ID   GFRA2_BOVIN             Reviewed;         464 AA.
AC   Q5E9X0; Q0P5A9;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=GDNF family receptor alpha-2;
DE            Short=GDNF receptor alpha-2;
DE            Short=GDNFR-alpha-2;
DE            Short=GFR-alpha-2;
DE   Flags: Precursor;
GN   Name=GFRA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for neurturin. Mediates the NRTN-induced
CC       autophosphorylation and activation of the RET receptor. Also able to
CC       mediate GDNF signaling through the RET tyrosine kinase receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SORL1. {ECO:0000250|UniProtKB:O00451}.
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; BT020800; AAX08817.1; -; mRNA.
DR   EMBL; BC120281; AAI20282.1; -; mRNA.
DR   RefSeq; NP_001015595.2; NM_001015595.2.
DR   AlphaFoldDB; Q5E9X0; -.
DR   SMR; Q5E9X0; -.
DR   STRING; 9913.ENSBTAP00000027545; -.
DR   PaxDb; Q5E9X0; -.
DR   PRIDE; Q5E9X0; -.
DR   GeneID; 514036; -.
DR   KEGG; bta:514036; -.
DR   CTD; 2675; -.
DR   eggNOG; ENOG502QS3P; Eukaryota.
DR   InParanoid; Q5E9X0; -.
DR   OrthoDB; 482696at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0016167; F:glial cell-derived neurotrophic factor receptor activity; 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; IPR003504; GDNF_rcpt_a2.
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; PR01318; GDNFRALPHA2.
DR   PRINTS; PR01316; GDNFRECEPTOR.
DR   SMART; SM00907; GDNF; 3.
DR   SUPFAM; SSF110035; SSF110035; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor;
KW   Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..440
FT                   /note="GDNF family receptor alpha-2"
FT                   /id="PRO_0000259986"
FT   PROPEP          441..464
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000259987"
FT   REGION          360..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           440
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        81
FT                   /note="A -> S (in Ref. 2; AAI20282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="K -> Q (in Ref. 2; AAI20282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  51659 MW;  BF0BF88F4298B5AA CRC64;
     MILANAFCLF FFLDETLRSL ASPSSPQGPE LHGWRPPVDC VRANELCAAE SNCSSRYRTL
     RQCLAGRDRN TMLANKECQA ALEVLQESPL YDCRCKRGMK KELQCLQIYW SIHLGLTEGE
     EFYEASPYEP VTARLSDIFR LASIFSGTGA DPAVSTKSNH CLDAAKACNL NDNCKKLRSS
     YISICNREIS PTERCNRRKC HKALRQFFDR VPSEYTYRML FCSCQDQACA ERRRQTILPS
     CSYEDKEKPN CLDLRSLCRT DHLCRSRLAD FHANCRASYQ TLTSCPTDNY QACLGSYAGM
     IGFDITPNYV DSSPTGIVVS PWCSCRGSGN MEEECEKFLK DFTENPCLRN AIQAFGNGTD
     VNLSPKSPPF QATQAPRVDK TPSLPDDLSD STSLGTSVIS TCTSVQDQGL KANNSKELSM
     CFTELTTNII PGSKRVIKPN SGPRRTRPSA ALTAASFLML KLAL