GFRA1_CHICK
ID GFRA1_CHICK Reviewed; 469 AA.
AC O13156;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=GDNF family receptor alpha-1;
DE Short=GDNF receptor alpha-1;
DE Short=GDNFR-alpha-1;
DE Short=GFR-alpha-1;
DE AltName: Full=TGF-beta-related neurotrophic factor receptor 1;
DE Flags: Precursor;
GN Name=GFRA1; Synonyms=GDNFRA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9192899; DOI=10.1038/42729;
RA Buj-Bello A., Adu J., Pinon L.G.P., Horton A., Thompson J., Rosenthal A.,
RA Chinchetru M., Buchman V.L., Davies A.M.;
RT "Neurturin responsiveness requires a GPI-linked receptor and the Ret
RT receptor tyrosine kinase.";
RL Nature 387:721-724(1997).
CC -!- FUNCTION: Receptor for GDNF. Mediates the GDNF-induced
CC autophosphorylation and activation of the RET receptor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex with
CC the disulfide-linked GDNF dimer and with 2 molecules of RET.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GDNFR family. {ECO:0000305}.
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DR EMBL; U90541; AAB61570.1; -; mRNA.
DR RefSeq; NP_990433.1; NM_205102.1.
DR AlphaFoldDB; O13156; -.
DR SMR; O13156; -.
DR STRING; 9031.ENSGALP00000014927; -.
DR PaxDb; O13156; -.
DR Ensembl; ENSGALT00000014943; ENSGALP00000014927; ENSGALG00000009173.
DR GeneID; 395994; -.
DR KEGG; gga:395994; -.
DR CTD; 2674; -.
DR VEuPathDB; HostDB:geneid_395994; -.
DR eggNOG; ENOG502QQA2; Eukaryota.
DR GeneTree; ENSGT00940000155560; -.
DR HOGENOM; CLU_040179_1_1_1; -.
DR InParanoid; O13156; -.
DR OMA; CKKFLNF; -.
DR OrthoDB; 482696at2759; -.
DR PhylomeDB; O13156; -.
DR Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-GGA-8853659; RET signaling.
DR PRO; PR:O13156; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000009173; Expressed in spleen and 8 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR InterPro; IPR016017; GDNF/GAS1.
DR InterPro; IPR037193; GDNF_alpha.
DR InterPro; IPR003438; GDNF_rcpt.
DR InterPro; IPR003503; GDNF_rcpt_A1.
DR InterPro; IPR017372; Glial_neurotroph_fac_rcpt_a1/2.
DR PANTHER; PTHR10269; PTHR10269; 1.
DR Pfam; PF02351; GDNF; 3.
DR PIRSF; PIRSF038071; GDNF_family_receptor_alpha; 1.
DR PRINTS; PR01317; GDNFRALPHA1.
DR PRINTS; PR01316; GDNFRECEPTOR.
DR SMART; SM00907; GDNF; 3.
DR SUPFAM; SSF110035; SSF110035; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..430
FT /note="GDNF family receptor alpha-1"
FT /id="PRO_0000010775"
FT PROPEP 431..469
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010776"
FT REPEAT 28..116
FT /note="1"
FT REPEAT 149..237
FT /note="2"
FT REPEAT 238..341
FT /note="3"
FT LIPID 430
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..90
FT /evidence="ECO:0000250"
FT DISULFID 39..45
FT /evidence="ECO:0000250"
FT DISULFID 55..75
FT /evidence="ECO:0000250"
FT DISULFID 92..102
FT /evidence="ECO:0000250"
FT DISULFID 153..213
FT /evidence="ECO:0000250"
FT DISULFID 160..166
FT /evidence="ECO:0000250"
FT DISULFID 177..191
FT /evidence="ECO:0000250"
FT DISULFID 186..232
FT /evidence="ECO:0000250"
FT DISULFID 215..220
FT /evidence="ECO:0000250"
FT DISULFID 242..312
FT /evidence="ECO:0000250"
FT DISULFID 249..255
FT /evidence="ECO:0000250"
FT DISULFID 266..284
FT /evidence="ECO:0000250"
FT DISULFID 276..336
FT /evidence="ECO:0000250"
FT DISULFID 314..324
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 52043 MW; B9DB86D15218AF39 CRC64;
MFLALLYLAL PLADVLLSAE VSGLPGGDRL DCVKASDQCL KEQSCSTKYR TLRQCVAGKE
SNFSRATGLE AKDECKSAME ALKQKSLYNC RCKRGMKKEK NCLRIYWSMY QSLQGNDLLE
DSPYEPVNSR LSDIFRLAPI VSVEPVLSKG NNCLDAAKAC NLNDTCKRFR SAYITPCTSS
TSNEICNKRK CHKALRLFFD KVPPKHSYGM LFCSCRDVAC TERRRQTIVP VCSYEDREKP
NCLNLQESCK KNYICRSRLA DFFTNCQPES RSVSSCLKEN YADCLLAYSG LIGTVMTPNY
IDSSSLSVAP WCDCSNSGND IDECRKFLNF FQDNTCLKNA IQAFGNGTDV NVWQPILPVQ
TTTATTTTAS RLKNTGSETT NNEIPTHNDS PACANLQAQK KRKSNESVDT ELCLNENAIG
KDNTPGVSTS HISSENSFAL PTSFYPSTPL ILMTIALSLF LFLSSSVVL
