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Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein)

 CXA1_MOUSE              Reviewed;         382 AA.
P23242; Q544I7; Q8CE05;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 189.
RecName: Full=Gap junction alpha-1 protein;
AltName: Full=Connexin-43;
Short=Cx43;
AltName: Full=Gap junction 43 kDa heart protein;
Name=Gja1; Synonyms=Cxn-43;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1708769;
Beyer E.C., Steinberg T.H.;
"Evidence that the gap junction protein connexin-43 is the ATP-induced
pore of mouse macrophages.";
J. Biol. Chem. 266:7971-7974(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1; TISSUE=Ovary;
PubMed=2060697; DOI=10.1016/0012-1606(91)90452-9;
Nishi M., Kumar N.M., Gilula N.B.;
"Developmental regulation of gap junction gene expression during mouse
embryonic development.";
Dev. Biol. 146:117-130(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=1318884; DOI=10.1083/jcb.117.6.1299;
Hennemann J., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E.,
Schwarz J., Nicholson B.J., Willecke K.;
"Molecular cloning and functional expression of mouse connexin40, a
second gap junction gene preferentially expressed in lung.";
J. Cell Biol. 117:1299-1310(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
TISSUE=Embryo;
PubMed=8395450; DOI=10.1016/0378-1119(93)90419-4;
Sullivan R., Ruangvoravat C., Joo D., Morgan J., Wang B.L., Wang X.K.,
Lo C.W.;
"Structure, sequence and expression of the mouse Cx43 gene encoding
connexin 43.";
Gene 130:191-199(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Blastocyst, Head, Lung, and Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
TISSUE SPECIFICITY.
PubMed=2178193; DOI=10.1016/0022-2828(90)90061-6;
Fromaget C., el Aoumari A., Dupont E., Briand J.-P., Gros D.;
"Changes in the expression of connexin 43, a cardiac gap junctional
protein, during mouse heart development.";
J. Mol. Cell. Cardiol. 22:1245-1258(1990).
[10]
TISSUE SPECIFICITY.
PubMed=11741837; DOI=10.1093/hmg/10.25.2945;
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.;
"Mutations in GJA1 (connexin 43) are associated with non-syndromic
autosomal recessive deafness.";
Hum. Mol. Genet. 10:2945-2951(2001).
[11]
FUNCTION.
PubMed=15181016; DOI=10.1074/jbc.M404073200;
Gellhaus A., Dong X., Propson S., Maass K., Klein-Hitpass L.,
Kibschull M., Traub O., Willecke K., Perbal B., Lye S.J.,
Winterhager E.;
"Connexin43 interacts with NOV: a possible mechanism for negative
regulation of cell growth in choriocarcinoma cells.";
J. Biol. Chem. 279:36931-36942(2004).
[12]
TISSUE SPECIFICITY.
PubMed=15213231; DOI=10.1074/jbc.M403952200;
Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
"CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
mechanism of connexin-mediated growth suppression.";
J. Biol. Chem. 279:36943-36950(2004).
[13]
INTERACTION WITH SGSM3.
PubMed=15709751; DOI=10.1021/bi048306w;
Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.;
"Novel rab GAP-like protein, CIP85, interacts with connexin43 and
induces its degradation.";
Biochemistry 44:2385-2396(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
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.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4.
PubMed=18079109; DOI=10.1074/jbc.M709288200;
Li X., Su V., Kurata W.E., Jin C., Lau A.F.;
"A novel connexin43-interacting protein, CIP75, which belongs to the
UbL-UBA protein family, regulates the turnover of connexin43.";
J. Biol. Chem. 283:5748-5759(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275; SER-306; SER-314;
SER-325; THR-326; SER-328; SER-330; SER-341; SER-365; SER-368 AND
SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
INTERACTION WITH CNST.
PubMed=19864490; DOI=10.1093/hmg/ddp490;
del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D.,
Lampe P.D., Chavrier P., Meda P., Petit C.;
"Consortin, a trans-Golgi network cargo receptor for the plasma
membrane targeting and recycling of connexins.";
Hum. Mol. Genet. 19:262-275(2010).
[19]
SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4.
PubMed=20940304; DOI=10.1074/jbc.M110.170753;
Su V., Nakagawa R., Koval M., Lau A.F.;
"Ubiquitin-independent proteasomal degradation of endoplasmic
reticulum-localized connexin43 mediated by CIP75.";
J. Biol. Chem. 285:40979-40990(2010).
[20]
S-NITROSYLATION AT CYS-271.
PubMed=21071693; DOI=10.1161/ATVBAHA.110.215939;
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.;
"Compartmentalized connexin 43 s-nitrosylation/denitrosylation
regulates heterocellular communication in the vessel wall.";
Arterioscler. Thromb. Vasc. Biol. 31:399-407(2011).
[21]
FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=22549838; DOI=10.1038/ncomms1812;
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.;
"Involvement of urinary bladder Connexin43 and the circadian clock in
coordination of diurnal micturition rhythm.";
Nat. Commun. 3:809-809(2012).
[22]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-368, AND
INTERACTION WITH TMEM65.
PubMed=26403541; DOI=10.1038/ncomms9391;
Sharma P., Abbasi C., Lazic S., Teng A.C., Wang D., Dubois N.,
Ignatchenko V., Wong V., Liu J., Araki T., Tiburcy M., Ackerley C.,
Zimmermann W.H., Hamilton R., Sun Y., Liu P.P., Keller G.,
Stagljar I., Scott I.C., Kislinger T., Gramolini A.O.;
"Evolutionarily conserved intercalated disc protein Tmem65 regulates
cardiac conduction and connexin 43 function.";
Nat. Commun. 6:8391-8391(2015).
-!- 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. 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 (PubMed:26403541).
{ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:22549838,
ECO:0000269|PubMed:26403541}.
-!- FUNCTION: Connexin 43 is possibly the ATP-induced pore of mouse
macrophages. {ECO:0000269|PubMed:22549838}.
-!- SUBUNIT: A connexon is composed of a hexamer of connexins.
Interacts with CSNK1D (By similarity). Interacts with RIC1/CIP150
(By similarity). Interacts (via C-terminus) with TJP1 (By
similarity). Interacts (via C-terminus) with SRC (via SH3 domain)
(By similarity). Interacts (not ubiquitinated) with UBQLN4 (via
UBA domain). Interacts with CNST. Interacts with SGSM3. Interacts
with NOV (By similarity). Interacts with TMEM65 (PubMed:26403541).
{ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302,
ECO:0000269|PubMed:15709751, ECO:0000269|PubMed:18079109,
ECO:0000269|PubMed:19864490, ECO:0000269|PubMed:20940304,
ECO:0000269|PubMed:26403541}.
-!- INTERACTION:
Q8CDJ3:Atg14; NbExp=2; IntAct=EBI-298630, EBI-3506699;
Q8C0J2:Atg16l1; NbExp=2; IntAct=EBI-298630, EBI-769195;
P28231:Gjb3; NbExp=2; IntAct=EBI-298630, EBI-1767245;
P28229:Gjc1; NbExp=2; IntAct=EBI-298630, EBI-1767271;
Q6NZM9:Hdac4; NbExp=2; IntAct=EBI-298630, EBI-646397;
Q9Z2V6:Hdac5; NbExp=2; IntAct=EBI-298630, EBI-645339;
Q63664:Kcnj8 (xeno); NbExp=4; IntAct=EBI-298630, EBI-6991142;
Q6PF93:Pik3c3; NbExp=4; IntAct=EBI-298630, EBI-6678149;
Q8VD65:Pik3r4; NbExp=3; IntAct=EBI-298630, EBI-6678184;
P28867:Prkcd; NbExp=4; IntAct=EBI-298630, EBI-1551324;
P16054:Prkce; NbExp=3; IntAct=EBI-298630, EBI-298451;
P05480:Src; NbExp=3; IntAct=EBI-298630, EBI-298680;
P39447:Tjp1; NbExp=4; IntAct=EBI-298630, EBI-79508;
P68254:Ywhaq; NbExp=3; IntAct=EBI-298630, EBI-400675;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26403541};
Multi-pass membrane protein {ECO:0000255}. Cell junction, gap
junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum
{ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}.
Note=Localizes at the intercalated disk (ICD) in cardiomyocytes
and proper localization at ICD is dependent on TMEM65.
