Gja1
entrez
24392
canonical
uniprot
P08050
canonical
ensembl
ENSRNOG00000000805
resolver
ensembl
ENSRNOG00055015329
resolver
ensembl
ENSRNOG00060008013
resolver
ensembl
ENSRNOG00065003322
resolver
ensp
ENSRNOP00000001054
resolver
ensp
ENSRNOP00000093256
resolver
ensp
ENSRNOP00000100528
resolver
ensp
ENSRNOP00000103696
resolver
ensp
ENSRNOP00000107427
resolver
ensp
ENSRNOP00055021299
resolver
ensp
ENSRNOP00060010026
resolver
ensp
ENSRNOP00065003381
resolver
enst
ENSRNOT00000001054
resolver
enst
ENSRNOT00000100494
resolver
enst
ENSRNOT00000121800
resolver
enst
ENSRNOT00000134128
resolver
enst
ENSRNOT00000134365
resolver
enst
ENSRNOT00055026181
resolver
enst
ENSRNOT00060013216
resolver
enst
ENSRNOT00065004734
resolver
genesymbol
Gja1
resolver
genesymbol_syn
Cxn-43
resolver
uniprot
Q53ZE1
resolver
uniprot_entry
CXA1_RAT
resolver
uniprot_sec
Q53ZE1
resolver
amino_acid_sequence
MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
uniprot
proteins
function
FUNCTION: Structural component of the gap junction, a specialized intercellular structure consisting of a cluster of closely packed pairs of transmembrane channels, the connexons, that allow passage of small molecules and electrical signals between neighboring cells. Forms homotypic and heterotypic channels gated by transjunctional voltage (PubMed:12011467). May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph (By similarity). Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in the conductive system of ventricular myocardium and heart morphogenesis (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization (PubMed:15181016). Involved in intercellular innate immune signaling. Mediates translocation of 2',3'-cGAMP and 2',5'-oligoadenylates (2-5A) second messengers from virus-infected cells to macrophages and uninfected neighboring cells to propagate and amplify the antiviral immune response (By similarity). {ECO:0000250|UniProtKB:P17302, ECO:0000250|UniProtKB:P23242, ECO:0000269|PubMed:12011467, ECO:0000269|PubMed:15181016}.
uniprot
proteins
mass_dalton
43031
uniprot
proteins
mutagenesis
MUTAGEN 368; /note="S->A: Loss of phosphorylation by PKC/PRKCD."; /evidence="ECO:0000269|PubMed:24500718
uniprot
proteins
post_translational_modification
PTM: Contains at least one intramolecular disulfide bond.; PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity (By similarity). Phosphorylation at Ser-368 by PRKCD triggers its internalization into small vesicles leading to proteasome-mediated degradation (PubMed:24500718). Phosphorylation by MAPK1/MAPK3 at Ser-279 and Ser-282 leads to increased ubiquitination and lysosomal degradation (By similarity). {ECO:0000250|UniProtKB:P17302, ECO:0000250|UniProtKB:P23242, ECO:0000250|UniProtKB:Q6TYA7, ECO:0000269|PubMed:24500718}.; PTM: Ubiquitination results in lysosomal degradation. {ECO:0000250|UniProtKB:P23242}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the level of functional Cx43 gap junctions at the plasma membrane. May be desumoylated by SENP1 or SENP2 (By similarity). {ECO:0000250|UniProtKB:P17302}.; PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial gap junction in arteries, it augments channel permeability and may regulate of smooth muscle cell to endothelial cell communication. {ECO:0000250|UniProtKB:P23242}.; PTM: Acetylated in the developing cortex; leading to delocalization from the cell membrane. {ECO:0000250|UniProtKB:P23242}.
uniprot
proteins
protein_family
Alpha-type (group II) subfamily
uniprot
proteins
protein_family
Connexin family
uniprot
proteins
pubmed
12011467
uniprot
proteins
pubmed
12417300
uniprot
proteins
pubmed
1371548
uniprot
proteins
pubmed
15181016
uniprot
proteins
pubmed
15213231
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492000
uniprot
proteins
pubmed
1651718
uniprot
proteins
pubmed
1652440
uniprot
proteins
pubmed
1852114
uniprot
proteins
pubmed
18636092
uniprot
proteins
pubmed
20127391
uniprot
proteins
pubmed
21617128
uniprot
proteins
pubmed
22549838
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24500718
uniprot
proteins
pubmed
2472402
uniprot
proteins
pubmed
25225338
uniprot
proteins
pubmed
2826492
uniprot
proteins
pubmed
2987225
uniprot
proteins
pubmed
29959233
uniprot
proteins
sequence_length
382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18636092}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:18636092, ECO:0000269|PubMed:2472402, ECO:0000269|PubMed:25225338, ECO:0000269|PubMed:29959233}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Cell junction {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk (ICD) between two adjacent cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..44; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 77..97; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 208..228; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins