ID   ACHB4_HUMAN             Reviewed;         498 AA.
AC   P30926; A4FTX5; E9PHE8; Q16607; Q4VBA5; Q8WXC8; Q9BQR4;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 218.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-4;
DE   Flags: Precursor;
GN   Name=CHRNB4;
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 [MRNA] (ISOFORM 1).
RX   PubMed=8906617; DOI=10.1007/bf02736842;
RA   Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E.,
RA   Johnson E.C., Velicelebi G., Harpold M.M.;
RT   "Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4
RT   nicotinic acetylcholine receptor subunits and functional expression of the
RT   alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits.";
RL   J. Mol. Neurosci. 7:217-228(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9203638; DOI=10.1124/mol.51.2.320;
RA   Gerzanich V., Kuryatov A., Anand R., Lindstrom J.;
RT   "'Orphan' alpha6 nicotinic AChR subunit can form a functional heteromeric
RT   acetylcholine receptor.";
RL   Mol. Pharmacol. 51:320-327(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9009220; DOI=10.1016/s0014-5793(96)01383-x;
RA   Groot Kormelink P.J., Luyten W.H.M.L.;
RT   "Cloning and sequence of full-length cDNAs encoding the human neuronal
RT   nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and
RT   expression of seven nAChR subunits in the human neuroblastoma cell line SH-
RT   SY5Y and/or IMR-32.";
RL   FEBS Lett. 400:309-314(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA   Duga S., Solda G., Asselta R., Bonati M.T., Dalpra L., Malcovati M.,
RA   Tenchini M.L.;
RT   "Characterization of the genomic structure of human nicotinic acetylcholine
RT   receptor CHRNA5/A3/B4 gene cluster: identification of two novel introns in
RT   the 3' untranslated region of CHRNA3 and of a tail-to-tail overlap between
RT   CHRNA3 and CHRNA5.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS TRP-136;
RP   GLY-140 AND VAL-467.
RX   PubMed=11450844; DOI=10.1007/pl00010921;
RA   Lev-Lehman E., Bercovich D., Xu W., Stockton D.W., Beaudet A.L.;
RT   "Characterization of the human beta4 nAChR gene and polymorphisms in CHRNA3
RT   and CHRNB4.";
RL   J. Hum. Genet. 46:362-366(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-198 (ISOFORM 2).
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX   PubMed=11742001; DOI=10.1074/jbc.m110454200;
RA   Valor L.M., Campos-Caro A., Carrasco-Serrano C., Ortiz J.A., Ballesta J.J.,
RA   Criado M.;
RT   "Transcription factors NF-Y and Sp1 are important determinants of the
RT   promoter activity of the bovine and human neuronal nicotinic receptor beta
RT   4 subunit genes.";
RL   J. Biol. Chem. 277:8866-8876(2002).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-498.
RX   PubMed=1330682; DOI=10.1016/0014-5793(92)81411-e;
RA   Tarroni P., Rubboli F., Chini B., Zwart R., Oortgiesen M., Sher E.,
RA   Clementi F.;
RT   "Neuronal-type nicotinic receptors in human neuroblastoma and small-cell
RT   lung carcinoma cell lines.";
RL   FEBS Lett. 312:66-70(1992).
RN   [10]
RP   SUBUNIT.
RX   PubMed=15609996; DOI=10.1021/bi048918g;
RA   Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT   "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT   nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT   subtypes.";
RL   Biochemistry 43:16019-16026(2004).
RN   [11]
RP   INTERACTION WITH RIC3.
RX   PubMed=16120769; DOI=10.1124/mol.105.017459;
RA   Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J.,
RA   Millar N.S.;
RT   "RIC-3 enhances functional expression of multiple nicotinic acetylcholine
RT   receptor subtypes in mammalian cells.";
RL   Mol. Pharmacol. 68:1431-1438(2005).
RN   [12]
RP   INTERACTION WITH LYPD6.
RX   PubMed=27344019; DOI=10.1111/jnc.13718;
RA   Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N.,
RA   Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M., Kohlmeier K.A.,
RA   Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S.;
RT   "Functional interaction between Lypd6 and nicotinic acetylcholine
RT   receptors.";
RL   J. Neurochem. 138:806-820(2016).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC       alpha and beta. Beta-4 subunit can be combined to alpha-2, alpha-3 or
CC       alpha-4 to give rise to functional receptors. Interacts with RIC3;
CC       which is required for proper folding and assembly (PubMed:16120769).
CC       Interacts with LYPD6 (PubMed:27344019). The pentamer alpha3-beta-4
CC       interacts with the conotoxin BuIA (By similarity). The heteropentamer
CC       composed of alpha-3 and beta-4 subunits interacts with the alpha-
CC       conotoxin ImI (PubMed:15609996). {ECO:0000250|UniProtKB:P12392,
CC       ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:16120769,
CC       ECO:0000269|PubMed:27344019}.
CC   -!- INTERACTION:
CC       P30926; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-9009018, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P30926-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P30926-2; Sequence=VSP_046674, VSP_046675;
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-4/CHRNB4 sub-
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U62439; AAB40117.1; -; mRNA.
DR   EMBL; U48861; AAA92123.1; -; mRNA.
DR   EMBL; Y08416; CAA69693.1; -; mRNA.
DR   EMBL; AJ306454; CAC34819.1; -; Genomic_DNA.
DR   EMBL; AJ306455; CAC34819.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306456; CAC34819.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306457; CAC34819.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306458; CAC34819.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306459; CAC34819.1; JOINED; Genomic_DNA.
DR   EMBL; AF306329; AAL02062.1; -; Genomic_DNA.
DR   EMBL; AF306325; AAL02062.1; JOINED; Genomic_DNA.
DR   EMBL; AF306326; AAL02062.1; JOINED; Genomic_DNA.
DR   EMBL; AF306327; AAL02062.1; JOINED; Genomic_DNA.
DR   EMBL; AF306328; AAL02062.1; JOINED; Genomic_DNA.
DR   EMBL; AC022748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC067863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096080; AAH96080.1; -; mRNA.
DR   EMBL; BC096081; AAH96081.1; -; mRNA.
DR   EMBL; BC096083; AAH96083.1; -; mRNA.
DR   EMBL; BC096082; AAH96082.1; -; mRNA.
DR   EMBL; AF453877; AAL57840.1; -; Genomic_DNA.
DR   EMBL; X68275; CAA48336.1; -; mRNA.
DR   CCDS; CCDS10306.1; -. [P30926-1]
DR   CCDS; CCDS58392.1; -. [P30926-2]
DR   PIR; G02421; G02421.
DR   RefSeq; NP_000741.1; NM_000750.3. [P30926-1]
DR   RefSeq; NP_001243496.1; NM_001256567.1. [P30926-2]
DR   PDB; 6PV7; EM; 3.34 A; B/C/E=22-361, B/C/E=417-498.
DR   PDB; 6PV8; EM; 3.87 A; B/C/E=22-361, B/C/E=417-498.
DR   PDBsum; 6PV7; -.
DR   PDBsum; 6PV8; -.
DR   AlphaFoldDB; P30926; -.
DR   EMDB; EMD-20487; -.
DR   EMDB; EMD-20488; -.
DR   SMR; P30926; -.
DR   BioGRID; 107565; 69.
DR   ComplexPortal; CPX-210; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR   ComplexPortal; CPX-213; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR   ComplexPortal; CPX-2190; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR   ComplexPortal; CPX-2200; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR   ComplexPortal; CPX-2203; Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4.
DR   CORUM; P30926; -.
DR   IntAct; P30926; 3.
DR   STRING; 9606.ENSP00000261751; -.
DR   BindingDB; P30926; -.
DR   ChEMBL; CHEMBL1907591; -.
DR   ChEMBL; CHEMBL1907594; -.
DR   ChEMBL; CHEMBL2109230; -.
DR   ChEMBL; CHEMBL3038459; -.
DR   ChEMBL; CHEMBL3137273; -.
DR   ChEMBL; CHEMBL3137285; -.
DR   ChEMBL; CHEMBL3885595; -.
DR   DrugBank; DB00237; Butabarbital.
DR   DrugBank; DB00565; Cisatracurium.
DR   DrugBank; DB00514; Dextromethorphan.
DR   DrugBank; DB07720; Epibatidine.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB00472; Fluoxetine.
DR   DrugBank; DB01227; Levacetylmethadol.
DR   DrugBank; DB00184; Nicotine.
DR   DrugBank; DB01090; Pentolinium.
DR   DrugBank; DB00202; Succinylcholine.
DR   DrugCentral; P30926; -.
DR   GlyCosmos; P30926; 4 sites, No reported glycans.
DR   GlyGen; P30926; 4 sites.
DR   iPTMnet; P30926; -.
DR   PhosphoSitePlus; P30926; -.
DR   BioMuta; CHRNB4; -.
DR   DMDM; 2506129; -.
DR   EPD; P30926; -.
DR   MassIVE; P30926; -.
DR   PaxDb; 9606-ENSP00000261751; -.
DR   PeptideAtlas; P30926; -.
DR   Antibodypedia; 15128; 186 antibodies from 29 providers.
DR   DNASU; 1143; -.
DR   Ensembl; ENST00000261751.8; ENSP00000261751.3; ENSG00000117971.12. [P30926-1]
DR   Ensembl; ENST00000412074.6; ENSP00000416386.2; ENSG00000117971.12. [P30926-2]
DR   GeneID; 1143; -.
DR   KEGG; hsa:1143; -.
DR   MANE-Select; ENST00000261751.8; ENSP00000261751.3; NM_000750.5; NP_000741.1.
DR   UCSC; uc002bed.2; human. [P30926-1]
DR   AGR; HGNC:1964; -.
DR   CTD; 1143; -.
DR   DisGeNET; 1143; -.
DR   GeneCards; CHRNB4; -.
DR   HGNC; HGNC:1964; CHRNB4.
DR   HPA; ENSG00000117971; Tissue enhanced (adrenal gland, lymphoid tissue, retina, testis).
DR   MIM; 118509; gene.