{ECO:0000269|PubMed:26403541}.
-!- 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). Expressed in astrocytes (at protein level)
(PubMed:15213231). {ECO:0000269|PubMed:11741837,
ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:2178193,
ECO:0000269|PubMed:22549838}.
-!- DEVELOPMENTAL STAGE: At 7.5 dpc, expressed in the embryo, but not
in the extraembryonic region containing the ectoplacental cone.
{ECO:0000269|PubMed:8395450}.
-!- 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). Down-regulation 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. {ECO:0000269|PubMed:22549838}.
-!- 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. Phosphorylation at Ser-
368 by PRKCD triggers its internalization into small vesicles
leading to proteasome-mediated degradation (By similarity).
{ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302,
ECO:0000250|UniProtKB:Q6TYA7}.
-!- 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}.
-!- 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:0000269|PubMed:21071693}.
-!- DISRUPTION PHENOTYPE: Mutant mice die shortly after birth.
{ECO:0000269|PubMed:22549838}.
-!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
subfamily. {ECO:0000305}.
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EMBL; M61896; AAA37444.1; -; Genomic_DNA.
EMBL; M63801; AAA53027.1; -; mRNA.
EMBL; X62836; CAA44640.1; -; Genomic_DNA.
EMBL; X61576; CAA43778.1; -; mRNA.
EMBL; AK029291; BAC26375.1; -; mRNA.
EMBL; AK036979; BAC29656.1; -; mRNA.
EMBL; AK145692; BAE26592.1; -; mRNA.
EMBL; AK165986; BAE38502.1; -; mRNA.
EMBL; CT010327; CAJ18535.1; -; mRNA.
EMBL; CH466540; EDL05108.1; -; Genomic_DNA.
EMBL; BC006894; AAH06894.1; -; mRNA.
CCDS; CCDS23851.1; -.
PIR; A39802; A39802.
RefSeq; NP_034418.1; NM_010288.3.
UniGene; Mm.378921; -.
ProteinModelPortal; P23242; -.
SMR; P23242; -.
BioGrid; 199923; 11.
DIP; DIP-29207N; -.
IntAct; P23242; 29.
MINT; MINT-1326689; -.
STRING; 10090.ENSMUSP00000064536; -.
iPTMnet; P23242; -.
PhosphoSitePlus; P23242; -.
PaxDb; P23242; -.
PeptideAtlas; P23242; -.
PRIDE; P23242; -.
Ensembl; ENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
Ensembl; ENSMUST00000220069; ENSMUSP00000151620; ENSMUSG00000050953.
GeneID; 14609; -.
KEGG; mmu:14609; -.
UCSC; uc007fcc.2; mouse.
CTD; 2697; -.
MGI; MGI:95713; Gja1.
eggNOG; ENOG410IF97; Eukaryota.
eggNOG; ENOG4110JTW; LUCA.
GeneTree; ENSGT00900000140773; -.
HOVERGEN; HBG009576; -.
InParanoid; P23242; -.
KO; K07372; -.
OMA; GANVDMH; -.
OrthoDB; EOG091G0FKH; -.
PhylomeDB; P23242; -.
TreeFam; TF329606; -.
Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-MMU-190861; Gap junction assembly.
Reactome; R-MMU-190873; Gap junction degradation.
Reactome; R-MMU-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-MMU-196025; Formation of annular gap junctions.
ChiTaRS; Gja1; mouse.
PRO; PR:P23242; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000050953; -.
CleanEx; MM_GJA1; -.
Genevisible; P23242; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005922; C:connexin complex; IEA:Ensembl.
GO; GO:0043292; C:contractile fiber; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005916; C:fascia adherens; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005921; C:gap junction; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
GO; GO:0071253; F:connexin binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
GO; GO:0086075; F:gap junction channel activity involved in cardiac conduction electrical coupling; TAS:UniProtKB.
GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:MGI.
GO; GO:0015075; F:ion transmembrane transporter activity; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:CAFA.
GO; GO:0005102; F:receptor binding; IPI:MGI.
GO; GO:0097110; F:scaffold protein binding; IPI:CAFA.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; ISO:MGI.
GO; GO:0007512; P:adult heart development; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0015867; P:ATP transport; IEA:Ensembl.
