GFRA1_HUMAN
ID GFRA1_HUMAN Reviewed; 465 AA.
AC P56159; A8KA21; O15507; O43912;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
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=RET ligand 1;
DE AltName: Full=TGF-beta-related neurotrophic factor receptor 1;
DE Flags: Precursor;
GN Name=GFRA1; Synonyms=GDNFRA, RETL1, TRNR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Substantia nigra;
RX PubMed=8674117; DOI=10.1016/s0092-8674(00)81311-2;
RA Jing S., Wen D., Yu Y., Holst P.L., Luo Y., Fang M., Tamir R., Antonio L.,
RA Hu Z., Cupples R., Louis J.-C., Hu S., Altrock B.W., Fox G.M.;
RT "GDNF-induced activation of the ret protein tyrosine kinase is mediated by
RT GDNFR-alpha, a novel receptor for GDNF.";
RL Cell 85:1113-1124(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=9177201; DOI=10.1073/pnas.94.12.6238;
RA Sanicola M., Hession C.A., Worley D.S., Carmillo P., Ehrenfels C.,
RA Walus L., Robinson S., Jaworski G., Wei H., Tizard R., Whitty A.,
RA Pepinsky R.B., Cate R.L.;
RT "Glial cell line-derived neurotrophic factor-dependent RET activation can
RT be mediated by two different cell-surface accessory proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6238-6243(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS ASN-85
RP AND ALA-366.
RX PubMed=9545641; DOI=10.1006/geno.1997.5191;
RA Angrist M., Jing S., Bolk S., Bentley K., Nallasamy S., Halushka M.,
RA Fox G.M., Chakravarti A.;
RT "Human GFRA1: cloning, mapping, genomic structure, and evaluation as a
RT candidate gene for Hirschsprung disease susceptibility.";
RL Genomics 48:354-362(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thyroid carcinoma;
RX PubMed=9600247; DOI=10.1007/s004390050724;
RA Shefelbine S.E., Khorana S., Schultz P.N., Huang E., Thobe N., Hu Z.J.,
RA Fox G.M., Jing S., Cote G.J., Gagel R.F.;
RT "Mutational analysis of the GDNF/RET-GDNFR-alpha signaling complex in a
RT kindred with vesicoureteral reflux.";
RL Hum. Genet. 102:474-478(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Substantia nigra;
RA Hishiki T., Kondoh K., Ichimiya S., Nimura Y., Seki N., Ozaki T.,
RA Sakiyama S., Takahashi H., Ohnuma N., Tanabe M., Fujimura S.,
RA Nakagawara A.;
RT "GDNF-induced differentiation and its enhancement by retinoic acid in
RT primary human neuroblastomas expressing c-Ret and GDNFR-alpha.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [10]
RP INTERACTION WITH RET AND SORL1.
RX PubMed=23333276; DOI=10.1016/j.celrep.2012.12.011;
RA Glerup S., Lume M., Olsen D., Nyengaard J.R., Vaegter C.B., Gustafsen C.,
RA Christensen E.I., Kjolby M., Hay-Schmidt A., Bender D., Madsen P.,
RA Saarma M., Nykjaer A., Petersen C.M.;
RT "SorLA controls neurotrophic activity by sorting of GDNF and its receptors
RT GFRalpha1 and RET.";
RL Cell Rep. 3:186-199(2013).
RN [11]
RP VARIANTS ALA-366 AND ARG-371.
RX PubMed=14566559; DOI=10.1007/s00439-003-1036-z;
RA Sasaki A., Kanai M., Kijima K., Akaba K., Hashimoto M., Hasegawa H.,
RA Otaki S., Koizumi T., Kusuda S., Ogawa Y., Tuchiya K., Yamamoto W.,
RA Nakamura T., Hayasaka K.;
RT "Molecular analysis of congenital central hypoventilation syndrome.";
RL Hum. Genet. 114:22-26(2003).
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 (By
CC similarity). Interacts with RET (PubMed:23333276). Interacts with
CC SORL1, either alone or in complex with GDNF (PubMed:23333276).
CC Interaction between SORL1 and GFRA1 leads to GFRA1 internalization, but
CC not degradation (PubMed:23333276). {ECO:0000250|UniProtKB:Q62997,
CC ECO:0000269|PubMed:23333276}.
CC -!- INTERACTION:
CC P56159-2; Q92673: SORL1; NbExp=3; IntAct=EBI-15854635, EBI-1171329;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62997};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q62997}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q62997}. Endosome
CC {ECO:0000250|UniProtKB:Q62997}. Endosome, multivesicular body
CC {ECO:0000250|UniProtKB:Q62997}. Note=Localizes mainly to the plasma
CC membrane. In the presence of SORL1, shifts to vesicular structures,
CC including trans-Golgi network, endosomes and multivesicular bodies.