DR   neXtProt; NX_P30926; -.
DR   OpenTargets; ENSG00000117971; -.
DR   PharmGKB; PA26496; -.
DR   VEuPathDB; HostDB:ENSG00000117971; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158708; -.
DR   HOGENOM; CLU_018074_1_1_1; -.
DR   InParanoid; P30926; -.
DR   OMA; PRQKPCN; -.
DR   OrthoDB; 2872899at2759; -.
DR   PhylomeDB; P30926; -.
DR   TreeFam; TF315605; -.
DR   PathwayCommons; P30926; -.
DR   Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR   Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-HSA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P30926; -.
DR   BioGRID-ORCS; 1143; 9 hits in 1154 CRISPR screens.
DR   GeneWiki; CHRNB4; -.
DR   GenomeRNAi; 1143; -.
DR   Pharos; P30926; Tclin.
DR   PRO; PR:P30926; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P30926; Protein.
DR   Bgee; ENSG00000117971; Expressed in primordial germ cell in gonad and 102 other cell types or tissues.
DR   ExpressionAtlas; P30926; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR   GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:UniProtKB.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; TAS:DFLAT.
DR   GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0006811; P:monoatomic ion transport; TAS:UniProtKB.
DR   GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR   GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; NAS:UniProtKB.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0060084; P:synaptic transmission involved in micturition; IMP:UniProtKB.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:ProtInc.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF385; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT BETA-4; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; P30926; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..498
FT                   /note="Neuronal acetylcholine receptor subunit beta-4"
FT                   /id="PRO_0000000389"
FT   TOPO_DOM        22..236
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..498
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          357..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            82
FT                   /note="Key residue that facilitates effective access of the
FT                   conotoxin BuIA to the channel binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P12392"
FT   SITE            134
FT                   /note="Key residue for a low dissociation (K(off)) from the
FT                   conotoxin BuIA"
FT                   /evidence="ECO:0000250|UniProtKB:P12392"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        153..167
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         120..217
FT                   /note="NADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKF
FT                   RSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDP -> KSLRTGSTW
FT                   LWWWTGCSCGCSCLCASWALWGSSYRPSSRPMQLLRGPTLPSVTEGPLGCGVRGCEWPG
FT                   GHFAASFWVVADEALSKYVSIGHQPHQTSHSRGTGKDGGLGCPL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046674"
FT   VAR_SEQ         218..498
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046675"
FT   VARIANT         91
FT                   /note="T -> I (in dbSNP:rs12914008)"
FT                   /id="VAR_048174"
FT   VARIANT         136
FT                   /note="R -> W (in dbSNP:rs141876090)"
FT                   /evidence="ECO:0000269|PubMed:11450844"
FT                   /id="VAR_013241"
FT   VARIANT         140
FT                   /note="S -> G (in dbSNP:rs56218866)"
FT                   /evidence="ECO:0000269|PubMed:11450844"
FT                   /id="VAR_013242"
FT   VARIANT         467
FT                   /note="M -> V (in dbSNP:rs61737502)"
FT                   /evidence="ECO:0000269|PubMed:11450844"
FT                   /id="VAR_013243"
FT   CONFLICT        72..73
FT                   /note="EQ -> DE (in Ref. 9; CAA48336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="Missing (in Ref. 4; CAC34819)"
FT                   /evidence="ECO:0000305"
FT   HELIX           26..34
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            35..39
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          57..69
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            70..73
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          74..86
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            94..98
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            158..161
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          164..175
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          199..205
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           233..248
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           263..284
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           294..318
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           319..321
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           331..336
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   TURN            337..340
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           341..344
FT                   /evidence="ECO:0007829|PDB:6PV7"
FT   HELIX           422..477
FT                   /evidence="ECO:0007829|PDB:6PV7"
SQ   SEQUENCE   498 AA;  56380 MW;  0D48AB203F3FD03E CRC64;
     MRRAPSLVLF FLVALCGRGN CRVANAEEKL MDDLLNKTRY NNLIRPATSS SQLISIKLQL
     SLAQLISVNE REQIMTTNVW LKQEWTDYRL TWNSSRYEGV NILRIPAKRI WLPDIVLYNN
     ADGTYEVSVY TNLIVRSNGS VLWLPPAIYK SACKIEVKYF PFDQQNCTLK FRSWTYDHTE
     IDMVLMTPTA SMDDFTPSGE WDIVALPGRR TVNPQDPSYV DVTYDFIIKR KPLFYTINLI
     IPCVLTTLLA ILVFYLPSDC GEKMTLCISV LLALTFFLLL ISKIVPPTSL DVPLIGKYLM
     FTMVLVTFSI VTSVCVLNVH HRSPSTHTMA PWVKRCFLHK LPTFLFMKRP GPDSSPARAF
     PPSKSCVTKP EATATSTSPS NFYGNSMYFV NPASAASKSP AGSTPVAIPR DFWLRSSGRF
     RQDVQEALEG VSFIAQHMKN DDEDQSVVED WKYVAMVVDR LFLWVFMFVC VLGTVGLFLP
     PLFQTHAASE GPYAAQRD
//