CXB2_SHEEP
ID CXB2_SHEEP Reviewed; 226 AA.
AC P46691;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Gap junction beta-2 protein;
DE AltName: Full=Connexin-26;
DE Short=Cx26;
GN Name=GJB2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea;
RA Dong Y., Green C., Donaldson P.J., Kistler J.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Structural component of gap junctions (By similarity). Gap
CC junctions are dodecameric channels that connect the cytoplasm of
CC adjoining cells. They are formed by the docking of two hexameric
CC hemichannels, one from each cell membrane (By similarity). Small
CC molecules and ions diffuse from one cell to a neighboring cell via the
CC central pore (By similarity). {ECO:0000250|UniProtKB:P29033,
CC ECO:0000250|UniProtKB:Q00977}.
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}.
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DR EMBL; U17592; AAA67446.1; -; mRNA.
DR RefSeq; NP_001009780.1; NM_001009780.1.
DR AlphaFoldDB; P46691; -.
DR SMR; P46691; -.
DR STRING; 9940.ENSOARP00000018338; -.
DR Ensembl; ENSOART00000018600; ENSOARP00000018338; ENSOARG00000017089.
DR Ensembl; ENSOART00020007702; ENSOARP00020006377; ENSOARG00020005049.
DR GeneID; 443345; -.
DR KEGG; oas:443345; -.
DR CTD; 2706; -.
DR eggNOG; ENOG502QWM8; Eukaryota.
DR HOGENOM; CLU_037388_4_1_1; -.
DR OMA; RKFMKGE; -.
DR OrthoDB; 1043502at2759; -.
DR Proteomes; UP000002356; Chromosome 10.
DR Bgee; ENSOARG00000017089; Expressed in rumen and 51 other tissues.
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 2: Evidence at transcript level;
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_0000057861"
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; 26215 MW; DCE2F0C1B4FCEF7D CRC64;
MDWSALQTIL GGVNKHSTSI GKIWLTVLFI FRIMILVVAA KEVWGDEQAD FVCNTLQPGC
KNVCYDHYFP ISHIRLWALQ LIFVSTPALL VAMHVAYYRH EKKRKFIRGE IKTEFKDIEE
IKNQKVRIEG SLWWTYTGSI FFRVIFEAAF MYVFYVMYDG FAMQRLVKCN AWPCPNTVDC
FVSRPTEKTV FTVFMIAVSG ICILLNVTEL CYLLIRFCSG KSKKPV
