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Q9R049

- AMFR_MOUSE

UniProt

Q9R049 - AMFR_MOUSE

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Protein

E3 ubiquitin-protein ligase AMFR

Gene

Amfr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis (By similarity).By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. nucleotide binding Source: UniProtKB-KW
  3. receptor activity Source: Ensembl
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular process Source: MGI
  3. endoplasmic reticulum unfolded protein response Source: Ensembl
  4. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. learning or memory Source: Ensembl
  6. protein oligomerization Source: Ensembl
  7. protein polyubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Receptor

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase AMFR (EC:6.3.2.-)
Alternative name(s):
Autocrine motility factor receptor
Short name:
AMF receptor
Gene namesi
Name:Amfr
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1345634. Amfr.

Subcellular locationi

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. growth cone Source: Ensembl
  3. Hrd1p ubiquitin ligase complex Source: Ensembl
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. integral component of plasma membrane Source: MGI
  6. neuronal cell body Source: Ensembl
  7. nucleus Source: Ensembl
  8. perinuclear region of cytoplasm Source: Ensembl
  9. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643E3 ubiquitin-protein ligase AMFRPRO_0000064580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei542 – 5421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9R049.
PaxDbiQ9R049.
PRIDEiQ9R049.

PTM databases

PhosphoSiteiQ9R049.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9R049.
CleanExiMM_AMFR.
ExpressionAtlasiQ9R049. baseline and differential.
GenevestigatoriQ9R049.

Interactioni

Subunit structurei

Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7. Interacts with DRL1. Interacts (via the VIM) with VCP/p97. Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway (By similarity). Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway. Interacts (via the VIM) with VCP/p97. Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ngly1Q9JI785EBI-3648125,EBI-3648128
VcpQ018534EBI-3648125,EBI-80597

Protein-protein interaction databases

BioGridi204722. 3 interactions.
IntActiQ9R049. 7 interactions.
MINTiMINT-1864613.
STRINGi10090.ENSMUSP00000052258.

Structurei

3D structure databases

ProteinModelPortaliQ9R049.
SMRiQ9R049. Positions 327-384, 453-504, 574-599.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence AnalysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence AnalysisAdd
BLAST
Transmembranei254 – 27421HelicalSequence AnalysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence AnalysisAdd
BLAST
Transmembranei429 – 44921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini456 – 49843CUEPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni614 – 64330VCP/p97-interacting motif (VIM)Add
BLAST

Domaini

The CUE domain is required for recognition of misfolded proteins such as mutant CFTR.
The VCP/p97-interacting motif (VIM) is sufficient for binding VCP/p97 to form a complex capable of transferring VCP/p97 from the cytosol to microsomes.

Sequence similaritiesi

Contains 1 CUE domain.CuratedPROSITE-ProRule annotation
Contains 1 RING-type zinc finger.CuratedPROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri341 – 37939RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5243.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000037436.
HOVERGENiHBG044694.
InParanoidiQ9R049.
KOiK10636.
OMAiNTACCFL.
OrthoDBiEOG7QRQT8.
PhylomeDBiQ9R049.
TreeFamiTF320052.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003892. CUE.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51140. CUE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9R049-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPLLFLERFP WPSLRTYTGL SGLALLGTIV SAYRALSQPE DGSGEPEPLT
60 70 80 90 100
APLQPEALAP ARLTAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK
110 120 130 140 150
LIQCIVFGPL RVSERQHLKD KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL
160 170 180 190 200
WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM SSHGRVLSLL IAMLLSCCGL
210 220 230 240 250
AVVCCVTGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH LWDLNHEGTW
260 270 280 290 300
EGKGTYVYYT DFVMELALLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY
310 320 330 340 350
LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA
360 370 380 390 400
ARKLPCGHLF HNSCLRSWLE QDTSCPTCRM SLNIADGSRA REDHQGENLD
410 420 430 440 450
ENLVPVAAAE GRPRLNQHNH FFHFDGSRIA SWLPSFSVEV MHTTNILGIT
460 470 480 490 500
QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL QMTRSVEITT DNILEGRIQV
510 520 530 540 550
PFPTQRSDSL RPALNSPVER PSPDLEEGEA SVQTERVPLD LSPRLEETLD
560 570 580 590 600
FSEVELEPIE VEDFEARGSR FSKSADERQR MLVQRKDDLL QQARKRFLNK
610 620 630 640
SSEDDGASER LLPSEGTSSD PVTLRRRMLA AAAERRLQRQ RTT
Length:643
Mass (Da):73,105
Last modified:June 1, 2003 - v2
Checksum:i7119277725982F79
GO
Isoform 2Curated (identifier: Q9R049-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-60: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:639
Mass (Da):72,753
Checksum:i22FF6303EEA033F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti412 – 4121R → S in AAD56721. (PubMed:10456327)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei57 – 604Missing in isoform 2. 1 PublicationVSP_008224