CC {ECO:0000250|UniProtKB:Q62997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56159-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56159-2; Sequence=VSP_001660;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GDNFR family. {ECO:0000305}.
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DR EMBL; U97144; AAC51646.1; -; mRNA.
DR EMBL; AF038420; AAC39693.1; -; Genomic_DNA.
DR EMBL; AF038411; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038412; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038413; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038414; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038415; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038416; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038417; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038418; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038419; AAC39693.1; JOINED; Genomic_DNA.
DR EMBL; AF038421; AAC39692.1; -; mRNA.
DR EMBL; AF042080; AAB97371.1; -; mRNA.
DR EMBL; AF058999; AAC14431.1; -; Genomic_DNA.
DR EMBL; AF058990; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058991; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058992; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058993; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058994; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058995; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058996; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058997; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; AF058998; AAC14431.1; JOINED; Genomic_DNA.
DR EMBL; U95847; AAB71811.1; -; mRNA.
DR EMBL; AK292886; BAF85575.1; -; mRNA.
DR EMBL; CH471066; EAW49458.1; -; Genomic_DNA.
DR EMBL; BC014962; AAH14962.1; -; mRNA.
DR CCDS; CCDS44481.1; -. [P56159-1]
DR CCDS; CCDS7593.1; -. [P56159-2]
DR RefSeq; NP_001138925.1; NM_001145453.2. [P56159-2]
DR RefSeq; NP_001335025.1; NM_001348096.1. [P56159-2]
DR RefSeq; NP_001335026.1; NM_001348097.1.
DR RefSeq; NP_001335027.1; NM_001348098.1. [P56159-1]
DR RefSeq; NP_005255.1; NM_005264.5. [P56159-1]
DR RefSeq; NP_665736.1; NM_145793.4. [P56159-2]
DR RefSeq; XP_011537936.1; XM_011539634.1. [P56159-1]
DR PDB; 6Q2N; EM; 4.40 A; C/D=25-426.
DR PDBsum; 6Q2N; -.
DR AlphaFoldDB; P56159; -.
DR SMR; P56159; -.
DR BioGRID; 108942; 8.
DR DIP; DIP-59052N; -.
DR IntAct; P56159; 4.
DR STRING; 9606.ENSP00000347591; -.
DR ChEMBL; CHEMBL3833481; -.
DR GuidetoPHARMACOLOGY; 1743; -.
DR GlyConnect; 1265; 9 N-Linked glycans (1 site).
DR GlyGen; P56159; 3 sites, 8 N-linked glycans (1 site).
DR iPTMnet; P56159; -.
DR PhosphoSitePlus; P56159; -.
DR BioMuta; GFRA1; -.
DR DMDM; 20141405; -.
DR jPOST; P56159; -.
DR MassIVE; P56159; -.
DR MaxQB; P56159; -.
DR PaxDb; P56159; -.
DR PeptideAtlas; P56159; -.
DR PRIDE; P56159; -.
DR ProteomicsDB; 56888; -. [P56159-1]
DR ProteomicsDB; 56889; -. [P56159-2]
DR Antibodypedia; 18697; 470 antibodies from 40 providers.
DR DNASU; 2674; -.
DR Ensembl; ENST00000355422.11; ENSP00000347591.6; ENSG00000151892.16. [P56159-1]
DR Ensembl; ENST00000369234.5; ENSP00000358237.4; ENSG00000151892.16. [P56159-1]
DR Ensembl; ENST00000369236.5; ENSP00000358239.1; ENSG00000151892.16. [P56159-2]
DR Ensembl; ENST00000439649.8; ENSP00000393725.3; ENSG00000151892.16. [P56159-2]
DR Ensembl; ENST00000682743.1; ENSP00000507970.1; ENSG00000151892.16. [P56159-2]
DR Ensembl; ENST00000684105.1; ENSP00000506818.1; ENSG00000151892.16. [P56159-2]
DR GeneID; 2674; -.
DR KEGG; hsa:2674; -.
DR MANE-Select; ENST00000355422.11; ENSP00000347591.6; NM_005264.8; NP_005255.1.
DR UCSC; uc001lci.4; human. [P56159-1]
DR CTD; 2674; -.
DR DisGeNET; 2674; -.
DR GeneCards; GFRA1; -.
DR HGNC; HGNC:4243; GFRA1.
DR HPA; ENSG00000151892; Low tissue specificity.
DR MIM; 601496; gene.
DR neXtProt; NX_P56159; -.
