Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23242 (CXA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gap junction alpha-1 protein
Alternative name(s):
Connexin-43
Short name=Cx43
Gap junction 43 kDa heart protein
Gene names
Name:Gja1
Synonyms:Cxn-43
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.16

Connexin 43 is possibly the ATP-induced pore of mouse macrophages. Ref.16

Subunit structure

A connexon is composed of a hexamer of connexins. Interacts with SGSM3 and CSNK1D. Interacts with KIAA1432/CIP150 By similarity. Interacts (via C-terminus) with TJP1. Interacts (via C-terminus) with SRC (via SH3 domain). Interacts with UBQLN4 By similarity. Interacts with CNST. Ref.11 Ref.14

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctiongap junction.

Tissue specificity

Expressed in heart, non-sensory epithelial cells, and in fibrocytes of the spiral ligament and the spiral limbus. Expressed in bladder smooth muscle cells (at protein level). Ref.9 Ref.10 Ref.16

Developmental stage

At 7.5 dpc, expressed in the embryo, but not in the extraembryonic region containing the ectoplacental cone. Ref.4

Induction

In bladder smooth muscle cells, exhibits night/day variations with low levels during the sleep phase, at circadian time (CT) 4-12 (at protein level). Downregulation during the night allows increase in bladder capacity, avoiding disturbance of sleep by micturition. Expression starts to increase around CT12 and forms a plateau during the active phase (CT16-24) (at protein level). Circadian transcription is activated by NR1D1. Up-regulated by SP1 and SP3. Ref.16

Post-translational modification

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.

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.

Disruption phenotype

Mutant mice die shortly after birth. Ref.16

Sequence similarities

Belongs to the connexin family. Alpha-type (group II) subfamily.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Gap junction
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
Isopeptide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP transport

Inferred from electronic annotation. Source: Ensembl

adult heart development

Inferred from mutant phenotype PubMed 9486664. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: Ensembl

atrial ventricular junction remodeling

Inferred from genetic interaction PubMed 10969038. Source: MGI

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 16624854. Source: MGI

cardiac conduction

Inferred from mutant phenotype PubMed 10969038PubMed 9109444. Source: MGI

cell communication by chemical coupling

Inferred from direct assay PubMed 15084279. Source: MGI

cell communication by electrical coupling

Inferred from direct assay PubMed 15084279. Source: MGI

cell-cell junction organization

Inferred from mutant phenotype PubMed 9620080. Source: MGI

cell-cell signaling

Inferred from direct assay PubMed 11397787. Source: MGI

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from mutant phenotype PubMed 19439426. Source: MGI

embryonic heart tube development

Inferred from mutant phenotype PubMed 14732399. Source: MGI

endothelium development

Inferred from electronic annotation. Source: Ensembl

epicardial cell to mesenchymal cell transition

Traceable author statement PubMed 20299672. Source: DFLAT

epithelial cell maturation

Inferred from mutant phenotype PubMed 16624854. Source: MGI

establishment of epithelial cell polarity

Traceable author statement PubMed 20299672. Source: DFLAT

heart development

Inferred from mutant phenotype PubMed 16624854. Source: MGI

heart looping

Inferred from mutant phenotype PubMed 9486664. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 9486664. Source: MGI

lens development in camera-type eye

Inferred from mutant phenotype PubMed 9620080. Source: MGI

milk ejection

Inferred from mutant phenotype PubMed 20089884. Source: MGI

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from mutant phenotype PubMed 19439426. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 12638734. Source: MGI

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from mutant phenotype PubMed 12606326. Source: MGI

positive regulation of behavioral fear response

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell communication by chemical coupling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 19439426. Source: MGI

positive regulation of glomerular filtration

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of striated muscle tissue development

Inferred from mutant phenotype PubMed 15601660. Source: MGI

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of atrial cardiac muscle cell membrane depolarization

Inferred from mutant phenotype PubMed 10969038. Source: MGI

regulation of blood vessel remodeling

Traceable author statement PubMed 20299672. Source: DFLAT

regulation of bone mineralization

Inferred from mutant phenotype PubMed 21346198. Source: MGI

regulation of bone remodeling

Inferred from mutant phenotype PubMed 21346198. Source: MGI

regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of heart contraction

Inferred from mutant phenotype PubMed 11179202PubMed 11397787. Source: MGI

regulation of tight junction assembly

Inferred from electronic annotation. Source: Ensembl

regulation of ventricular cardiac muscle cell membrane depolarization

Inferred from mutant phenotype PubMed 10969038PubMed 9109444. Source: MGI

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype PubMed 10969038. Source: MGI

response to fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue regeneration

