ACHB4_HUMAN
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 03-AUG-2022, entry version 209.
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 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; 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 GlyGen; P30926; 4 sites.
DR iPTMnet; P30926; -.
DR PhosphoSitePlus; P30926; -.
DR BioMuta; CHRNB4; -.
DR DMDM; 2506129; -.
DR EPD; P30926; -.
DR MassIVE; P30926; -.
DR PaxDb; P30926; -.
DR PeptideAtlas; P30926; -.
DR PRIDE; P30926; -.
DR Antibodypedia; 15128; 176 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 CTD; 1143; -.
DR DisGeNET; 1143; -.
DR GeneCards; CHRNB4; -.
DR HGNC; HGNC:1964; CHRNB4.
DR HPA; ENSG00000117971; Tissue enhanced (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; PSKLYGN; -.
DR OrthoDB; 381858at2759; -.
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; 8 hits in 1065 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 right testis and 100 other tissues.
DR ExpressionAtlas; P30926; baseline and differential.
DR Genevisible; P30926; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 cation-selective channel activity; IDA:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; TAS:DFLAT.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; TAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
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 Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
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 PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
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
