CXA1_MOUSE
ID CXA1_MOUSE Reviewed; 382 AA.
AC P23242; Q544I7; Q8CE05;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Gap junction alpha-1 protein;
DE AltName: Full=Connexin-43;
DE Short=Cx43;
DE AltName: Full=Gap junction 43 kDa heart protein;
GN Name=Gja1; Synonyms=Cxn-43;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1708769; DOI=10.1016/s0021-9258(18)92924-8;
RA Beyer E.C., Steinberg T.H.;
RT "Evidence that the gap junction protein connexin-43 is the ATP-induced pore
RT of mouse macrophages.";
RL J. Biol. Chem. 266:7971-7974(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Ovary;
RX PubMed=2060697; DOI=10.1016/0012-1606(91)90452-9;
RA Nishi M., Kumar N.M., Gilula N.B.;
RT "Developmental regulation of gap junction gene expression during mouse
RT embryonic development.";
RL Dev. Biol. 146:117-130(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=1318884; DOI=10.1083/jcb.117.6.1299;
RA Hennemann J., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E.,
RA Schwarz J., Nicholson B.J., Willecke K.;
RT "Molecular cloning and functional expression of mouse connexin40, a second
RT gap junction gene preferentially expressed in lung.";
RL J. Cell Biol. 117:1299-1310(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8395450; DOI=10.1016/0378-1119(93)90419-4;
RA Sullivan R., Ruangvoravat C., Joo D., Morgan J., Wang B.L., Wang X.K.,
RA Lo C.W.;
RT "Structure, sequence and expression of the mouse Cx43 gene encoding
RT connexin 43.";
RL Gene 130:191-199(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Head, Lung, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=2178193; DOI=10.1016/0022-2828(90)90061-6;
RA Fromaget C., el Aoumari A., Dupont E., Briand J.-P., Gros D.;
RT "Changes in the expression of connexin 43, a cardiac gap junctional
RT protein, during mouse heart development.";
RL J. Mol. Cell. Cardiol. 22:1245-1258(1990).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11741837; DOI=10.1093/hmg/10.25.2945;
RA Liu X.Z., Xia X.J., Adams J., Chen Z.Y., Welch K.O., Tekin M., Ouyang X.M.,
RA Kristiansen A., Pandya A., Balkany T., Arnos K.S., Nance W.E.;
RT "Mutations in GJA1 (connexin 43) are associated with non-syndromic
RT autosomal recessive deafness.";
RL Hum. Mol. Genet. 10:2945-2951(2001).
RN [11]
RP FUNCTION.
RX PubMed=15181016; DOI=10.1074/jbc.m404073200;
RA Gellhaus A., Dong X., Propson S., Maass K., Klein-Hitpass L., Kibschull M.,
RA Traub O., Willecke K., Perbal B., Lye S.J., Winterhager E.;
RT "Connexin43 interacts with NOV: a possible mechanism for negative
RT regulation of cell growth in choriocarcinoma cells.";
RL J. Biol. Chem. 279:36931-36942(2004).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=15213231; DOI=10.1074/jbc.m403952200;
RA Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
RT "CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
RT mechanism of connexin-mediated growth suppression.";
RL J. Biol. Chem. 279:36943-36950(2004).
RN [13]
RP INTERACTION WITH SGSM3.
RX PubMed=15709751; DOI=10.1021/bi048306w;
RA Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.;
RT "Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces
RT its degradation.";
RL Biochemistry 44:2385-2396(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4.
RX PubMed=18079109; DOI=10.1074/jbc.m709288200;
RA Li X., Su V., Kurata W.E., Jin C., Lau A.F.;
RT "A novel connexin43-interacting protein, CIP75, which belongs to the UbL-
RT UBA protein family, regulates the turnover of connexin43.";
RL J. Biol. Chem. 283:5748-5759(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275; SER-306; SER-314;
RP SER-325; THR-326; SER-328; SER-330; SER-341; SER-365; SER-368 AND SER-369,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [18]
RP INTERACTION WITH CNST.
