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Protein

GDNF family receptor alpha-1

Gene

Gfra1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor.

GO - Molecular functioni

  • integrin binding Source: RGD
  • receptor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cell migration Source: RGD
  • kidney development Source: RGD
  • male gonad development Source: RGD
  • neuron differentiation Source: RGD
  • neuron projection development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiR-RNO-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
GDNF family receptor alpha-1
Short name:
GDNF receptor alpha-1
Short name:
GDNFR-alpha-1
Short name:
GFR-alpha-1
Alternative name(s):
RET ligand 1
TGF-beta-related neurotrophic factor receptor 1
Gene namesi
Name:Gfra1
Synonyms:Gdnfra, Retl1, Trnr1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2681. Gfra1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • axon Source: RGD
  • external side of plasma membrane Source: RGD
  • extracellular space Source: RGD
  • neuronal cell body Source: RGD
  • plasma membrane Source: Reactome
  • receptor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 430406GDNF family receptor alpha-1PRO_0000010781Add
BLAST
Propeptidei431 – 46838Removed in mature formSequence analysisPRO_0000010782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 87By similarity
Disulfide bondi36 ↔ 42By similarity
Disulfide bondi52 ↔ 72By similarity
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi89 ↔ 99By similarity
Disulfide bondi154 ↔ 214By similarity
Disulfide bondi161 ↔ 167By similarity
Disulfide bondi178 ↔ 192By similarity
Disulfide bondi187 ↔ 233By similarity
Disulfide bondi216 ↔ 221By similarity
Disulfide bondi243 ↔ 3131 Publication
Disulfide bondi250 ↔ 2561 Publication
Disulfide bondi267 ↔ 2851 Publication
Disulfide bondi277 ↔ 3371 Publication
Disulfide bondi315 ↔ 3251 Publication
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Lipidationi430 – 4301GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ62997.
PRIDEiQ62997.

Expressioni

Tissue specificityi

Expressed in liver, brain, kidney and cochlea.1 Publication

Interactioni

Subunit structurei

2 molecules of GDNFR-alpha are thought to form a complex with the disulfide-linked GDNF dimer and with 2 molecules of RET.1 Publication

GO - Molecular functioni

  • integrin binding Source: RGD

Protein-protein interaction databases

BioGridi247488. 2 interactions.
STRINGi10116.ENSRNOP00000023667.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi153 – 16210Combined sources
Helixi165 – 17915Combined sources
Beta strandi185 – 1873Combined sources
Helixi189 – 20214Combined sources
Helixi205 – 2139Combined sources
Helixi219 – 2268Combined sources
Turni227 – 2293Combined sources
Helixi231 – 2344Combined sources
Helixi243 – 2519Combined sources
Helixi254 – 26613Combined sources
Beta strandi270 – 2734Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 2909Combined sources
Turni291 – 2944Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi309 – 3124Combined sources
Helixi319 – 3213Combined sources
Helixi322 – 33312Combined sources
Helixi336 – 34510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q8DX-ray1.80A239-346[»]
2V5EX-ray2.35A150-349[»]
3FUBX-ray2.35A/C145-425[»]
4UX8electron microscopy24.00C/E1-468[»]
ProteinModelPortaliQ62997.
SMRiQ62997. Positions 239-346.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62997.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati25 – 113891Add
BLAST
Repeati150 – 238892Add
BLAST
Repeati239 – 3421043Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi362 – 3698Poly-Thr

Sequence similaritiesi

Belongs to the GDNFR family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IU4F. Eukaryota.
ENOG410XPTA. LUCA.
HOGENOMiHOG000008695.
HOVERGENiHBG051725.
InParanoidiQ62997.
KOiK19895.
PhylomeDBiQ62997.
TreeFamiTF331647.