DR OpenTargets; ENSG00000151892; -.
DR PharmGKB; PA28653; -.
DR VEuPathDB; HostDB:ENSG00000151892; -.
DR eggNOG; ENOG502QQA2; Eukaryota.
DR GeneTree; ENSGT00940000155560; -.
DR HOGENOM; CLU_040179_1_1_1; -.
DR InParanoid; P56159; -.
DR OMA; CKKFLNF; -.
DR OrthoDB; 482696at2759; -.
DR PhylomeDB; P56159; -.
DR TreeFam; TF331647; -.
DR PathwayCommons; P56159; -.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-8853659; RET signaling.
DR SignaLink; P56159; -.
DR SIGNOR; P56159; -.
DR BioGRID-ORCS; 2674; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; GFRA1; human.
DR GeneWiki; GDNF_family_receptor_alpha_1; -.
DR GenomeRNAi; 2674; -.
DR Pharos; P56159; Tbio.
DR PRO; PR:P56159; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P56159; protein.
DR Bgee; ENSG00000151892; Expressed in endometrium epithelium and 153 other tissues.
DR Genevisible; P56159; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098797; C:plasma membrane protein complex; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0016167; F:glial cell-derived neurotrophic factor receptor activity; TAS:ProtInc.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0005030; F:neurotrophin receptor activity; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; GPI-anchor; Lipoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..429
FT /note="GDNF family receptor alpha-1"
FT /id="PRO_0000010777"
FT PROPEP 430..465
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010778"
FT REPEAT 25..113
FT /note="1"
FT REPEAT 150..238
FT /note="2"
FT REPEAT 239..342
FT /note="3"
FT LIPID 429
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..87
FT /evidence="ECO:0000250"
FT DISULFID 36..42
FT /evidence="ECO:0000250"
FT DISULFID 52..72
FT /evidence="ECO:0000250"
FT DISULFID 89..99
FT /evidence="ECO:0000250"
FT DISULFID 154..214
FT /evidence="ECO:0000250"
FT DISULFID 161..167
FT /evidence="ECO:0000250"
FT DISULFID 178..192
FT /evidence="ECO:0000250"
FT DISULFID 187..233
FT /evidence="ECO:0000250"
FT DISULFID 216..221
FT /evidence="ECO:0000250"
FT DISULFID 243..313
FT /evidence="ECO:0000250"
FT DISULFID 250..256
FT /evidence="ECO:0000250"
FT DISULFID 267..285
FT /evidence="ECO:0000250"
FT DISULFID 277..337
FT /evidence="ECO:0000250"
FT DISULFID 315..325
FT /evidence="ECO:0000250"
FT VAR_SEQ 140..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9177201,
FT ECO:0000303|Ref.5"
FT /id="VSP_001660"
FT VARIANT 85
FT /note="Y -> N (in dbSNP:rs8192662)"
FT /evidence="ECO:0000269|PubMed:9545641"
FT /id="VAR_012488"
FT VARIANT 366
FT /note="T -> A (in dbSNP:rs2072276)"
FT /evidence="ECO:0000269|PubMed:14566559,
FT ECO:0000269|PubMed:9545641"
FT /id="VAR_012489"
FT VARIANT 371
FT /note="L -> R (may be involved in congenital central
FT hypoventilation syndrome; dbSNP:rs924541616)"
FT /evidence="ECO:0000269|PubMed:14566559"
FT /id="VAR_018261"
FT CONFLICT 245
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="F -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51456 MW; 91A550D06A6777BD CRC64;
MFLATLYFAL PLLDLLLSAE VSGGDRLDCV KASDQCLKEQ SCSTKYRTLR QCVAGKETNF
SLASGLEAKD ECRSAMEALK QKSLYNCRCK RGMKKEKNCL RIYWSMYQSL QGNDLLEDSP
YEPVNSRLSD IFRVVPFISD VFQQVEHIPK GNNCLDAAKA CNLDDICKKY RSAYITPCTT
SVSNDVCNRR KCHKALRQFF DKVPAKHSYG MLFCSCRDIA CTERRRQTIV PVCSYEEREK
PNCLNLQDSC KTNYICRSRL ADFFTNCQPE SRSVSSCLKE NYADCLLAYS GLIGTVMTPN
YIDSSSLSVA PWCDCSNSGN DLEECLKFLN FFKDNTCLKN AIQAFGNGSD VTVWQPAFPV
QTTTATTTTA LRVKNKPLGP AGSENEIPTH VLPPCANLQA QKLKSNVSGN THLCISNGNY
EKEGLGASSH ITTKSMAAPP SCGLSPLLVL VVTALSTLLS LTETS
