ID   CXB2_MOUSE              Reviewed;         226 AA.
AC   Q00977;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Gap junction beta-2 protein;
DE   AltName: Full=Connexin-26;
DE            Short=Cx26;
GN   Name=Gjb2; Synonyms=Cxn-26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1322820;
RA   Willecke K., Nicholson B.J., Dahl E., Kozjek G., Hennemann H.;
RT   "Molecular cloning of mouse connexins26 and -32: similar genomic
RT   organization but distinct promoter sequences of two gap junction genes.";
RL   Eur. J. Cell Biol. 58:81-89(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2060697; DOI=10.1016/0012-1606(91)90452-9;
RA   Nishi M., Kumar N.M., Gilula N.B.;
RT   "Developmental regulation of gap junction gene expression during mouse
RT   embryonic development.";
RL   Dev. Biol. 146:117-130(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15692151; DOI=10.1152/ajpcell.00341.2004;
RA   Sun J., Ahmad S., Chen S., Tang W., Zhang Y., Chen P., Lin X.;
RT   "Cochlear gap junctions coassembled from Cx26 and 30 show faster
RT   intercellular Ca2+ signaling than homomeric counterparts.";
RL   Am. J. Physiol. 288:C613-C623(2005).
RN   [5]
RP   INTERACTION WITH CNST, AND SUBCELLULAR LOCATION.
RX   PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA   del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D.,
RA   Chavrier P., Meda P., Petit C.;
RT   "Consortin, a trans-Golgi network cargo receptor for the plasma membrane
RT   targeting and recycling of connexins.";
RL   Hum. Mol. Genet. 19:262-275(2010).
CC   -!- FUNCTION: Structural component of gap junctions (PubMed:15692151). 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 (PubMed:15692151). {ECO:0000250|UniProtKB:P29033,
CC       ECO:0000269|PubMed:15692151}.
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       (PubMed:15692151). Interacts with CNST (PubMed:19864490).
CC       {ECO:0000250|UniProtKB:P29033, ECO:0000269|PubMed:15692151,
CC       ECO:0000269|PubMed:19864490}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15692151,
CC       ECO:0000269|PubMed:19864490}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P29033}. Cell junction, gap junction
CC       {ECO:0000269|PubMed:15692151, ECO:0000269|PubMed:19864490}.
CC       Note=Colocalizes with GJB4 at gap junction plaques in the cochlea.
CC       {ECO:0000269|PubMed:15692151}.
CC   -!- TISSUE SPECIFICITY: Detected in cochlea (at protein level)
CC       (PubMed:15692151). Detected in cochlea (PubMed:15692151). Liver,
CC       kidney, intestine, lung, spleen, stomach, testis and brain, but not
CC       heart and adult skeletal muscle. {ECO:0000269|PubMed:15692151}.
CC   -!- DEVELOPMENTAL STAGE: Detected in cochlea after 14.5 dpc. Detected in
CC       the spiral limbus in neoneates at 2, 8 and 12 days after birth, before
CC       the onset of hearing. {ECO:0000269|PubMed:15692151}.
CC   -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M81445; AAA37495.1; -; Genomic_DNA.
DR   EMBL; M63803; AAA37276.1; -; mRNA.
DR   EMBL; BC013634; AAH13634.1; -; mRNA.
DR   EMBL; BC051437; AAH51437.1; -; mRNA.
DR   CCDS; CCDS27153.1; -.
DR   RefSeq; NP_032151.1; NM_008125.3.
DR   AlphaFoldDB; Q00977; -.
DR   SMR; Q00977; -.
DR   BioGRID; 199932; 1.
DR   IntAct; Q00977; 1.
DR   STRING; 10090.ENSMUSP00000054343; -.
DR   iPTMnet; Q00977; -.
DR   PhosphoSitePlus; Q00977; -.
DR   SwissPalm; Q00977; -.
DR   jPOST; Q00977; -.
DR   PaxDb; 10090-ENSMUSP00000054343; -.
DR   PeptideAtlas; Q00977; -.
DR   ProteomicsDB; 284074; -.
DR   Antibodypedia; 4587; 373 antibodies from 37 providers.
DR   DNASU; 14619; -.
DR   Ensembl; ENSMUST00000055698.8; ENSMUSP00000054343.8; ENSMUSG00000046352.8.
DR   GeneID; 14619; -.
DR   KEGG; mmu:14619; -.
DR   UCSC; uc007ucx.2; mouse.
DR   AGR; MGI:95720; -.
DR   CTD; 2706; -.
DR   MGI; MGI:95720; Gjb2.
DR   VEuPathDB; HostDB:ENSMUSG00000046352; -.
DR   eggNOG; ENOG502QWM8; Eukaryota.
DR   GeneTree; ENSGT01030000234513; -.
DR   HOGENOM; CLU_037388_4_1_1; -.
DR   InParanoid; Q00977; -.
DR   OMA; MYNGFSM; -.
DR   OrthoDB; 5301774at2759; -.
DR   PhylomeDB; Q00977; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-MMU-190872; Transport of connexons to the plasma membrane.
DR   BioGRID-ORCS; 14619; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Gjb2; mouse.
DR   PRO; PR:Q00977; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q00977; Protein.
DR   Bgee; ENSMUSG00000046352; Expressed in placenta labyrinth and 203 other cell types or tissues.
DR   ExpressionAtlas; Q00977; baseline and differential.
DR   GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005922; C:connexin complex; IDA:UniProtKB.
DR   GO; GO:0005921; C:gap junction; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005243; F:gap junction channel activity; IDA:UniProtKB.
DR   GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR   GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:1905867; P:epididymis development; IEA:Ensembl.
DR   GO; GO:0016264; P:gap junction assembly; IMP:MGI.
DR   GO; GO:1990349; P:gap junction-mediated intercellular transport; IDA:UniProtKB.
DR   GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0044752; P:response to human chorionic gonadotropin; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   Gene3D; 1.20.1440.80; Gap junction channel protein cysteine-rich domain; 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   PANTHER; PTHR11984:SF46; GAP JUNCTION BETA-2 PROTEIN; 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.
DR   Genevisible; Q00977; MM.
PE   1: Evidence at protein 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_0000057858"
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;  26411 MW;  0D8178F7A339E0B6 CRC64;
     MDWGTLQSIL GGVNKHSTSI GKIWLTVLFI FRIMILVVAA KEVWGDEQAD FVCNTLQPGC
     KNVCYDHHFP ISHIRLWALQ LIMVSTPALL VAMHVAYRRH EKKRKFMKGE IKNEFKDIEE
     IKTQKVRIEG SLWWTYTTSI FFRVIFEAVF MYVFYIMYNG FFMQRLVKCN AWPCPNTVDC
     FISRPTEKTV FTVFMISVSG ICILLNITEL CYLFVRYCSG KSKRPV
//