P08050 · CXA1_RAT
- ProteinGap junction alpha-1 protein
- GeneGja1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. 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 cell growth inhibition through the regulation of NOV expression and localization (PubMed:15181016).
Plays an essential role in gap junction communication in the ventricles (By similarity).
May play a role in cell growth inhibition through the regulation of NOV expression and localization (PubMed:15181016).
Plays an essential role in gap junction communication in the ventricles (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGap junction alpha-1 protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP08050
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localizes at the intercalated disk (ICD) in cardiomyocytes and the proper localization at ICD is dependent on TMEM65.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-23 | Cytoplasmic | ||||
Sequence: GDWSALGKLLDKVQAYSTAGGK | ||||||
Transmembrane | 24-44 | Helical | ||||
Sequence: VWLSVLFIFRILLLGTAVESA | ||||||
Topological domain | 45-76 | Extracellular | ||||
Sequence: WGDEQSAFRCNTQQPGCENVCYDKSFPISHVR | ||||||
Transmembrane | 77-97 | Helical | ||||
Sequence: FWVLQIIFVSVPTLLYLAHVF | ||||||
Topological domain | 98-155 | Cytoplasmic | ||||
Sequence: YVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTY | ||||||
Transmembrane | 156-176 | Helical | ||||
Sequence: IISILFKSVFEVAFLLIQWYI | ||||||
Topological domain | 177-207 | Extracellular | ||||
Sequence: YGFSLSAVYTCKRDPCPHQVDCFLSRPTEKT | ||||||
Transmembrane | 208-228 | Helical | ||||
Sequence: IFIIFMLVVSLVSLALNIIEL | ||||||
Topological domain | 229-382 | Cytoplasmic | ||||
Sequence: FYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 368 | Loss of phosphorylation by PKC/PRKCD. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, disulfide bond, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000057804 | 2-382 | Gap junction alpha-1 protein | |||
Sequence: GDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 54↔192 | |||||
Sequence: CNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPC | ||||||
Cross-link | 144 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Disulfide bond | 187↔198 | |||||
Sequence: CKRDPCPHQVDC | ||||||
Cross-link | 237 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Modified residue | 247 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 255 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 257 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 262 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 271 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 275 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 306 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 314 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 325 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 326 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 328 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 330 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 368 | Phosphoserine; by PKC/PRKCG and PKC/PRKCD | ||||
Sequence: S | ||||||
Modified residue | 369 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 373 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Contains at least one intramolecular disulfide bond.
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 at Ser-368 by PRKCD triggers its internalization into small vesicles leading to proteasome-mediated degradation (PubMed:24500718).
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).
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.
Acetylated in the developing cortex; leading to delocalization from the cell membrane.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in ventricle and atrium (at protein level).
Induction
In bladder smooth muscle cells, exhibits night/day variations with low levels during the sleep phase, at circadian time (CT) 4-8 (at protein level). Expression starts to increase around CT12 and forms a plateau during the active phase (CT16-24) (at protein level).
Gene expression databases
Interaction
Subunit
A connexon is composed of a hexamer of connexins (PubMed:1371548).
Interacts with SGSM3 (By similarity).
Interacts with RIC1/CIP150 (By similarity).
Interacts with CNST and CSNK1D (By similarity).
Interacts (via C-terminus) with TJP1 (PubMed:15492000, PubMed:18636092).
Interacts (via C-terminus) with SRC (via SH3 domain) (PubMed:15492000).
Interacts (not ubiquitinated) with UBQLN4 (via UBA domain) (PubMed:20127391).
Interacts with NOV (PubMed:15181016, PubMed:15213231).
Interacts with TMEM65 (By similarity).
Interacts with ANK3/ANKG and PKP2 (PubMed:21617128).
Interacts with SGSM3 (By similarity).
Interacts with RIC1/CIP150 (By similarity).
Interacts with CNST and CSNK1D (By similarity).
Interacts (via C-terminus) with TJP1 (PubMed:15492000, PubMed:18636092).
Interacts (via C-terminus) with SRC (via SH3 domain) (PubMed:15492000).
Interacts (not ubiquitinated) with UBQLN4 (via UBA domain) (PubMed:20127391).
Interacts with NOV (PubMed:15181016, PubMed:15213231).
Interacts with TMEM65 (By similarity).
Interacts with ANK3/ANKG and PKP2 (PubMed:21617128).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08050 | Kcnj8 Q63664 | 4 | EBI-476947, EBI-6991142 | |
XENO | P08050 | Sgsm3 Q8VCZ6 | 4 | EBI-476947, EBI-525155 | |
XENO | P08050 | UBQLN4 Q9NRR5 | 2 | EBI-476947, EBI-711226 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 244-382 | Interaction with NOV | ||||
Sequence: SDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI | ||||||
Region | 264-382 | Interaction with UBQLN4 | ||||
Sequence: KYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI | ||||||
Compositional bias | 317-337 | Polar residues | ||||
Sequence: QNRMGQAGSTISNSHAQPFDF | ||||||
Region | 317-382 | Disordered | ||||
Sequence: QNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI |
Sequence similarities
Belongs to the connexin family. Alpha-type (group II) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)43,031
- Last updated2007-01-23 v2
- Checksum0196416EA6A69490
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2UHE4 | A0A8L2UHE4_RAT | Gja1 | 360 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 5; AA sequence | ||||
Sequence: G → A | ||||||
Sequence conflict | 16 | in Ref. 2; no nucleotide entry | ||||
Sequence: A → T | ||||||
Sequence conflict | 28 | in Ref. 5; AA sequence | ||||
Sequence: V → I | ||||||
Compositional bias | 317-337 | Polar residues | ||||
Sequence: QNRMGQAGSTISNSHAQPFDF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X06656 EMBL· GenBank· DDBJ | CAA29855.1 EMBL· GenBank· DDBJ | mRNA | ||
AY324140 EMBL· GenBank· DDBJ | AAP88589.1 EMBL· GenBank· DDBJ | mRNA | ||
BC081842 EMBL· GenBank· DDBJ | AAH81842.1 EMBL· GenBank· DDBJ | mRNA |