RX PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D.,
RA Chavrier P., Meda P., Petit C.;
RT "Consortin, a trans-Golgi network cargo receptor for the plasma membrane
RT targeting and recycling of connexins.";
RL Hum. Mol. Genet. 19:262-275(2010).
RN [19]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4.
RX PubMed=20940304; DOI=10.1074/jbc.m110.170753;
RA Su V., Nakagawa R., Koval M., Lau A.F.;
RT "Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-
RT localized connexin43 mediated by CIP75.";
RL J. Biol. Chem. 285:40979-40990(2010).
RN [20]
RP S-NITROSYLATION AT CYS-271.
RX PubMed=21071693; DOI=10.1161/atvbaha.110.215939;
RA Straub A.C., Billaud M., Johnstone S.R., Best A.K., Yemen S., Dwyer S.T.,
RA Looft-Wilson R., Lysiak J.J., Gaston B., Palmer L., Isakson B.E.;
RT "Compartmentalized connexin 43 s-nitrosylation/denitrosylation regulates
RT heterocellular communication in the vessel wall.";
RL Arterioscler. Thromb. Vasc. Biol. 31:399-407(2011).
RN [21]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22549838; DOI=10.1038/ncomms1812;
RA Negoro H., Kanematsu A., Doi M., Suadicani S.O., Matsuo M., Imamura M.,
RA Okinami T., Nishikawa N., Oura T., Matsui S., Seo K., Tainaka M., Urabe S.,
RA Kiyokage E., Todo T., Okamura H., Tabata Y., Ogawa O.;
RT "Involvement of urinary bladder Connexin43 and the circadian clock in
RT coordination of diurnal micturition rhythm.";
RL Nat. Commun. 3:809-809(2012).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-368, AND INTERACTION
RP WITH TMEM65.
RX PubMed=26403541; DOI=10.1038/ncomms9391;
RA Sharma P., Abbasi C., Lazic S., Teng A.C., Wang D., Dubois N.,
RA Ignatchenko V., Wong V., Liu J., Araki T., Tiburcy M., Ackerley C.,
RA Zimmermann W.H., Hamilton R., Sun Y., Liu P.P., Keller G., Stagljar I.,
RA Scott I.C., Kislinger T., Gramolini A.O.;
RT "Evolutionarily conserved intercalated disc protein Tmem65 regulates
RT cardiac conduction and connexin 43 function.";
RL Nat. Commun. 6:8391-8391(2015).
RN [23]
RP ACETYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=28507509; DOI=10.3389/fncel.2017.00122;
RA Laguesse S., Close P., Van Hees L., Chariot A., Malgrange B., Nguyen L.;
RT "Loss of Elp3 impairs the acetylation and distribution of connexin-43 in
RT the developing cerebral cortex.";
RL Front. Cell. Neurosci. 11:122-122(2017).
CC -!- FUNCTION: Gap junction protein that acts as a regulator of bladder
CC capacity. A gap junction consists of a cluster of closely packed pairs
CC of transmembrane channels, the connexons, through which materials of
CC low MW diffuse from one cell to a neighboring cell. Negative regulator
CC of bladder functional capacity: acts by enhancing intercellular
CC electrical and chemical transmission, thus sensitizing bladder muscles
CC to cholinergic neural stimuli and causing them to contract. May play a
CC role in cell growth inhibition through the regulation of NOV expression
CC and localization (PubMed:15181016). Plays an essential role in gap
CC junction communication in the ventricles (PubMed:26403541).
CC {ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:22549838,
CC ECO:0000269|PubMed:26403541}.
CC -!- FUNCTION: Connexin 43 is possibly the ATP-induced pore of mouse
CC macrophages. {ECO:0000269|PubMed:22549838}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with CSNK1D (By similarity). Interacts with RIC1/CIP150 (By
CC similarity). Interacts (via C-terminus) with TJP1 (By similarity).
CC Interacts (via C-terminus) with SRC (via SH3 domain) (By similarity).
CC Interacts (not ubiquitinated) with UBQLN4 (via UBA domain). Interacts
CC with CNST. Interacts with SGSM3. Interacts with NOV (By similarity).
CC Interacts with TMEM65 (PubMed:26403541). {ECO:0000250|UniProtKB:P08050,
CC ECO:0000250|UniProtKB:P17302, ECO:0000269|PubMed:15709751,
CC ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:19864490,
CC ECO:0000269|PubMed:20940304, ECO:0000269|PubMed:26403541}.
CC -!- INTERACTION:
CC P23242; Q8CDJ3: Atg14; NbExp=2; IntAct=EBI-298630, EBI-3506699;
CC P23242; Q8C0J2: Atg16l1; NbExp=2; IntAct=EBI-298630, EBI-769195;
CC P23242; Q7TT37: Elp1; NbExp=3; IntAct=EBI-298630, EBI-8418161;
CC P23242; P28231: Gjb3; NbExp=2; IntAct=EBI-298630, EBI-1767245;
CC P23242; P28229: Gjc1; NbExp=2; IntAct=EBI-298630, EBI-1767271;
CC P23242; Q6NZM9: Hdac4; NbExp=2; IntAct=EBI-298630, EBI-646397;
CC P23242; Q9Z2V6: Hdac5; NbExp=2; IntAct=EBI-298630, EBI-645339;
CC P23242; Q6PF93: Pik3c3; NbExp=4; IntAct=EBI-298630, EBI-6678149;
CC P23242; Q8VD65: Pik3r4; NbExp=3; IntAct=EBI-298630, EBI-6678184;
CC P23242; P28867: Prkcd; NbExp=4; IntAct=EBI-298630, EBI-1551324;
CC P23242; P16054: Prkce; NbExp=3; IntAct=EBI-298630, EBI-298451;
CC P23242; P05480: Src; NbExp=3; IntAct=EBI-298630, EBI-298680;
CC P23242; P39447: Tjp1; NbExp=4; IntAct=EBI-298630, EBI-79508;
CC P23242; P68254: Ywhaq; NbExp=3; IntAct=EBI-298630, EBI-400675;
CC P23242; Q63664: Kcnj8; Xeno; NbExp=4; IntAct=EBI-298630, EBI-6991142;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26403541,
CC ECO:0000269|PubMed:28507509}; Multi-pass membrane protein
CC {ECO:0000255}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}.
CC Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and
CC proper localization at ICD is dependent on TMEM65.
CC {ECO:0000269|PubMed:26403541}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, non-sensory epithelial cells,
CC and in fibrocytes of the spiral ligament and the spiral limbus.
CC Expressed in bladder smooth muscle cells (at protein level). Expressed
CC in astrocytes (at protein level) (PubMed:15213231).
CC {ECO:0000269|PubMed:11741837, ECO:0000269|PubMed:15213231,
CC ECO:0000269|PubMed:2178193, ECO:0000269|PubMed:22549838}.
CC -!- DEVELOPMENTAL STAGE: At 7.5 dpc, expressed in the embryo, but not in
CC the extraembryonic region containing the ectoplacental cone.
CC {ECO:0000269|PubMed:8395450}.
CC -!- INDUCTION: In bladder smooth muscle cells, exhibits night/day
CC variations with low levels during the sleep phase, at circadian time
CC (CT) 4-12 (at protein level). Down-regulation during the night allows
CC increase in bladder capacity, avoiding disturbance of sleep by
CC micturition. Expression starts to increase around CT12 and forms a
CC plateau during the active phase (CT16-24) (at protein level). Circadian
CC transcription is activated by NR1D1. Up-regulated by SP1 and SP3.