Inferred from direct assay PubMed 15601660. Source: MGI

transmembrane transport

Inferred from direct assay PubMed 11397787PubMed 15084279. Source: GOC

vascular transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15084279. Source: MGI

apical plasma membrane

Inferred from direct assay PubMed 9620080. Source: MGI

cell junction

Inferred from direct assay PubMed 15601660. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 15331634PubMed 21296051. Source: MGI

connexon complex

Inferred from electronic annotation. Source: InterPro

contractile fiber

Inferred from direct assay PubMed 21708977. Source: MGI

cytoplasm

Inferred from direct assay PubMed 9620080. Source: MGI

cytosol

Inferred from direct assay PubMed 15331634. Source: MGI

early endosome

Inferred from electronic annotation. Source: Ensembl

fascia adherens

Inferred from direct assay PubMed 11732910. Source: MGI

gap junction

Inferred from direct assay PubMed 11922902PubMed 12738802PubMed 14595769PubMed 15084279PubMed 20086016PubMed 20089884. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intercalated disc

Inferred from direct assay PubMed 17884088. Source: BHF-UCL

intermediate filament

Inferred from direct assay PubMed 16917092. Source: BHF-UCL

lateral plasma membrane

Inferred from direct assay PubMed 9620080. Source: MGI

lysosome

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 15084279. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

multivesicular body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15084279PubMed 15331634. Source: MGI

   Molecular_functionbeta-tubulin binding

Inferred from direct assay PubMed 15084279. Source: MGI

gap junction channel activity

Inferred from direct assay PubMed 11397787PubMed 15084279. Source: MGI

protein binding

Inferred from physical interaction PubMed 18055446. Source: IntAct

receptor binding

Inferred from physical interaction PubMed 15331634. Source: MGI

scaffold protein binding

Inferred from physical interaction PubMed 19544087. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 382381Gap junction alpha-1 protein
PRO_0000057802

Regions

Topological domain2 – 1312Cytoplasmic Potential
Transmembrane14 – 3623Helical; Potential
Topological domain37 – 7640Extracellular Potential
Transmembrane77 – 9923Helical; Potential
Topological domain100 – 15455Cytoplasmic Potential
Transmembrane155 – 17723Helical; Potential
Topological domain178 – 20831Extracellular Potential
Transmembrane209 – 23123Helical; Potential
Topological domain232 – 382151Cytoplasmic Potential

Amino acid modifications

Modified residue2471Phosphotyrosine Ref.13
Modified residue2551Phosphoserine By similarity
Modified residue2621Phosphoserine By similarity
Modified residue2711S-nitrosocysteine Ref.15
Modified residue3061Phosphoserine By similarity
Modified residue3141Phosphoserine By similarity
Modified residue3251Phosphoserine; by CK1 By similarity
Modified residue3281Phosphoserine; by CK1
Modified residue3301Phosphoserine; by CK1
Modified residue3651Phosphoserine By similarity
Modified residue3681Phosphoserine; by PKC/PRKCG By similarity
Modified residue3691Phosphoserine By similarity
Modified residue3731Phosphoserine By similarity
Disulfide bond54 ↔ 192 By similarity
Disulfide bond187 ↔ 198 By similarity
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict211G → V in BAC26375. Ref.5
Sequence conflict3201M → T in AAA53027. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P23242 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 018DCB461FA69490

FASTA38243,004
        10         20         30         40         50         60 
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG 

        70         80         90        100        110        120 
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG 

       130        140        150        160        170        180 
VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS 

       190        200        210        220        230        240 
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV 

       250        260        270        280        290        300 
KGRSDPYHAT TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN 

       310        320        330        340        350        360 
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD SQNAKKVAAG HELQPLAIVD 

