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 31-JUL-2019, entry version 106. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; 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 CC cells. They are formed by the docking of two hexameric CC hemichannels, one from each cell membrane. Small molecules and CC ions diffuse from one cell to a neighboring cell via the central CC 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 CC of two hemichannels (By similarity). Forms heteromeric channels CC with GJB4. Interacts with CNST (By similarity). CC {ECO:0000250|UniProtKB:P29033, ECO:0000250|UniProtKB:Q00977}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:Q00977}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P29033}. Cell junction, gap junction CC {ECO:0000250|UniProtKB:Q00977}. Note=Colocalizes with GJB4 at gap CC junction plaques in the cochlea. {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 SMR; Q8MIT8; -. DR STRING; 9544.ENSMMUP00000013790; -. DR Ensembl; ENSMMUT00000014720; ENSMMUP00000013790; ENSMMUG00000010522. DR GeneID; 704224; -. DR KEGG; mcc:704224; -. DR CTD; 2706; -. DR VGNC; VGNC:73060; GJB2. DR eggNOG; ENOG410IFM8; Eukaryota. DR eggNOG; ENOG410Y7VN; LUCA. DR GeneTree; ENSGT00950000182704; -. DR HOGENOM; HOG000231127; -. DR InParanoid; Q8MIT8; -. DR KO; K07621; -. DR OMA; MYVFYIM; -. DR OrthoDB; 1043502at2759; -. DR TreeFam; TF329606; -. DR Proteomes; UP000006718; Chromosome 17. DR Bgee; ENSMMUG00000010522; Expressed in 12 organ(s), highest expression level in testis. DR ExpressionAtlas; Q8MIT8; baseline. DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB. DR GO; GO:0005887; C:integral component of 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; PTHR11984; 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; Complete proteome; KW Disulfide bond; Gap junction; Hearing; Membrane; Metal-binding; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 226 Gap junction beta-2 protein. FT /FTId=PRO_0000057857. FT INTRAMEM 2 13 {ECO:0000250|UniProtKB:P29033}. FT TOPO_DOM 14 20 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 21 40 Helical. {ECO:0000250|UniProtKB:P29033}. FT TOPO_DOM 41 73 Extracellular. {ECO:0000305}. FT TRANSMEM 74 94 Helical. {ECO:0000250|UniProtKB:P29033}. FT TOPO_DOM 95 135 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 136 156 Helical. {ECO:0000250|UniProtKB:P29033}. FT TOPO_DOM 157 189 Extracellular. {ECO:0000305}. FT TRANSMEM 190 210 Helical. {ECO:0000250|UniProtKB:P29033}. FT TOPO_DOM 211 226 Cytoplasmic. {ECO:0000305}. FT METAL 42 42 Calcium; shared with neighboring subunit. FT {ECO:0000250|UniProtKB:P29033}. FT METAL 45 45 Calcium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P29033}. FT METAL 47 47 Calcium. {ECO:0000250|UniProtKB:P29033}. FT DISULFID 53 180 {ECO:0000250|UniProtKB:P29033}. FT DISULFID 60 174 {ECO:0000250|UniProtKB:P29033}. FT DISULFID 64 169 {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 //