ID A0A1B0GVD7_HUMAN Unreviewed; 504 AA. AC A0A1B0GVD7; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 05-DEC-2018, entry version 13. DE SubName: Full=Neuronal acetylcholine receptor subunit beta-2 {ECO:0000313|Ensembl:ENSP00000490474}; GN Name=CHRNB2 {ECO:0000313|Ensembl:ENSP00000490474}; 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:ENSP00000490474, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000490474, 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:ENSP00000490474} 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}. 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; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A1B0GVD7; -. DR Ensembl; ENST00000637900; ENSP00000490474; ENSG00000160716. DR HGNC; HGNC:1962; CHRNB2. DR OpenTargets; ENSG00000160716; -. DR GeneTree; ENSGT00940000158417; -. DR ChiTaRS; CHRNB2; human. DR Proteomes; UP000005640; Chromosome 1. DR ExpressionAtlas; A0A1B0GVD7; 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 26 504 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008408660. FT TRANSMEM 237 258 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 302 323 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 463 485 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 29 236 Neur_chan_LBD. FT {ECO:0000259|Pfam:PF02931}. FT DOMAIN 243 480 Neur_chan_memb. FT {ECO:0000259|Pfam:PF02932}. SQ SEQUENCE 504 AA; 57205 MW; 7593CD1A408DACAD CRC64; MARRCGPVAL LLGFGLLRLC SGVWGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL MVSLAQLISV HEREQIMTTN VWLTQVSEWE DYRLTWKPEE FDNMKKVRLP SKHIWLPDVV LYNNADGMYE VSFYSNAVVS YDGSIFWLPP AIYKSACKIE VKHFPFDQQN CTMKFRSWTY DRTEIDLVLK SEVASLDDFT PSGEWDIVAL PGRRNENPDD STYVDITYDF IIRRKPLFYT INLIIPCVLI TSLAILVFYL PSDCGEKMTL CISVLLALTV FLLLISKIVP PTSLDVPLVG KYLMFTMVLV TFSIVTSVCV LNVHHRSPTT HTMAPWVKVV FLEKLPALLF MQQPRHHCAR QRLRLRRRQR EREGAGALFF REAPGADSCT CFVNRASVQG LAGAFGAEPA PVAGPGRSGE PCGCGLREAV DGVRFIADHM RSEDDDQSVS EDWKYVAMVI DRLFLWIFVF VCVFGTIGMF LQPLFQNYTT TTFLHSDHSA PSSK //