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF124144 mRNA. Translation: AAD56721.1.
BC003256 mRNA. Translation: AAH03256.1.
BC034538 mRNA. Translation: AAH34538.1.
BC040338 mRNA. Translation: AAH40338.1.
CCDSiCCDS22533.1. [Q9R049-2]
RefSeqiNP_035917.2. NM_011787.2. [Q9R049-2]
UniGeneiMm.34641.
Mm.490433.

Genome annotation databases

EnsembliENSMUST00000053766; ENSMUSP00000052258; ENSMUSG00000031751. [Q9R049-2]
GeneIDi23802.
KEGGimmu:23802.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF124144 mRNA. Translation: AAD56721.1 .
BC003256 mRNA. Translation: AAH03256.1 .
BC034538 mRNA. Translation: AAH34538.1 .
BC040338 mRNA. Translation: AAH40338.1 .
CCDSi CCDS22533.1. [Q9R049-2 ]
RefSeqi NP_035917.2. NM_011787.2. [Q9R049-2 ]
UniGenei Mm.34641.
Mm.490433.

3D structure databases

ProteinModelPortali Q9R049.
SMRi Q9R049. Positions 327-384, 453-504, 574-599.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204722. 3 interactions.
IntActi Q9R049. 7 interactions.
MINTi MINT-1864613.
STRINGi 10090.ENSMUSP00000052258.

PTM databases

PhosphoSitei Q9R049.

Proteomic databases

MaxQBi Q9R049.
PaxDbi Q9R049.
PRIDEi Q9R049.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053766 ; ENSMUSP00000052258 ; ENSMUSG00000031751 . [Q9R049-2 ]
GeneIDi 23802.
KEGGi mmu:23802.

Organism-specific databases

CTDi 267.
MGIi MGI:1345634. Amfr.

Phylogenomic databases

eggNOGi COG5243.
GeneTreei ENSGT00530000062938.
HOGENOMi HOG000037436.
HOVERGENi HBG044694.
InParanoidi Q9R049.
KOi K10636.
OMAi NTACCFL.
OrthoDBi EOG7QRQT8.
PhylomeDBi Q9R049.
TreeFami TF320052.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi AMFR. mouse.
NextBioi 303423.
PROi Q9R049.
SOURCEi Search...

Gene expression databases

Bgeei Q9R049.
CleanExi MM_AMFR.
ExpressionAtlasi Q9R049. baseline and differential.
Genevestigatori Q9R049.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR003892. CUE.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02845. CUE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00546. CUE. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS51140. CUE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Lung1 Publication and Testis1 Publication.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N1 Publication.
    Tissue: Colon1 Publication and Mammary gland1 Publication.
  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] [Europe PMC] [Abstract]
    Cited for: ROLE IN METASTASIS.
  4. "The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation."
    Ballar P., Shen Y., Yang H., Fang S.
    J. Biol. Chem. 281:35359-35368(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCP IN THE VCP/P97-AMFR/GP78 COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGLY1; PSMC1; SAKS1; RAD23B AND VCP.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF MISFOLDED PROTEINS, INTERACTION WITH RNF5.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAMFR_MOUSE
AccessioniPrimary (citable) accession number: Q9R049
Secondary accession number(s): Q8K008, Q99LH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3