Family and domain databases

InterProiIPR016017. GDNF/GAS1.
IPR003438. GDNF_rcpt.
IPR003503. GDNF_rcpt_A1.
IPR017372. Glial_neurotroph_fac_rcpt_a1/2.
[Graphical view]
PfamiPF02351. GDNF. 3 hits.
[Graphical view]
PIRSFiPIRSF038071. GDNF_family_receptor_alpha. 1 hit.
PRINTSiPR01317. GDNFRALPHA1.
PR01316. GDNFRECEPTOR.
SMARTiSM00907. GDNF. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62997-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLATLYFAL PLLDLLMSAE VSGGDRLDCV KASDQCLKEQ SCSTKYRTLR
60 70 80 90 100
QCVAGKETNF SLTSGLEAKD ECRSAMEALK QKSLYNCRCK RGMKKEKNCL
110 120 130 140 150
RIYWSMYQSL QGNDLLEDSP YEPVNSRLSD IFRAVPFISD VFQQVEHISK
160 170 180 190 200
GNNCLDAAKA CNLDDTCKKY RSAYITPCTT SMSNEVCNRR KCHKALRQFF
210 220 230 240 250
DKVPAKHSYG MLFCSCRDIA CTERRRQTIV PVCSYEERER PNCLSLQDSC
260 270 280 290 300
KTNYICRSRL ADFFTNCQPE SRSVSNCLKE NYADCLLAYS GLIGTVMTPN
310 320 330 340 350
YVDSSSLSVA PWCDCSNSGN DLEDCLKFLN FFKDNTCLKN AIQAFGNGSD
360 370 380 390 400
VTMWQPAPPV QTTTATTTTA FRVKNKPLGP AGSENEIPTH VLPPCANLQA
410 420 430 440 450
QKLKSNVSGS THLCLSDSDF GKDGLAGASS HITTKSMAAP PSCSLSSLPV
460
LMLTALAALL SVSLAETS
Length:468
Mass (Da):51,650
Last modified:November 1, 1996 - v1
Checksum:iB2EE5906F5025E0F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59486 mRNA. Translation: AAC52663.1.
U97142 mRNA. Translation: AAC53300.1.
RefSeqiNP_037091.1. NM_012959.1.
XP_008758734.1. XM_008760512.1.
XP_008758735.1. XM_008760513.1.
UniGeneiRn.88489.

Genome annotation databases

GeneIDi25454.
KEGGirno:25454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59486 mRNA. Translation: AAC52663.1.
U97142 mRNA. Translation: AAC53300.1.
RefSeqiNP_037091.1. NM_012959.1.
XP_008758734.1. XM_008760512.1.
XP_008758735.1. XM_008760513.1.
UniGeneiRn.88489.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q8DX-ray1.80A239-346[»]
2V5EX-ray2.35A150-349[»]
3FUBX-ray2.35A/C145-425[»]
4UX8electron microscopy24.00C/E1-468[»]
ProteinModelPortaliQ62997.
SMRiQ62997. Positions 239-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247488. 2 interactions.
STRINGi10116.ENSRNOP00000023667.

Proteomic databases

PaxDbiQ62997.
PRIDEiQ62997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25454.
KEGGirno:25454.

Organism-specific databases

CTDi2674.
RGDi2681. Gfra1.

Phylogenomic databases

eggNOGiENOG410IU4F. Eukaryota.
ENOG410XPTA. LUCA.
HOGENOMiHOG000008695.
HOVERGENiHBG051725.
InParanoidiQ62997.
KOiK19895.
PhylomeDBiQ62997.
TreeFamiTF331647.

Enzyme and pathway databases

ReactomeiR-RNO-419037. NCAM1 interactions.

Miscellaneous databases

EvolutionaryTraceiQ62997.
PROiQ62997.

Family and domain databases

InterProiIPR016017. GDNF/GAS1.
IPR003438. GDNF_rcpt.
IPR003503. GDNF_rcpt_A1.
IPR017372. Glial_neurotroph_fac_rcpt_a1/2.
[Graphical view]
PfamiPF02351. GDNF. 3 hits.
[Graphical view]
PIRSFiPIRSF038071. GDNF_family_receptor_alpha. 1 hit.
PRINTSiPR01317. GDNFRALPHA1.
PR01316. GDNFRECEPTOR.
SMARTiSM00907. GDNF. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF."
    Jing S., Wen D., Yu Y., Holst P.L., Luo Y., Fang M., Tamir R., Antonio L., Hu Z., Cupples R., Louis J.-C., Hu S., Altrock B.W., Fox G.M.
    Cell 85:1113-1124(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Glial cell line-derived neurotrophic factor-dependent RET activation can be mediated by two different cell-surface accessory proteins."
    Sanicola M., Hession C.A., Worley D.S., Carmillo P., Ehrenfels C., Walus L., Robinson S., Jaworski G., Wei H., Tizard R., Whitty A., Pepinsky R.B., Cate R.L.
    Proc. Natl. Acad. Sci. U.S.A. 94:6238-6243(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Expression of the GDNF family members and their receptors in the mature rat cochlea."
    Stoever T., Gong T.-W.L., Cho Y., Altschuler R.A., Lomax M.I.
    Brain Res. Mol. Brain Res. 76:25-35(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "The structure of GFRalpha1 domain 3 reveals new insights into GDNF binding and RET activation."
    Leppanen V.M., Bespalov M.M., Runeberg-Roos P., Puurand U., Merits A., Saarma M., Goldman A.
    EMBO J. 23:1452-1462(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 239-346, DISULFIDE BONDS.

Entry informationi

Entry nameiGFRA1_RAT
AccessioniPrimary (citable) accession number: Q62997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.