GO; GO:0003294; P:atrial ventricular junction remodeling; IGI:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0061337; P:cardiac conduction; IMP:MGI.
GO; GO:0010643; P:cell communication by chemical coupling; IDA:MGI.
GO; GO:0010644; P:cell communication by electrical coupling; IDA:MGI.
GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0071467; P:cellular response to pH; IDA:CAFA.
GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
GO; GO:0003158; P:endothelium development; IEA:Ensembl.
GO; GO:0003347; P:epicardial cell to mesenchymal cell transition; TAS:DFLAT.
GO; GO:1905867; P:epididymis development; IEA:Ensembl.
GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
GO; GO:0090162; P:establishment of epithelial cell polarity; TAS:DFLAT.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
GO; GO:0060156; P:milk ejection reflex; IMP:MGI.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
GO; GO:2000987; P:positive regulation of behavioral fear response; IEA:Ensembl.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0010652; P:positive regulation of cell communication by chemical coupling; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0003104; P:positive regulation of glomerular filtration; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0045844; P:positive regulation of striated muscle tissue development; IMP:MGI.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; IEA:Ensembl.
GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:MGI.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0060312; P:regulation of blood vessel remodeling; TAS:DFLAT.
GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IMP:MGI.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:MGI.
GO; GO:0010232; P:vascular transport; IEA:Ensembl.
Gene3D; 1.20.5.1130; -; 1.
InterPro; IPR035091; Alpha_helix_domain.
InterPro; IPR000500; Connexin.
InterPro; IPR002261; Connexin43.
InterPro; IPR013124; Connexin43_C.
InterPro; IPR034634; Connexin_C.
InterPro; IPR019570; Connexin_CCC.
InterPro; IPR017990; Connexin_CS.
InterPro; IPR013092; Connexin_N.
PANTHER; PTHR11984; PTHR11984; 1.
PANTHER; PTHR11984:SF33; PTHR11984:SF33; 1.
Pfam; PF00029; Connexin; 1.
Pfam; PF03508; Connexin43; 1.
PRINTS; PR00206; CONNEXIN.
PRINTS; PR01132; CONNEXINA1.
SMART; SM00037; CNX; 1.
SMART; SM01089; Connexin_CCC; 1.
SUPFAM; SSF118220; SSF118220; 1.
PROSITE; PS00407; CONNEXINS_1; 1.
PROSITE; PS00408; CONNEXINS_2; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Gap junction; Isopeptide bond; Membrane;
Phosphoprotein; Reference proteome; S-nitrosylation; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 382 Gap junction alpha-1 protein.
/FTId=PRO_0000057802.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 36 Helical. {ECO:0000255}.
TOPO_DOM 37 76 Extracellular. {ECO:0000255}.
TRANSMEM 77 99 Helical. {ECO:0000255}.
TOPO_DOM 100 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 177 Helical. {ECO:0000255}.
TOPO_DOM 178 208 Extracellular. {ECO:0000255}.
TRANSMEM 209 231 Helical. {ECO:0000255}.
TOPO_DOM 232 382 Cytoplasmic. {ECO:0000255}.
REGION 244 382 Interaction with NOV.
{ECO:0000250|UniProtKB:P08050}.
REGION 264 382 Interaction with UBQLN4.
{ECO:0000269|PubMed:18079109}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P08050}.
MOD_RES 247 247 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:P17302}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000250|UniProtKB:P08050}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:P17302}.
MOD_RES 271 271 S-nitrosocysteine.
{ECO:0000269|PubMed:21071693}.
MOD_RES 275 275 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 326 326 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 368 368 Phosphoserine; by PKC/PRKCG and
PKC/PRKCD. {ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:26403541}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:P08050}.
DISULFID 54 192 {ECO:0000250}.
DISULFID 187 198 {ECO:0000250}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CONFLICT 21 21 G -> V (in Ref. 5; BAC26375).
{ECO:0000305}.
CONFLICT 320 320 M -> T (in Ref. 3; AAA53027).
{ECO:0000305}.
SEQUENCE 382 AA; 43004 MW; 018DCB461FA69490 CRC64;
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
KGRSDPYHAT TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD SQNAKKVAAG HELQPLAIVD
QRPSSRASSR ASSRPRPDDL EI


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