ID   A0A1B0GTH5_HUMAN        Unreviewed;       518 AA.
AC   A0A1B0GTH5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-DEC-2018, entry version 14.
DE   SubName: Full=Neuronal acetylcholine receptor subunit beta-2 {ECO:0000313|Ensembl:ENSP00000489703};
GN   Name=CHRNB2 {ECO:0000313|Ensembl:ENSP00000489703};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000489703, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000489703, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S.,
RA   Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J.,
RA   James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K.,
RA   Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G.,
RA   Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J.,
RA   Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L.,
RA   Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J.,
RA   Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A.,
RA   Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K.,
RA   Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N.,
RA   Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S.,
RA   Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L.,
RA   Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.,
RA   Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T.,
RA   Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R.,
RA   Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P.,
RA   Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D.,
RA   Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000489703}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000256|SAAS:SAAS00569352}; Multi-pass membrane
CC       protein {ECO:0000256|SAAS:SAAS00569352}. Cell membrane
CC       {ECO:0000256|SAAS:SAAS00569391}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00569391}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. {ECO:0000256|RuleBase:RU000687,
CC       ECO:0000256|SAAS:SAAS00978283}.
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DR   EMBL; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PeptideAtlas; A0A1B0GTH5; -.
DR   Ensembl; ENST00000636034; ENSP00000489703; ENSG00000160716.
DR   HGNC; HGNC:1962; CHRNB2.
DR   OpenTargets; ENSG00000160716; -.
DR   GeneTree; ENSGT00940000158417; -.
DR   OMA; PAHYNKL; -.
DR   ChiTaRS; CHRNB2; human.
DR   Proteomes; UP000005640; Chromosome 1.
DR   ExpressionAtlas; A0A1B0GTH5; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR032932; CHRNB2.
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; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   PANTHER; PTHR18945:SF80; PTHR18945:SF80; 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   3: Inferred from homology;
KW   Cell junction {ECO:0000256|SAAS:SAAS00103558};
KW   Cell membrane {ECO:0000256|SAAS:SAAS00081553};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00103544};
KW   Ion channel {ECO:0000256|SAAS:SAAS00032596};
KW   Ion transport {ECO:0000256|SAAS:SAAS00032596};
KW   Ligand-gated ion channel {ECO:0000256|SAAS:SAAS00032596};
KW   Membrane {ECO:0000256|SAAS:SAAS00081553,
KW   ECO:0000256|SAAS:SAAS00103558, ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|SAAS:SAAS00103558};
KW   Receptor {ECO:0000256|SAAS:SAAS00079193};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|SAAS:SAAS00103558};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00032596}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    518       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008408617.
FT   TRANSMEM    235    256       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    268    288       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    300    321       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    461    483       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       29    234       Neur_chan_LBD.
FT                                {ECO:0000259|Pfam:PF02931}.
FT   DOMAIN      241    478       Neur_chan_memb.
FT                                {ECO:0000259|Pfam:PF02932}.
SQ   SEQUENCE   518 AA;  58791 MW;  E1F3010DA966C0B4 CRC64;
     MARRCGPVAL LLGFGLLRLC SGVWGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL
     MVSLAQLISV HEREQIMTTN VWLTQEWEDY RLTWKPEEFD NMKKVRLPSK HIWLPDVVLY
     NNADGMYEVS FYSNAVVSYD GSIFWLPPAI YKSACKIEVK HFPFDQQNCT MKFRSWTYDR
     TEIDLVLKSE VASLDDFTPS GEWDIVALPG RRNENPDDST YVDITYDFII RRKPLFYTIN
     LIIPCVLITS LAILVFYLPS DCGEKMTLCI SVLLALTVFL LLISKIVPPT SLDVPLVGKY
     LMFTMVLVTF SIVTSVCVLN VHHRSPTTHT MAPWVKVVFL EKLPALLFMQ QPRHHCARQR
     LRLRRRQRER EGAGALFFRE APGADSCTCF VNRASVQGLA GAFGAEPAPV AGPGRSGEPC
     GCGLREAVDG VRFIADHMRS EDDDQSVSED WKYVAMVIDR LFLWIFVFVC VFGTIGMFLQ
     PLFQNYTTTT FLHSDHSAPS SKLKVWGARL SIRGASEF
//