P23242 (CXA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › gap 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 component	Cell junction Cell membrane Gap junction Membrane
Domain	Transmembrane Transmembrane helix
PTM	Disulfide bond Isopeptide bond Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP transport Inferred from electronic annotation. Source: Compara adult heart development Inferred from mutant phenotype PubMed 9486664. Source: MGI apoptotic process Inferred from mutant phenotype PubMed 19439426. Source: MGI 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 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 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 limb bud formation Inferred from mutant phenotype PubMed 19439426. Source: MGI milk ejection Inferred from mutant phenotype PubMed 20089884. Source: MGI negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara 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: Compara osteoblast differentiation Inferred from mutant phenotype PubMed 12606326. Source: MGI positive regulation of gene expression Inferred from mutant phenotype PubMed 19439426. Source: MGI positive regulation of protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of striated muscle tissue development Inferred from mutant phenotype PubMed 15601660. Source: MGI protein oligomerization Inferred from electronic annotation. Source: Compara 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: Compara regulation of tight junction assembly Inferred from electronic annotation. Source: Compara 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 pH Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara skeletal muscle tissue regeneration Inferred from direct assay PubMed 15601660. Source: MGI vascular transport Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 15084279. Source: MGI apical plasma membrane Inferred from direct assay PubMed 9620080. Source: MGI connexon complex Inferred from electronic annotation. Source: InterPro contractile fiber Inferred from direct assay PubMed 21708977. Source: MGI cytosol Inferred from direct assay PubMed 15331634. Source: MGI early endosome Inferred from electronic annotation. Source: Compara 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW 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: Compara membrane raft Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from electronic annotation. Source: Compara multivesicular body Inferred from electronic annotation. Source: Compara
Molecular_function	beta-tubulin binding Inferred from direct assay PubMed 15084279. Source: MGI gap junction channel activity Inferred from direct assay PubMed 11397787PubMed 15084279. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gjb3	P28231	2	EBI-298630,EBI-1767245
Gjc1	P28229	2	EBI-298630,EBI-1767271

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 382	381	Gap junction alpha-1 protein		PRO_0000057802
Regions
	Topological domain	2 – 13	12	Cytoplasmic Potential
	Transmembrane	14 – 36	23	Helical; Potential
	Topological domain	37 – 76	40	Extracellular Potential
	Transmembrane	77 – 99	23	Helical; Potential
	Topological domain	100 – 154	55	Cytoplasmic Potential
	Transmembrane	155 – 177	23	Helical; Potential
	Topological domain	178 – 208	31	Extracellular Potential
	Transmembrane	209 – 231	23	Helical; Potential
	Topological domain	232 – 382	151	Cytoplasmic Potential
Amino acid modifications
	Modified residue	247	1	Phosphotyrosine Ref.12
	Modified residue	255	1	Phosphoserine By similarity
	Modified residue	262	1	Phosphoserine By similarity
	Modified residue	271	1	S-nitrosocysteine Ref.15
	Modified residue	306	1	Phosphoserine Ref.13
	Modified residue	313	1	Phosphotyrosine Ref.12
	Modified residue	314	1	Phosphoserine Ref.13
	Modified residue	325	1	Phosphoserine; by CK1 By similarity
	Modified residue	326	1	Phosphothreonine Ref.13
	Modified residue	328	1	Phosphoserine; by CK1 Ref.13
	Modified residue	330	1	Phosphoserine; by CK1 Ref.13
	Modified residue	365	1	Phosphoserine By similarity
	Modified residue	368	1	Phosphoserine; by PKC/PRKCG By similarity
	Modified residue	369	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphoserine By similarity
	Disulfide bond	54 ↔ 192		By similarity
	Disulfide bond	187 ↔ 198		By similarity
	Cross-link	144		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	237		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Experimental info
	Sequence conflict	21	1	G → V in BAC26375. Ref.5
	Sequence conflict	320	1	M → T in AAA53027. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P23242 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 018DCB461FA69490	FASTA	382	43,004
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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 AND TYR-313, MASS SPECTROMETRY. Tissue: Brain.
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-314; THR-326; SER-328 AND SER-330, MASS SPECTROMETRY. Tissue: Brain cortex.
[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.
IPI	IPI00989666.
PIR	A39802.
RefSeq	NP_034418.1. NM_010288.3.
UniGene	Mm.378921.
3D structure databases
ProteinModelPortal	P23242.
SMR	P23242. Positions 3-234, 252-382.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29207N.
IntAct	P23242. 7 interactions.
MINT	MINT-1326689.
PTM databases
PhosphoSite	P23242.
Proteomic databases
PaxDb	P23242.
PRIDE	P23242.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
GeneID	14609.
KEGG	mmu:14609.
Organism-specific databases
CTD	2697.
MGI	MGI:95713. Gja1.
Phylogenomic databases
eggNOG	NOG45368.
GeneTree	ENSGT00700000104079.
HOVERGEN	HBG009576.
InParanoid	P23242.
KO	K07372.
OMA	GANVDMH.
OrthoDB	EOG402WSC.
Gene expression databases
ArrayExpress	P23242.
Bgee	P23242.
CleanEx	MM_GJA1.
Genevestigator	P23242.
GermOnline	ENSMUSG00000050953. Mus musculus.
Family and domain databases
InterPro	IPR000500. Connexin. IPR002261. Connexin43. IPR013124. Connexin43_C. IPR019570. Connexin_CCC. IPR017990. Connexin_CS. IPR013092. Connexin_N. [Graphical view]
PANTHER	PTHR11984. PTHR11984. 1 hit.
Pfam	PF00029. Connexin. 1 hit. PF03508. Connexin43. 1 hit. PF10582. Connexin_CCC. 1 hit. [Graphical view]
PRINTS	PR00206. CONNEXIN. PR01132. CONNEXINA1.
SMART	SM00037. CNX. 1 hit. SM01089. Connexin_CCC. 1 hit. [Graphical view]
PROSITE	PS00407. CONNEXINS_1. 1 hit. PS00408. CONNEXINS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GJA1. mouse.
NextBio	286404.
SOURCE	Search...

Entry information

Entry name

CXA1_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program