ID CXB2_MACMU Reviewed; 226 AA. AC Q8MIT8; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 14-DEC-2022, entry version 118. DE RecName: Full=Gap junction beta-2 protein; DE AltName: Full=Connexin-26; DE Short=Cx26; GN Name=GJB2; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Orten D.J., Bizzarri-Kriener C., Askew J.W., Li J.-L., Louis E., RA Kelley P.M., Kimberling W.J.; RT "Sequence comparison of primate connexin 26 (GJB2) genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Structural component of gap junctions. Gap junctions are CC dodecameric channels that connect the cytoplasm of adjoining cells. CC They are formed by the docking of two hexameric hemichannels, one from CC each cell membrane. Small molecules and ions diffuse from one cell to a CC neighboring cell via the central pore. {ECO:0000250|UniProtKB:P29033}. CC -!- SUBUNIT: A hemichannel or connexon is composed of a hexamer of CC connexins. A functional gap junction is formed by the apposition of two CC hemichannels (By similarity). Forms heteromeric channels with GJB4. CC Interacts with CNST (By similarity). {ECO:0000250|UniProtKB:P29033, CC ECO:0000250|UniProtKB:Q00977}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00977}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P29033}. Cell CC junction, gap junction {ECO:0000250|UniProtKB:Q00977}. Note=Colocalizes CC with GJB4 at gap junction plaques in the cochlea. CC {ECO:0000250|UniProtKB:Q00977}. CC -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I) 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; AY046584; AAL03976.1; -; Genomic_DNA. DR RefSeq; NP_001038200.1; NM_001044735.1. DR RefSeq; XP_014976159.1; XM_015120673.1. DR RefSeq; XP_014976160.1; XM_015120674.1. DR AlphaFoldDB; Q8MIT8; -. DR SMR; Q8MIT8; -. DR STRING; 9544.ENSMMUP00000013790; -. DR Ensembl; ENSMMUT00000014720; ENSMMUP00000013790; ENSMMUG00000010522. DR GeneID; 704224; -. DR KEGG; mcc:704224; -. DR CTD; 2706; -. DR VEuPathDB; HostDB:ENSMMUG00000010522; -. DR VGNC; VGNC:73060; GJB2. DR eggNOG; ENOG502QWM8; Eukaryota. DR GeneTree; ENSGT01030000234513; -. DR HOGENOM; CLU_037388_4_1_1; -. DR InParanoid; Q8MIT8; -. DR OMA; RKFMKGE; -. DR OrthoDB; 1043502at2759; -. DR TreeFam; TF329606; -. DR Proteomes; UP000006718; Chromosome 17. DR Bgee; ENSMMUG00000010522; Expressed in spermatocyte and 19 other tissues. DR ExpressionAtlas; Q8MIT8; baseline. DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005243; F:gap junction channel activity; ISS:UniProtKB. DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB. DR GO; GO:0016264; P:gap junction assembly; IEA:Ensembl. DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW. DR Gene3D; 1.20.1440.80; -; 1. DR InterPro; IPR000500; Connexin. DR InterPro; IPR002268; Connexin26. DR InterPro; IPR019570; Connexin_CCC. DR InterPro; IPR017990; Connexin_CS. DR InterPro; IPR013092; Connexin_N. DR InterPro; IPR038359; Connexin_N_sf. DR PANTHER; PTHR11984; CONNEXIN; 1. DR Pfam; PF00029; Connexin; 1. DR PRINTS; PR00206; CONNEXIN. DR PRINTS; PR01139; CONNEXINB2. DR SMART; SM00037; CNX; 1. DR SMART; SM01089; Connexin_CCC; 1. DR PROSITE; PS00407; CONNEXINS_1; 1. DR PROSITE; PS00408; CONNEXINS_2; 1. PE 3: Inferred from homology; KW Calcium; Cell junction; Cell membrane; Disulfide bond; Gap junction; KW Hearing; Membrane; Metal-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..226 FT /note="Gap junction beta-2 protein" FT /id="PRO_0000057857" FT INTRAMEM 2..13 FT /evidence="ECO:0000250|UniProtKB:P29033" FT TOPO_DOM 14..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 21..40 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P29033" FT TOPO_DOM 41..73 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P29033" FT TOPO_DOM 95..135 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 136..156 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P29033" FT TOPO_DOM 157..189 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 190..210 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P29033" FT TOPO_DOM 211..226 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT BINDING 42 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P29033" FT BINDING 45 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P29033" FT BINDING 47 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:P29033" FT DISULFID 53..180 FT /evidence="ECO:0000250|UniProtKB:P29033" FT DISULFID 60..174 FT /evidence="ECO:0000250|UniProtKB:P29033" FT DISULFID 64..169 FT /evidence="ECO:0000250|UniProtKB:P29033" SQ SEQUENCE 226 AA; 26224 MW; 1F4BAC3BB20D0528 CRC64; MDWGALQTIL GGVNKYSTSI GKIWLTVLFI FRIMILVVAA KEVWGDEQAD FVCNTLQPGC KNVCYDHYFP ISHIRLWALQ LIFVSTPALL VAMHVAYRRH EKKRKFIKGE IKNEFKDIEE IKTQKVRIEG SLWWTYTSSI FFRVVFEAAF MYVFYVMYDG FSMQRLVKCN AWPCPNTVDC FVSRPTEKTV FTVFMIAVSG ICILLNVTEL CYLLIRYCSG KSKKPV //