CC {ECO:0000269|PubMed:22549838}.
CC -!- PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates
CC gap junction assembly. Phosphorylated at Ser-368 by PRKCG;
CC phosphorylation induces disassembly of gap junction plaques and
CC inhibition of gap junction activity. Phosphorylation at Ser-368 by
CC PRKCD triggers its internalization into small vesicles leading to
CC proteasome-mediated degradation (By similarity).
CC {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302,
CC ECO:0000250|UniProtKB:Q6TYA7}.
CC -!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the
CC level of functional Cx43 gap junctions at the plasma membrane. May be
CC desumoylated by SENP1 or SENP2 (By similarity).
CC {ECO:0000250|UniProtKB:P17302}.
CC -!- PTM: Acetylated in the developing cortex; leading to delocalization
CC from the cell membrane. {ECO:0000269|PubMed:28507509}.
CC -!- PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial
CC gap junction in arteries, it augments channel permeability and may
CC regulate of smooth muscle cell to endothelial cell communication.
CC {ECO:0000269|PubMed:21071693}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice die shortly after birth.
CC {ECO:0000269|PubMed:22549838}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; M61896; AAA37444.1; -; Genomic_DNA.
DR EMBL; M63801; AAA53027.1; -; mRNA.
DR EMBL; X62836; CAA44640.1; -; Genomic_DNA.
DR EMBL; X61576; CAA43778.1; -; mRNA.
DR EMBL; AK029291; BAC26375.1; -; mRNA.
DR EMBL; AK036979; BAC29656.1; -; mRNA.
DR EMBL; AK145692; BAE26592.1; -; mRNA.
DR EMBL; AK165986; BAE38502.1; -; mRNA.
DR EMBL; CT010327; CAJ18535.1; -; mRNA.
DR EMBL; CH466540; EDL05108.1; -; Genomic_DNA.
DR EMBL; BC006894; AAH06894.1; -; mRNA.
DR CCDS; CCDS23851.1; -.
DR PIR; A39802; A39802.
DR RefSeq; NP_034418.1; NM_010288.3.
DR AlphaFoldDB; P23242; -.
DR BMRB; P23242; -.
DR SMR; P23242; -.
DR BioGRID; 199923; 22.
DR DIP; DIP-29207N; -.
DR IntAct; P23242; 32.
DR MINT; P23242; -.
DR STRING; 10090.ENSMUSP00000064536; -.
DR iPTMnet; P23242; -.
DR PhosphoSitePlus; P23242; -.
DR jPOST; P23242; -.
DR PaxDb; P23242; -.
DR PeptideAtlas; P23242; -.
DR PRIDE; P23242; -.
DR ProteomicsDB; 285405; -.
DR DNASU; 14609; -.
DR Ensembl; ENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
DR Ensembl; ENSMUST00000220069; ENSMUSP00000151620; ENSMUSG00000050953.
DR GeneID; 14609; -.
DR KEGG; mmu:14609; -.
DR UCSC; uc007fcc.2; mouse.
DR CTD; 2697; -.
DR MGI; MGI:95713; Gja1.
DR VEuPathDB; HostDB:ENSMUSG00000050953; -.
DR eggNOG; ENOG502QRAE; Eukaryota.
DR GeneTree; ENSGT01050000244914; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; P23242; -.
DR OMA; LIQWYMY; -.
DR OrthoDB; 823525at2759; -.
DR PhylomeDB; P23242; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-191650; Regulation of gap junction activity.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 14609; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Gja1; mouse.
DR PRO; PR:P23242; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P23242; protein.
DR Bgee; ENSMUSG00000050953; Expressed in ciliary body and 345 other tissues.
DR ExpressionAtlas; P23242; baseline and differential.
DR Genevisible; P23242; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070160; C:tight junction; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR GO; GO:0071253; F:connexin binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
DR GO; GO:0086075; F:gap junction channel activity involved in cardiac conduction electrical coupling; TAS:UniProtKB.
DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:MGI.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015075; F:ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:CAFA.
DR GO; GO:0097110; F:scaffold protein binding; IPI:CAFA.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0007512; P:adult heart development; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0015867; P:ATP transport; ISO:MGI.
DR GO; GO:0003294; P:atrial ventricular junction remodeling; IGI:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:0046849; P:bone remodeling; IMP:UniProtKB.
DR GO; GO:0061337; P:cardiac conduction; IMP:MGI.
DR GO; GO:0007154; P:cell communication; ISO:MGI.
DR GO; GO:0010643; P:cell communication by chemical coupling; IDA:MGI.
DR GO; GO:0010644; P:cell communication by electrical coupling; IDA:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0071467; P:cellular response to pH; IDA:CAFA.
DR GO; GO:0002544; P:chronic inflammatory response; ISO:MGI.
DR GO; GO:0002069; P:columnar/cuboidal epithelial cell maturation; IMP:MGI.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0003158; P:endothelium development; IEA:Ensembl.
DR GO; GO:0003347; P:epicardial cell to mesenchymal cell transition; TAS:DFLAT.
DR GO; GO:1905867; P:epididymis development; IEA:Ensembl.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; TAS:DFLAT.
DR GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0014047; P:glutamate secretion; IMP:ARUK-UCL.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISO:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
DR GO; GO:0099111; P:microtubule-based transport; ISS:UniProtKB.
DR GO; GO:0060156; P:milk ejection reflex; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:0097402; P:neuroblast migration; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISO:MGI.
DR GO; GO:0010652; P:positive regulation of cell communication by chemical coupling; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0003104; P:positive regulation of glomerular filtration; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0045844; P:positive regulation of striated muscle tissue development; IMP:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:MGI.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0060312; P:regulation of blood vessel remodeling; TAS:DFLAT.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
DR GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0010649; P:regulation of cell communication by electrical coupling; ISO:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:MGI.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IMP:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:0010232; P:vascular transport; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR GO; GO:0042908; P:xenobiotic transport; IMP:ARUK-UCL.
DR Gene3D; 1.20.1440.80; -; 1.
DR Gene3D; 1.20.5.1130; -; 1.
DR InterPro; IPR035091; Alpha_helix_dom_sf.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002261; Connexin43.
DR InterPro; IPR013124; Connexin43_C.
DR InterPro; IPR034634; Connexin_C.
DR InterPro; IPR019570; Connexin_CCC.
DR InterPro; IPR017990; Connexin_CS.
DR InterPro; IPR013092; Connexin_N.
DR InterPro; IPR038359; Connexin_N_sf.
DR PANTHER; PTHR11984; PTHR11984; 1.
DR PANTHER; PTHR11984:SF33; PTHR11984:SF33; 1.
DR Pfam; PF00029; Connexin; 1.
DR Pfam; PF03508; Connexin43; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01132; CONNEXINA1.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR SUPFAM; SSF118220; SSF118220; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Gap junction; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT CHAIN 2..382
FT /note="Gap junction alpha-1 protein"
FT /id="PRO_0000057802"
FT TOPO_DOM 2..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..76
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..207
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT REGION 244..382
FT /note="Interaction with NOV"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT REGION 264..382
FT /note="Interaction with UBQLN4"
FT /evidence="ECO:0000269|PubMed:18079109"
FT REGION 317..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT MOD_RES 247
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT MOD_RES 271
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:21071693"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine; by PKC/PRKCG and PKC/PRKCD"
FT /evidence="ECO:0000269|PubMed:26403541,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT DISULFID 54..192
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT DISULFID 187..198
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT CONFLICT 21
FT /note="G -> V (in Ref. 5; BAC26375)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="M -> T (in Ref. 3; AAA53027)"
FT /evidence="ECO:0000305"
SQ 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
