteins including CD3D and APOB for proteasomal degradation. Mediates polyubiquitination of CYP3A4. Specific receptor for the autocrine motility factor. Mediates tumor invasion and metastasis. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulun that are retrotranslocated in the cytosol By similarity. Promotes ubiquitination of misfolded proteins such as mutant CFTR; proposed to mediate sequential ubiquitination by recognizing already ubiquitin-conjugated substrates and to cooperate with E3 ubiquitin-protein ligase RNF5. Ref.3 Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with UBE2G2/UBC7 through a region distinct from the RING finger. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with RNF5. Ref.4 Ref.6 UniProtKB Q9UKV5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed in heart, brain, liver, lung, skeletal muscle, kidney and testis. Not detected in spleen. Ref.1

Domain

The CUE domain is required for recognition of misfolded proteins such as mutant CFTR.

Sequence similarities

Contains 1 CUE domain.

Contains 1 RING-type zinc finger.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9R049-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9R049-2)

The sequence of this isoform differs from the canonical sequence as follows:
     57-60: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643E3 ubiquitin-protein ligase AMFR
PRO_0000064580

Regions

Transmembrane82 – 10221Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane215 – 23521Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane276 – 29621Helical; Potential
Transmembrane429 – 44921Helical; Potential
Domain456 – 49843CUE
Zinc finger341 – 37939RING-type

Amino acid modifications

Modified residue5421Phosphoserine Ref.5 Ref.7

Natural variations

Alternative sequence57 – 604Missing in isoform 2.
VSP_008224

Experimental info

Sequence conflict4121R → S in AAD56721. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 2.
Checksum: 7119277725982F79

FASTA64373,105
        10         20         30         40         50         60 
MPLLFLERFP WPSLRTYTGL SGLALLGTIV SAYRALSQPE DGSGEPEPLT APLQPEALAP 

        70         80         90        100        110        120 
ARLTAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK LIQCIVFGPL RVSERQHLKD 

       130        140        150        160        170        180 
KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM 

       190        200        210        220        230        240 
SSHGRVLSLL IAMLLSCCGL AVVCCVTGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH 

       250        260        270        280        290        300 
LWDLNHEGTW EGKGTYVYYT DFVMELALLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY 

       310        320        330        340        350        360 
LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA ARKLPCGHLF 

       370        380        390        400        410        420 
HNSCLRSWLE QDTSCPTCRM SLNIADGSRA REDHQGENLD ENLVPVAAAE GRPRLNQHNH 

       430        440        450        460        470        480 
FFHFDGSRIA SWLPSFSVEV MHTTNILGIT QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL 

       490        500        510        520        530        540 
QMTRSVEITT DNILEGRIQV PFPTQRSDSL RPALNSPVER PSPDLEEGEA SVQTERVPLD 

       550        560        570        580        590        600 
LSPRLEETLD FSEVELEPIE VEDFEARGSR FSKSADERQR MLVQRKDDLL QQARKRFLNK 

       610        620        630        640 
SSEDDGASER LLPSEGTSSD PVTLRRRMLA AAAERRLQRQ RTT 

« Hide

Isoform 2 [UniParc].

Checksum: 22FF6303EEA033F1
Show »

FASTA63972,753

References

« Hide 'large scale' references
[1]"The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein."
Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y., Shiroishi T., Ohwada S., Raz A., Yokota J.
FEBS Lett. 456:295-300(1999) [PubMed: 10456327] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Lung and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Colon and Mammary gland.
[3]"Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation."
Onishi Y., Tsukada K., Yokota J., Raz A.
Clin. Exp. Metastasis 20:51-58(2003) [PubMed: 12650607] [Abstract]
Cited for: ROLE IN METASTASIS.
[4]"The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor."
Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006) [PubMed: 16709668] [Abstract]
Cited for: INTERACTION WITH NGLY1; PSMC1; SAKS1; RAD23B AND VCP.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, MASS SPECTROMETRY.
Tissue: Brain cortex.
[6]"Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508."
Morito D., Hirao K., Oda Y., Hosokawa N., Tokunaga F., Cyr D.M., Tanaka K., Iwai K., Nagata K.
Mol. Biol. Cell 19:1328-1336(2008) [PubMed: 18216283] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF MISFOLDED PROTEINS, INTERACTION WITH RNF5.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF124144 mRNA. Translation: AAD56721.1.
BC003256 mRNA. Translation: AAH03256.1.
BC034538 mRNA. Translation: AAH34538.1.
BC040338 mRNA. Translation: AAH40338.1.
IPIIPI00319880.
IPI00351315.
RefSeqNP_035917.2. NM_011787.2.
UniGeneMm.34641.

3D structure databases

ProteinModelPortalQ9R049.
SMRQ9R049. Positions 329-386, 456-502, 574-600.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9R049. 5 interactions.
STRINGQ9R049.

PTM databases

PhosphoSiteQ9R049.

Proteomic databases

PRIDEQ9R049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053766; ENSMUSP00000052258; ENSMUSG00000031751.
GeneID23802.
KEGGmmu:23802.

Organism-specific databases

CTD267.
MGIMGI:1345634. Amfr.

Phylogenomic databases

GeneTreeENSGT00530000062938.
HOGENOMHBG445825.
HOVERGENHBG044694.
InParanoidQ9R049.
OMAARDVAQY.
OrthoDBEOG4DJJW8.

Gene expression databases

ArrayExpressQ9R049.
BgeeQ9R049.
CleanExMM_AMFR.
GenevestigatorQ9R049.
GermOnlineENSMUSG00000031751. Mus musculus.

Family and domain databases

InterProIPR003892. CUE.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KOK10636.
PfamPF02845. CUE. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00546. CUE. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS51140. CUE. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameAMFR_MOUSE
AccessionPrimary (citable) accession number: Q9R049
Secondary accession number(s): Q8K008, Q99LH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families