CXB2_RAT
ID CXB2_RAT Reviewed; 226 AA.
AC P21994;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Gap junction beta-2 protein;
DE AltName: Full=Connexin-26 {ECO:0000303|PubMed:2557354};
DE Short=Cx26 {ECO:0000303|PubMed:2557354};
GN Name=Gjb2; Synonyms=Cxn-26;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2557354; DOI=10.1083/jcb.109.6.3391;
RA Zhang J.T., Nicholson B.J.;
RT "Sequence and tissue distribution of a second protein of hepatic gap
RT junctions, Cx26, as deduced from its cDNA.";
RL J. Cell Biol. 109:3391-3401(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 1-18.
RX PubMed=2823143; DOI=10.1038/329732a0;
RA Nicholson B.J., Dermietzel R., Teplow D., Traub O., Willecke K.,
RA Revel J.-P.;
RT "Two homologous protein components of hepatic gap junctions.";
RL Nature 329:732-734(1987).
RN [4]
RP INTERACTION WITH CNST.
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. 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 (By
CC similarity). Interacts with CNST (PubMed:19864490).
CC {ECO:0000250|UniProtKB:P29033, ECO:0000250|UniProtKB:Q00977,
CC ECO:0000269|PubMed:19864490}.
CC -!- INTERACTION:
CC P21994; Q8CBC4-3: Cnst; Xeno; NbExp=2; IntAct=EBI-2616119, EBI-2615407;
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 -!- TISSUE SPECIFICITY: Liver, kidney, intestine, lung, spleen, stomach,
CC testis and brain, but not heart and adult skeletal muscle.
CC {ECO:0000269|PubMed:2557354}.
CC -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC subfamily. {ECO:0000305}.
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DR EMBL; BC078952; AAH78952.1; -; mRNA.
DR PIR; A33646; A33646.
DR RefSeq; NP_001004099.1; NM_001004099.2.
DR RefSeq; XP_017455254.1; XM_017599765.1.
DR AlphaFoldDB; P21994; -.
DR SMR; P21994; -.
DR BioGRID; 267087; 1.
DR DIP; DIP-48901N; -.
DR IntAct; P21994; 2.
DR STRING; 10116.ENSRNOP00000011711; -.
DR PaxDb; P21994; -.
DR Ensembl; ENSRNOT00000011711; ENSRNOP00000011711; ENSRNOG00000008855.
DR Ensembl; ENSRNOT00000104368; ENSRNOP00000082358; ENSRNOG00000008855.
DR GeneID; 394266; -.
DR KEGG; rno:394266; -.
DR UCSC; RGD:728891; rat.
DR CTD; 2706; -.
DR RGD; 728891; Gjb2.
DR eggNOG; ENOG502QWM8; Eukaryota.
DR GeneTree; ENSGT01030000234513; -.
DR HOGENOM; CLU_037388_4_1_1; -.
DR InParanoid; P21994; -.
DR OMA; RKFMKGE; -.
DR OrthoDB; 1043502at2759; -.
DR PhylomeDB; P21994; -.
DR TreeFam; TF329606; -.
DR Reactome; R-RNO-190872; Transport of connexons to the plasma membrane.
DR PRO; PR:P21994; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000008855; Expressed in esophagus and 19 other tissues.
DR Genevisible; P21994; RN.
DR GO; GO:0097449; C:astrocyte projection; IDA:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0030054; C:cell junction; IDA:RGD.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005921; C:gap junction; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; IMP:RGD.
DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0046697; P:decidualization; IEP:RGD.
DR GO; GO:1905867; P:epididymis development; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0016264; P:gap junction assembly; ISO:RGD.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IEP:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; ISO:RGD.
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 1: Evidence at protein level;
KW Calcium; Cell junction; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Gap junction; Hearing; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="Gap junction beta-2 protein"
FT /id="PRO_0000057860"
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; 26451 MW; E36EC95F1B235A0D CRC64;
MDWGTLQSIL GGVNKHSTSI GKIWLTVLFI FRIMILVVAA KEVWGDEQAD FVCNTLQPGC
KNVCYDHYFP ISHIRLWALQ LIMVSTPALL VAMHVAYRRH EKKRKFMKGE IKNEFKDIEE
IKTQKVRIEG SLWWTYTTSI FFRVIFEAVF MYVFYIMYNG FFMQRLVKCN AWPCPNTVDC
FISRPTEKTV FTVFMISVSG ICILLNITEL CYLFIRYCSG KSKRPV