       370        380 
QRPSSRASSR ASSRPRPDDL EI 

« Hide

References

« Hide 'large scale' references
[1]"Evidence that the gap junction protein connexin-43 is the ATP-induced pore of mouse macrophages."
Beyer E.C., Steinberg T.H.
J. Biol. Chem. 266:7971-7974(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Developmental regulation of gap junction gene expression during mouse embryonic development."
Nishi M., Kumar N.M., Gilula N.B.
Dev. Biol. 146:117-130(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Ovary.
[3]"Molecular cloning and functional expression of mouse connexin40, a second gap junction gene preferentially expressed in lung."
Hennemann J., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E., Schwarz J., Nicholson B.J., Willecke K.
J. Cell Biol. 117:1299-1310(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6.
[4]"Structure, sequence and expression of the mouse Cx43 gene encoding connexin 43."
Sullivan R., Ruangvoravat C., Joo D., Morgan J., Wang B.L., Wang X.K., Lo C.W.
Gene 130:191-199(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Tissue: Embryo.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Blastocyst, Head, Lung and Vagina.
[6]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[9]"Changes in the expression of connexin 43, a cardiac gap junctional protein, during mouse heart development."
Fromaget C., el Aoumari A., Dupont E., Briand J.-P., Gros D.
J. Mol. Cell. Cardiol. 22:1245-1258(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Mutations in GJA1 (connexin 43) are associated with non-syndromic autosomal recessive deafness."
Liu X.Z., Xia X.J., Adams J., Chen Z.Y., Welch K.O., Tekin M., Ouyang X.M., Kristiansen A., Pandya A., Balkany T., Arnos K.S., Nance W.E.
Hum. Mol. Genet. 10:2945-2951(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation."
Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.
Biochemistry 44:2385-2396(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGSM3.
[12]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[13]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[14]"Consortin, a trans-Golgi network cargo receptor for the plasma membrane targeting and recycling of connexins."
del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D., Chavrier P., Meda P., Petit C.
Hum. Mol. Genet. 19:262-275(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNST.
[15]"Compartmentalized connexin 43 s-nitrosylation/denitrosylation regulates heterocellular communication in the vessel wall."
Straub A.C., Billaud M., Johnstone S.R., Best A.K., Yemen S., Dwyer S.T., Looft-Wilson R., Lysiak J.J., Gaston B., Palmer L., Isakson B.E.
Arterioscler. Thromb. Vasc. Biol. 31:399-407(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-271.
[16]"Involvement of urinary bladder Connexin43 and the circadian clock in coordination of diurnal micturition rhythm."
Negoro H., Kanematsu A., Doi M., Suadicani S.O., Matsuo M., Imamura M., Okinami T., Nishikawa N., Oura T., Matsui S., Seo K., Tainaka M., Urabe S., Kiyokage E., Todo T., Okamura H., Tabata Y., Ogawa O.
Nat. Commun. 3:809-809(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61896 Genomic DNA. Translation: AAA37444.1.
M63801 mRNA. Translation: AAA53027.1.
X62836 Genomic DNA. Translation: CAA44640.1.
X61576 mRNA. Translation: CAA43778.1.
AK029291 mRNA. Translation: BAC26375.1.
AK036979 mRNA. Translation: BAC29656.1.
AK145692 mRNA. Translation: BAE26592.1.
AK165986 mRNA. Translation: BAE38502.1.
CT010327 mRNA. Translation: CAJ18535.1.
CH466540 Genomic DNA. Translation: EDL05108.1.
BC006894 mRNA. Translation: AAH06894.1.
CCDSCCDS23851.1.
PIRA39802.
RefSeqNP_034418.1. NM_010288.3.
XP_006512604.1. XM_006512541.1.
UniGeneMm.378921.

3D structure databases

ProteinModelPortalP23242.
SMRP23242. Positions 3-234, 252-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199923. 6 interactions.
DIPDIP-29207N.
IntActP23242. 10 interactions.
MINTMINT-1326689.

PTM databases

PhosphoSiteP23242.

Proteomic databases

MaxQBP23242.
PaxDbP23242.
PRIDEP23242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
GeneID14609.
KEGGmmu:14609.
UCSCuc007fcc.2. mouse.

Organism-specific databases

CTD2697.
MGIMGI:95713. Gja1.

Phylogenomic databases

eggNOGNOG45368.
GeneTreeENSGT00740000115305.
HOVERGENHBG009576.
InParanoidP23242.
KOK07372.
OMAGANVDMH.
OrthoDBEOG7P2XSS.
PhylomeDBP23242.
TreeFamTF329606.

Gene expression databases

ArrayExpressP23242.
BgeeP23242.
CleanExMM_GJA1.
GenevestigatorP23242.

Family and domain databases

InterProIPR000500. Connexin.
IPR002261. Connexin43.
IPR013124. Connexin43_C.
IPR019570. Connexin_CCC.
IPR017990. Connexin_CS.
IPR013092. Connexin_N.
[Graphical view]
PANTHERPTHR11984. PTHR11984. 1 hit.
PfamPF00029. Connexin. 1 hit.
PF03508. Connexin43. 1 hit.
PF10582. Connexin_CCC. 1 hit.
[Graphical view]
PRINTSPR00206. CONNEXIN.
PR01132. CONNEXINA1.
SMARTSM00037. CNX. 1 hit.
SM01089. Connexin_CCC. 1 hit.
[Graphical view]
PROSITEPS00407. CONNEXINS_1. 1 hit.
PS00408. CONNEXINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGJA1. mouse.
NextBio286404.
PROP23242.
SOURCESearch...

Entry information

Entry nameCXA1_MOUSE
AccessionPrimary (citable) accession number: P23242
Secondary accession number(s): Q544I7, Q8CE05
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot