P97785 · GFRA1_MOUSE

  • Protein
    GDNF family receptor alpha-1
  • Gene
    Gfra1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Coreceptor for GDNF, a neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. GDNF-binding leads to autophosphorylation and activation of the RET receptor.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaxon
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular space
Cellular Componentextrinsic component of membrane
Cellular ComponentGolgi apparatus
Cellular Componentmultivesicular body
Cellular Componentneuronal cell body
Cellular Componentplasma membrane
Cellular Componentplasma membrane protein complex
Cellular Componentreceptor complex
Molecular Functionglial cell-derived neurotrophic factor receptor activity
Molecular Functionintegrin binding
Molecular Functionneurotrophin receptor activity
Molecular Functionsignaling receptor activity
Biological Processanatomical structure morphogenesis
Biological Processcell migration
Biological Processcell surface receptor protein tyrosine kinase signaling pathway
Biological Processglial cell-derived neurotrophic factor receptor signaling pathway
Biological Processkidney development
Biological Processmale gonad development
Biological Processnervous system development
Biological Processneuron projection development
Biological Processpositive regulation of peptidyl-tyrosine phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    GDNF family receptor alpha-1
  • Short names
    GDNF receptor alpha-1; GDNFR-alpha-1; GFR-alpha-1
  • Alternative names
    • TGF-beta-related neurotrophic factor receptor 1

Gene names

    • Name
      Gfra1
    • Synonyms
      Gdnfra, Trnr1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P97785
  • Secondary accessions
    • O35246
    • O35252

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor
Endosome
Note: Localizes mainly to the plasma membrane. In the presence of SORL1, shifts to vesicular structures, including trans-Golgi network, endosomes and multivesicular bodies.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_000001077925-430GDNF family receptor alpha-1
Disulfide bond36↔42
Glycosylation59N-linked (GlcNAc...) asparagine
Disulfide bond154↔214
Disulfide bond161↔167
Disulfide bond178↔192
Disulfide bond187↔233
Disulfide bond216↔221
Disulfide bond243↔313
Disulfide bond250↔256
Disulfide bond267↔285
Disulfide bond277↔337
Disulfide bond315↔325
Glycosylation347N-linked (GlcNAc...) asparagine
Glycosylation406N-linked (GlcNAc...) asparagine
Lipidation430GPI-anchor amidated serine
PropeptidePRO_0000010780431-468Removed in mature form

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the brain, in hippocampal neurons (at protein level) (PubMed:23333276).
Isoform 1 and isoform 2 are expressed in heart, brain, lung, liver, kidney and testis.

Gene expression databases

Interaction

Subunit

Interacts with GDNF ligand and RET: forms a 2:2:2 ternary complex composed of GDNF ligand, GFRA1 and RET receptor. Interacts with SORL1, either alone or in complex with GDNF. Interaction between SORL1 and GFRA1 leads to GFRA1 internalization, but not degradation.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P97785Ret P355462EBI-5549349, EBI-2480800

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat25-1131
Repeat150-2382
Repeat239-3423

Sequence similarities

Belongs to the GDNFR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

P97785-1

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.

  • Name
    1
  • Synonyms
    GDNFR-alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    468
  • Mass (Da)
    51,752
  • Last updated
    2011-07-27 v2
  • Checksum
    997105C2A6DD6446
MFLATLYFVLPLLDLLMSAEVSGGDRLDCVKASDQCLKEQSCSTKYRTLRQCVAGKETNFSLTSGLEAKDECRSAMEALKQKSLYNCRCKRGMKKEKNCLRIYWSMYQSLQGNDLLEDSPYEPVNSRLSDIFRAVPFISDVFQQVEHISKGNNCLDAAKACNLDDTCKKYRSAYITPCTTSMSNEVCNRRKCHKALRQFFDKVPAKHSYGMLFCSCRDVACTERRRQTIVPVCSYEERERPNCLNLQDSCKTNYICRSRLADFFTNCQPESRSVSNCLKENYADCLLAYSGLIGTVMTPNYIDSSSLSVAPWCDCSNSGNDLEDCLKFLNFFKDNTCLKNAIQAFGNGSDVTMWQPAPPVQTTTATTTTAFRIKNKPLGPAGSENEIPTHVLPPCANLQAQKLKSNVSGSTHLCLSDNDYGKDGLAGASSHITTKSMAAPPSCGLSSLPVMVFTALAALLSVSLAETS

P97785-2

  • Name
    2
  • Synonyms
    GDNFR-beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YUD5D3YUD5_MOUSEGfra154
D3YWL3D3YWL3_MOUSEGfra125
D3Z3C9D3Z3C9_MOUSEGfra148
D6RDD4D6RDD4_MOUSEGfra1419
A0A1C7ZN00A0A1C7ZN00_MOUSEGfra18

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_041630140-144in isoform 2
Sequence conflict366in Ref. 2; BAA19185

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF014117
EMBL· GenBank· DDBJ
AAB86599.1
EMBL· GenBank· DDBJ
mRNA
AF015172
EMBL· GenBank· DDBJ
AAB86600.1
EMBL· GenBank· DDBJ
mRNA
AB000800
EMBL· GenBank· DDBJ
BAA19185.1
EMBL· GenBank· DDBJ
mRNA
CH466585
EMBL· GenBank· DDBJ
EDL01795.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466585
EMBL· GenBank· DDBJ
EDL01796.1
EMBL· GenBank· DDBJ
Genomic DNA
BC054378
EMBL· GenBank· DDBJ
AAH54378.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp