ID CXA1_HUMAN Reviewed; 382 AA.
AC P17302; B2R5U9; Q6FHU1; Q9Y5I8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 260.
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=GJAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=1696265; DOI=10.1083/jcb.111.2.589;
RA Fishman G.I., Spray D.C., Leinwand L.A.;
RT "Molecular characterization and functional expression of the human cardiac
RT gap junction channel.";
RL J. Cell Biol. 111:589-598(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1646158; DOI=10.1016/0888-7543(91)90507-b;
RA Fishman G.I., Eddy R.L., Shows T.B., Rosenthal L., Leinwand L.A.;
RT "The human connexin gene family of gap junction proteins: distinct
RT chromosomal locations but similar structures.";
RL Genomics 10:250-256(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10581143; DOI=10.1053/euhj.1999.1718;
RA Haefliger J.-A., Goy J.J., Waeber G.;
RT "Sporadic cases of dilated cardiomyopathies associated with
RT atrioventricular conduction defects are not linked to mutation within the
RT connexins 40 and 43 genes.";
RL Eur. Heart J. 20:1843-1843(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 DISULFIDE BONDS.
RX PubMed=9430691; DOI=10.1074/jbc.273.3.1519;
RA Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M.;
RT "Intercellular calcium signaling via gap junction in connexin-43-
RT transfected cells.";
RL J. Biol. Chem. 273:1519-1528(1998).
RN [10]
RP INTERACTION WITH NOV.
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 [11]
RP INTERACTION WITH NOV.
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 [12]
RP PHOSPHORYLATION AT SER-262.
RX PubMed=14702389; DOI=10.1242/jcs.00889;
RA Doble B.W., Dang X., Ping P., Fandrich R.R., Nickel B.E., Jin Y.,
RA Cattini P.A., Kardami E.;
RT "Phosphorylation of serine 262 in the gap junction protein connexin-43
RT regulates DNA synthesis in cell-cell contact forming cardiomyocytes.";
RL J. Cell Sci. 117:507-514(2004).
RN [13]
RP REVIEW.
RX PubMed=10764404; DOI=10.1161/01.res.86.7.723;
RA Saffitz J.E., Laing J.G., Yamada K.A.;
RT "Connexin expression and turnover: implications for cardiac excitability.";
RL Circ. Res. 86:723-728(2000).
RN [14]
RP SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
RX PubMed=8873667; DOI=10.1161/01.cir.94.8.1909;
RA Gebbia M., Towbin J.A., Casey B.;
RT "Failure to detect connexin43 mutations in 38 cases of sporadic and
RT familial heterotaxy.";
RL Circulation 94:1909-1912(1996).
RN [15]
RP SHOWS THAT HEART LATERALIZATION DEFECTS ARE NOT DUE TO GJA1.
RX PubMed=9155619; DOI=10.1136/hrt.77.4.369;
RA Penman Splitt M., Tsai M.Y., Burn J., Goodship J.A.;
RT "Absence of mutations in the regulatory domain of the gap junction protein
RT connexin 43 in patients with visceroatrial heterotaxy.";
RL Heart 77:369-370(1997).
RN [16]
RP SHOWS THAT HEART LATERALIZATION DEFECTS ARE NOT DUE TO GJA1.
RX PubMed=9443444; DOI=10.1161/01.cir.97.1.117;
RA Toth T., Hajdu J., Marton T., Nagy B., Papp Z.;
RT "Connexin43 gene mutations and heterotaxy.";
RL Circulation 97:117-118(1998).
RN [17]
RP ASSOCIATION WITH NON-SYNDROMIC AUTOSOMAL RECESSIVE DEAFNESS, AND TISSUE
RP 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 [18]
RP PHOSPHORYLATION AT SER-325; SER-328 AND SER-330 BY CSNK1D/CK1, AND
RP INTERACTION WITH CSNK1D.
RX PubMed=12270943; DOI=10.1074/jbc.m209427200;
RA Cooper C.D., Lampe P.D.;
RT "Casein kinase 1 regulates connexin-43 gap junction assembly.";
RL J. Biol. Chem. 277:44962-44968(2002).
RN [19]
RP INTERACTION WITH RIC1.
RX PubMed=16112082; DOI=10.1016/j.bbrc.2005.08.019;
RA Akiyama M., Ishida N., Ogawa T., Yogo K., Takeya T.;
RT "Molecular cloning and functional analysis of a novel Cx43 partner protein
RT CIP150.";
RL Biochem. Biophys. Res. Commun. 335:1264-1271(2005).
RN [20]
RP PHOSPHORYLATION AT SER-255 AND SER-262.
RX PubMed=15605363; DOI=10.1002/mc.20072;
RA Arnold J.M., Phipps M.W., Chen J., Phipps J.;
RT "Cellular sublocalization of Cx43 and the establishment of functional
RT coupling in IMR-32 neuroblastoma cells.";
RL Mol. Carcinog. 42:159-169(2005).
RN [21]
RP INVOLVEMENT IN ODDD-AR.
RX PubMed=16816024; DOI=10.1136/jmg.2005.037655;
RA Richardson R.J., Joss S., Tomkin S., Ahmed M., Sheridan E., Dixon M.J.;
RT "A nonsense mutation in the first transmembrane domain of connexin 43
RT underlies autosomal recessive oculodentodigital syndrome.";
RL J. Med. Genet. 43:E37-E37(2006).
RN [22]
RP NON-ASSOCIATION WITH NON-SYNDROMIC AUTOSOMAL RECESSIVE DEAFNESS, VARIANTS
RP ODDD SER-17; PRO-18; ARG-21; GLU-22; THR-23; VAL-40; LYS-49; PHE-52 INS;
RP SER-76; VAL-90; CYS-98; ASN-102; THR-130; GLU-134; ARG-138; HIS-202 AND
RP LEU-216, AND VARIANT VAL-253.
RX PubMed=12457340; DOI=10.1086/346090;
RA Paznekas W.A., Boyadjiev S.A., Shapiro R.E., Daniels O., Wollnik B.,
RA Keegan C.E., Innis J.W., Dinulos M.B., Christian C., Hannibal M.C.,
RA Jabs E.W.;
RT "Connexin 43 (GJA1) mutations cause the pleiotropic phenotype of
RT oculodentodigital dysplasia.";
RL Am. J. Hum. Genet. 72:408-418(2003).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-314 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP SUMOYLATION AT LYS-144 AND LYS-237, AND SUBCELLULAR LOCATION.
RX PubMed=22411987; DOI=10.1074/jbc.m111.281832;
RA Kjenseth A., Fykerud T.A., Sirnes S., Bruun J., Yohannes Z., Kolberg M.,
RA Omori Y., Rivedal E., Leithe E.;
RT "The gap junction channel protein connexin 43 is covalently modified and
RT regulated by SUMOylation.";
RL J. Biol. Chem. 287:15851-15861(2012).
RN [25]
RP INVOLVEMENT IN PPKCA1, VARIANT PPKCA1 VAL-8, AND CHARACTERIZATION OF
RP VARIANT PPKCA1 VAL-8.
RX PubMed=25168385; DOI=10.1093/hmg/ddu442;
RA Wang H., Cao X., Lin Z., Lee M., Jia X., Ren Y., Dai L., Guan L., Zhang J.,
RA Lin X., Zhang J., Chen Q., Feng C., Zhou E.Y., Yin J., Xu G., Yang Y.;
RT "Exome sequencing reveals mutation in GJA1 as a cause of keratoderma-
RT hypotrichosis-leukonychia totalis syndrome.";
RL Hum. Mol. Genet. 24:243-250(2015).
RN [26]
RP INVOLVEMENT IN EKVP3, VARIANTS EKVP3 VAL-44 AND ASP-227, CHARACTERIZATION
RP OF VARIANTS EKVP3 VAL-44 AND ASP-227, AND SUBCELLULAR LOCATION.
RX PubMed=25398053; DOI=10.1038/jid.2014.485;
RG Yale Center for Mendelian Genomics;
RA Boyden L.M., Craiglow B.G., Zhou J., Hu R., Loring E.C., Morel K.D.,
RA Lauren C.T., Lifton R.P., Bilguvar K., Paller A.S., Choate K.A.;
RT "Dominant de novo mutations in GJA1 cause erythrokeratodermia variabilis et
RT progressiva, without features of oculodentodigital dysplasia.";
RL J. Invest. Dermatol. 135:1540-1547(2015).
RN [27]
RP VARIANTS HEART MALFORMATIONS GLY-352; PRO-364 AND ASN-365, VARIANTS ALA-326
RP AND GLY-373, AND CHARACTERIZATION OF VARIANT HEART MALFORMATIONS PRO-364.
RX PubMed=7715640; DOI=10.1056/nejm199505183322002;
RA Britz-Cunningham S.H., Shah M.M., Zuppan C.W., Fletcher W.H.;
RT "Mutations of the connexin43 gap-junction gene in patients with heart
RT malformations and defects of laterality.";
RL N. Engl. J. Med. 332:1323-1329(1995).
RN [28]
RP VARIANTS HLHS1 GLN-362 AND GLN-376, AND CHARACTERIZATION OF VARIANTS HLHS1
RP GLN-362 AND GLN-376.
RX PubMed=11470490; DOI=10.1016/s0027-5107(01)00160-9;
RA Dasgupta C., Martinez A.-M., Zuppan C.W., Shah M.M., Bailey L.L.,
RA Fletcher W.H.;
RT "Identification of connexin43 (alpha1) gap junction gene mutations in
RT patients with hypoplastic left heart syndrome by denaturing gradient gel
RT electrophoresis (DGGE).";
RL Mutat. Res. 479:173-186(2001).
RN [29]
RP VARIANT ODDD MET-96.
RX PubMed=15108203; DOI=10.1002/ajmg.a.20614;
RA Kjaer K.W., Hansen L., Eiberg H., Leicht P., Opitz J.M., Tommerup N.;
RT "Novel Connexin 43 (GJA1) mutation causes oculo-dento-digital dysplasia
RT with curly hair.";
RL Am. J. Med. Genet. A 127:152-157(2004).
RN [30]
RP VARIANT HSS HIS-76.
RX PubMed=14974090; DOI=10.1002/humu.9220;
RA Pizzuti A., Flex E., Mingarelli R., Salpietro C., Zelante L.,
RA Dallapiccola B.;
RT "A homozygous GJA1 gene mutation causes a Hallermann-Streiff/ODDD spectrum
RT phenotype.";
RL Hum. Mutat. 23:286-286(2004).
RN [31]
RP VARIANTS ODDD PRO-27; MET-31; VAL-40; TYR-69; PRO-113; ASN-134; GLN-148 AND
RP HIS-202, AND VARIANT SDTY3 SER-143.
RX PubMed=14729836; DOI=10.1136/jmg.2003.012005;
RA Richardson R.R., Donnai D., Meire F., Dixon M.J.;
RT "Expression of Gja1 correlates with the phenotype observed in
RT oculodentodigital syndrome/type III syndactyly.";
RL J. Med. Genet. 41:60-67(2004).
RN [32]
RP VARIANT ODDD PRO-194.
RX PubMed=15637728; DOI=10.1002/ajmg.a.30554;
RA Vitiello C., D'Adamo P., Gentile F., Vingolo E.M., Gasparini P., Banfi S.;
RT "A novel GJA1 mutation causes oculodentodigital dysplasia without
RT syndactyly.";
RL Am. J. Med. Genet. A 133:58-60(2005).
RN [33]
RP VARIANT ODDD ARG-95.
RX PubMed=16222672; DOI=10.1002/ajmg.a.30925;
RA Honkaniemi J., Kalkkila J.P., Koivisto P., Kahara V., Latvala T.,
RA Simola K.;
RT "Letter to the editor: Novel GJA1 mutation in oculodentodigital
RT dysplasia.";
RL Am. J. Med. Genet. A 139:48-49(2005).
RN [34]
RP VARIANT ODDD HIS-59.
RX PubMed=16219735; DOI=10.1001/archopht.123.10.1422;
RA Vasconcellos J.P.C., Melo M.B., Schimiti R.B., Bressanim N.C., Costa F.F.,
RA Costa V.P.;
RT "A novel mutation in the GJA1 gene in a family with oculodentodigital
RT dysplasia.";
RL Arch. Ophthalmol. 123:1422-1426(2005).
RN [35]
RP VARIANTS CONGENITAL HEART MALFORMATIONS TRP-239; THR-251; PRO-253; LEU-283
RP AND ASN-290.
RX PubMed=15978203;
RA Chen P., Xie L.-J., Huang G.-Y., Zhao X.-Q., Chang C.;
RT "Mutations of connexin43 in fetuses with congenital heart malformations.";
RL Chin. Med. J. 118:971-976(2005).
RN [36]
RP VARIANT LEU-41.
RX PubMed=15757815;
RA Kellermayer R., Keller M., Ratajczak P., Richardson E., Harangi F.,
RA Merei E., Melegh B., Kosztolanyi G., Richard G.;
RT "Bigenic connexin mutations in a patient with hidrotic ectodermal
RT dysplasia.";
RL Eur. J. Dermatol. 15:75-79(2005).
RN [37]
RP VARIANTS ODDD VAL-40; ASP-110; THR-147 AND PHE-169 DEL.
RX PubMed=16378922; DOI=10.1016/j.ejmg.2005.05.003;
RA Debeer P., Van Esch H., Huysmans C., Pijkels E., De Smet L., Van de Ven W.,
RA Devriendt K., Fryns J.-P.;
RT "Novel GJA1 mutations in patients with oculo-dento-digital dysplasia
RT (ODDD).";
RL Eur. J. Med. Genet. 48:377-387(2005).
RN [38]
RP VARIANTS ODDD GLU-96; PRO-113; ASN-154 AND TYR-220.
RX PubMed=16813608; DOI=10.1111/j.1399-0004.2006.00631.x;
RA Wiest T., Herrmann O., Stoegbauer F., Grasshoff U., Enders H., Koch M.J.,
RA Grond-Ginsbach C., Schwaninger M.;
RT "Clinical and genetic variability of oculodentodigital dysplasia.";
RL Clin. Genet. 70:71-72(2006).
RN [39]
RP VARIANT ODDD PRO-11.
RX PubMed=16709485;
RA Kelly S.C., Ratajczak P., Keller M., Purcell S.M., Griffin T., Richard G.;
RT "A novel GJA 1 mutation in oculo-dento-digital dysplasia with curly hair
RT and hyperkeratosis.";
RL Eur. J. Dermatol. 16:241-245(2006).
RN [40]
RP VARIANT ODDD ALA-154.
RX PubMed=17509830; DOI=10.1016/j.ijom.2007.03.004;
RA van Es R.J.J., Wittebol-Post D., Beemer F.A.;
RT "Oculodentodigital dysplasia with mandibular retrognathism and absence of
RT syndactyly: a case report with a novel mutation in the connexin 43 gene.";
RL Int. J. Oral Maxillofac. Surg. 36:858-860(2007).
RN [41]
RP VARIANT ODDD VAL-2.
RX PubMed=18161618; DOI=10.1080/13816810701538620;
RA de la Parra D.R., Zenteno J.C.;
RT "A new GJA1 (connexin 43) mutation causing oculodentodigital dysplasia
RT associated to uncommon features.";
RL Ophthalmic Genet. 28:198-202(2007).
RN [42]
RP VARIANTS ODDD VAL-7; VAL-40; PRO-49; GLN-49 INS; ALA-96; PRO-106; ALA-154;
RP PHE-201 AND HIS-202.
RX PubMed=19338053; DOI=10.1002/humu.20958;
RA Paznekas W.A., Karczeski B., Vermeer S., Lowry R.B., Delatycki M.,
RA Laurence F., Koivisto P.A., Van Maldergem L., Boyadjiev S.A.,
RA Bodurtha J.N., Jabs E.W.;
RT "GJA1 mutations, variants, and connexin 43 dysfunction as it relates to the
RT oculodentodigital dysplasia phenotype.";
RL Hum. Mutat. 30:724-733(2009).
RN [43]
RP VARIANTS ODDD PRO-11 AND 41-VAL--ALA-44 DEL.
RX PubMed=21670345; DOI=10.1001/archophthalmol.2011.113;
RA Gabriel L.A., Sachdeva R., Marcotty A., Rockwood E.J., Traboulsi E.I.;
RT "Oculodentodigital dysplasia: new ocular findings and a novel connexin 43
RT mutation.";
RL Arch. Ophthalmol. 129:781-784(2011).
RN [44]
RP VARIANT ODDD ARG-206.
RX PubMed=23550541; DOI=10.1111/cge.12158;
RA Brice G., Ostergaard P., Jeffery S., Gordon K., Mortimer P.S., Mansour S.;
RT "A novel mutation in GJA1 causing oculodentodigital syndrome and primary
RT lymphoedema in a three generation family.";
RL Clin. Genet. 84:378-381(2013).
RN [45]
RP VARIANT CMDR GLN-239.
RX PubMed=23951358; DOI=10.1371/journal.pone.0073576;
RA Hu Y., Chen I.P., de Almeida S., Tiziani V., Do Amaral C.M.,
RA Gowrishankar K., Passos-Bueno M.R., Reichenberger E.J.;
RT "A novel autosomal recessive GJA1 missense mutation linked to
RT Craniometaphyseal dysplasia.";
RL PLoS ONE 8:E73576-E73576(2013).
RN [46]
RP VARIANTS ODDD HIS-47; TYR-86 AND ARG-106.
RX PubMed=24508941; DOI=10.1016/j.gene.2014.01.066;
RA Jamsheer A., Sowinska-Seidler A., Socha M., Stembalska A., Kiraly-Borri C.,
RA Latos-Bielenska A.;
RT "Three novel GJA1 missense substitutions resulting in oculo-dento-digital
RT dysplasia (ODDD) - further extension of the mutational spectrum.";
RL Gene 539:157-161(2014).
RN [47]
RP VARIANT ODDD ILE-11.
RX PubMed=28258662; DOI=10.1111/odi.12663;
RA Porntaveetus T., Srichomthong C., Ohazama A., Suphapeetiporn K.,
RA Shotelersuk V.;
RT "A novel GJA1 mutation in oculodentodigitaldysplasia with extensive loss of
RT enamel.";
RL Oral Dis. 23:795-800(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. May play a critical
CC role in the physiology of hearing by participating in the recycling of
CC potassium to the cochlear endolymph. Negative regulator of bladder
CC functional capacity: acts by enhancing intercellular electrical and
CC chemical transmission, thus sensitizing bladder muscles to cholinergic
CC neural stimuli and causing them to contract (By similarity). May play a
CC role in cell growth inhibition through the regulation of NOV expression
CC and localization. Plays an essential role in gap junction communication
CC in the ventricles (By similarity). {ECO:0000250|UniProtKB:P08050,
CC ECO:0000250|UniProtKB:P23242}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC (via C-terminus) with TJP1 (By similarity). Interacts (via C-terminus)
CC with SRC (via SH3 domain) (By similarity). Interacts (not
CC ubiquitinated) with UBQLN4 (via UBA domain) (By similarity). Interacts
CC with SGSM3 and CNST (By similarity). Interacts with RIC1/CIP150.
CC Interacts with CSNK1D. Interacts with NOV (PubMed:15181016,
CC PubMed:15213231). Interacts with TMEM65 (By similarity). Interacts with
CC ANK3/ANKG and PKP2 (By similarity). {ECO:0000250|UniProtKB:P08050,
CC ECO:0000250|UniProtKB:P23242, ECO:0000269|PubMed:12270943,
CC ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:15213231,
CC ECO:0000269|PubMed:16112082}.
CC -!- INTERACTION:
CC P17302; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-1103439, EBI-2875816;
CC P17302; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-1103439, EBI-747505;
CC P17302; O43889-2: CREB3; NbExp=4; IntAct=EBI-1103439, EBI-625022;
CC P17302; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-1103439, EBI-9087876;
CC P17302; Q02487-1: DSC2; NbExp=2; IntAct=EBI-1103439, EBI-6900677;
CC P17302; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-1103439, EBI-10317425;
CC P17302; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-1103439, EBI-10485931;
CC P17302; Q07157: TJP1; NbExp=3; IntAct=EBI-1103439, EBI-79553;
CC P17302; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-1103439, EBI-10694905;
CC P17302; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1103439, EBI-2548832;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22411987,
CC ECO:0000269|PubMed:25398053}; Multi-pass membrane protein
CC {ECO:0000255}. Cell junction, gap junction
CC {ECO:0000269|PubMed:22411987, ECO:0000269|PubMed:25398053}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the
CC intercalated disk (ICD) in cardiomyocytes and the proper localization
CC at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart and fetal cochlea.
CC {ECO:0000269|PubMed:11741837}.
CC -!- PTM: Phosphorylated at Ser-368 by PRKCG; phosphorylation induces
CC disassembly of gap junction plaques and inhibition of gap junction
CC activity (By similarity). Phosphorylation at Ser-325, Ser-328 and Ser-
CC 330 by CK1 modulates gap junction assembly. Phosphorylation at Ser-368
CC by PRKCD triggers its internalization into small vesicles leading to
CC proteasome-mediated degradation (By similarity).
CC {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:Q6TYA7,
CC ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14702389,
CC ECO:0000269|PubMed:15605363}.
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. {ECO:0000269|PubMed:22411987}.
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:0000250|UniProtKB:P23242}.
CC -!- PTM: Acetylated in the developing cortex; leading to delocalization
CC from the cell membrane. {ECO:0000250|UniProtKB:P23242}.
CC -!- DISEASE: Oculodentodigital dysplasia (ODDD) [MIM:164200]: A disease
CC characterized by a typical facial appearance and variable involvement
CC of the eyes, dentition, and fingers. Characteristic facial features
CC include a narrow, pinched nose with hypoplastic alae nasi, prominent
CC columella and thin anteverted nares together with a narrow nasal
CC bridge, and prominent epicanthic folds giving the impression of
CC hypertelorism. The teeth are usually small and carious. Typical eye
CC findings include microphthalmia and microcornea. The characteristic
CC digital malformation is complete syndactyly of the fourth and fifth
CC fingers (syndactyly type III) but the third finger may be involved and
CC associated camptodactyly is a common finding. Cardiac abnormalities are
CC observed in rare instances. {ECO:0000269|PubMed:12457340,
CC ECO:0000269|PubMed:14729836, ECO:0000269|PubMed:15108203,
CC ECO:0000269|PubMed:15637728, ECO:0000269|PubMed:16219735,
CC ECO:0000269|PubMed:16222672, ECO:0000269|PubMed:16378922,
CC ECO:0000269|PubMed:16709485, ECO:0000269|PubMed:16813608,
CC ECO:0000269|PubMed:16816024, ECO:0000269|PubMed:17509830,
CC ECO:0000269|PubMed:18161618, ECO:0000269|PubMed:19338053,
CC ECO:0000269|PubMed:21670345, ECO:0000269|PubMed:23550541,
CC ECO:0000269|PubMed:24508941, ECO:0000269|PubMed:28258662}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Oculodentodigital dysplasia, autosomal recessive (ODDD-AR)
CC [MIM:257850]: A disease characterized by a typical facial appearance
CC and variable involvement of the eyes, dentition, and fingers.
CC Characteristic facial features include a narrow, pinched nose with
CC hypoplastic alae nasi, prominent columella and thin anteverted nares
CC together with a narrow nasal bridge, and prominent epicanthic folds
CC giving the impression of hypertelorism. The teeth are usually small and
CC carious. Typical eye findings include microphthalmia and microcornea.
CC The characteristic digital malformation is complete syndactyly of the
CC fourth and fifth fingers (syndactyly type III) but the third finger may
CC be involved and associated camptodactyly is a common finding. Cardiac
CC abnormalities are observed in rare instances.
CC {ECO:0000269|PubMed:16816024}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Syndactyly 3 (SDTY3) [MIM:186100]: A form of syndactyly, a
CC congenital anomaly of the hand or foot marked by persistence of the
CC webbing between adjacent digits that are more or less completely
CC attached. In SDTY3, there is usually complete and bilateral syndactyly
CC between the fourth and fifth fingers. Usually it is soft tissue
CC syndactyly but occasionally the distal phalanges are fused. The fifth
CC finger is short with absent or rudimentary middle phalanx. The feet are
CC not affected. {ECO:0000269|PubMed:14729836}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Hypoplastic left heart syndrome 1 (HLHS1) [MIM:241550]: A
CC syndrome due to defective development of the aorta proximal to the
CC entrance of the ductus arteriosus, and hypoplasia of the left ventricle
CC and mitral valve. As a result of the abnormal circulation, the ductus
CC arteriosus and foramen ovale are patent and the right atrium, right
CC ventricle, and pulmonary artery are enlarged.
CC {ECO:0000269|PubMed:11470490}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Hallermann-Streiff syndrome (HSS) [MIM:234100]: A disorder
CC characterized by a typical skull shape (brachycephaly with frontal
CC bossing), hypotrichosis, microphthalmia, cataracts, beaked nose,
CC micrognathia, skin atrophy, dental anomalies and proportionate short
CC stature. Intellectual disability is present in a minority of cases.
CC {ECO:0000269|PubMed:14974090}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Craniometaphyseal dysplasia, autosomal recessive (CMDR)
CC [MIM:218400]: An osteochondrodysplasia characterized by hyperostosis
CC and sclerosis of the craniofacial bones associated with abnormal
CC modeling of the metaphyses. Sclerosis of the skull may lead to
CC asymmetry of the mandible, as well as to cranial nerve compression,
CC that may finally result in hearing loss and facial palsy.
CC {ECO:0000269|PubMed:23951358}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Erythrokeratodermia variabilis et progressiva 3 (EKVP3)
CC [MIM:617525]: A form of erythrokeratodermia variabilis et progressiva,
CC a genodermatosis characterized by the coexistence of two independent
CC skin lesions: transient erythema and hyperkeratosis that is usually
CC localized but occasionally occurs in its generalized form. Clinical
CC presentation varies significantly within a family and from one family
CC to another. Palmoplantar keratoderma is present in around 50% of cases.
CC {ECO:0000269|PubMed:25398053}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Palmoplantar keratoderma and congenital alopecia 1 (PPKCA1)
CC [MIM:104100]: A rare autosomal dominant disorder characterized by
CC severe hyperkeratosis of the palms and soles, and congenital
CC hypotrichosis or alopecia. Dystrophic nail changes occur in some
CC patients. {ECO:0000269|PubMed:25168385}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:7715640 reported a mutation Pro-364 linked to
CC congenital heart diseases. PubMed:8873667 later shown that it is an
CC artifact. {ECO:0000305}.
CC -!- CAUTION: PubMed:11741837 reported 2 mutations (Phe-11 and Ala-24)
CC linked to non-syndromic autosomal recessive deafness (DFNBG). These
CC mutations have subsequently been shown (PubMed:12457340) to involve the
CC pseudogene of connexin-43 located on chromosome 5.
CC {ECO:0000305|PubMed:12457340}.
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DR EMBL; X52947; CAA37122.1; -; mRNA.
DR EMBL; M65188; AAA52131.1; -; mRNA.
DR EMBL; AF151980; AAD37802.2; -; Genomic_DNA.
DR EMBL; CR541660; CAG46461.1; -; mRNA.
DR EMBL; AK312324; BAG35246.1; -; mRNA.
DR EMBL; AL139098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48178.1; -; Genomic_DNA.
DR EMBL; BC026329; AAH26329.1; -; mRNA.
DR CCDS; CCDS5123.1; -.
DR PIR; A35853; A35853.
DR RefSeq; NP_000156.1; NM_000165.4.
DR PDB; 2LL2; NMR; -; A=234-259.
DR PDB; 7F92; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7F93; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7F94; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-257.
DR PDB; 7XQ9; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7XQB; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7XQD; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-257.
DR PDB; 7XQF; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-257.
DR PDB; 7XQG; EM; 3.80 A; A/B/C/D/E/F=1-257.
DR PDB; 7XQH; EM; 3.80 A; A/B/C/D/E/F=1-257.
DR PDB; 7XQI; EM; 3.70 A; A/B/C/D/E/F=1-257.
DR PDB; 7XQJ; EM; 4.00 A; A/B/C/D/E/F=1-257.
DR PDB; 7Z1T; EM; 2.26 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7Z22; EM; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-382.
DR PDB; 7Z23; EM; 3.98 A; A/B/C/D/E/F=1-382.
DR PDBsum; 2LL2; -.
DR PDBsum; 7F92; -.
DR PDBsum; 7F93; -.
DR PDBsum; 7F94; -.
DR PDBsum; 7XQ9; -.
DR PDBsum; 7XQB; -.
DR PDBsum; 7XQD; -.
DR PDBsum; 7XQF; -.
DR PDBsum; 7XQG; -.
DR PDBsum; 7XQH; -.
DR PDBsum; 7XQI; -.
DR PDBsum; 7XQJ; -.
DR PDBsum; 7Z1T; -.
DR PDBsum; 7Z22; -.
DR PDBsum; 7Z23; -.
DR AlphaFoldDB; P17302; -.
DR BMRB; P17302; -.
DR EMDB; EMD-14452; -.
DR EMDB; EMD-14455; -.
DR EMDB; EMD-14456; -.
DR EMDB; EMD-31495; -.
DR EMDB; EMD-31496; -.
DR EMDB; EMD-31497; -.
DR EMDB; EMD-33391; -.
DR EMDB; EMD-33392; -.
DR EMDB; EMD-33393; -.
DR EMDB; EMD-33394; -.
DR EMDB; EMD-33395; -.
DR EMDB; EMD-33396; -.
DR EMDB; EMD-33397; -.
DR EMDB; EMD-33398; -.
DR EMDB; EMD-33399; -.
DR SMR; P17302; -.
DR BioGRID; 108964; 575.
DR IntAct; P17302; 55.
DR MINT; P17302; -.
DR STRING; 9606.ENSP00000282561; -.
DR BindingDB; P17302; -.
DR ChEMBL; CHEMBL4680024; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB01136; Carvedilol.
DR TCDB; 1.A.24.1.16; the gap junction-forming connexin (connexin) family.
DR iPTMnet; P17302; -.
DR PhosphoSitePlus; P17302; -.
DR SwissPalm; P17302; -.
DR BioMuta; GJA1; -.
DR DMDM; 117706; -.
DR EPD; P17302; -.
DR jPOST; P17302; -.
DR MassIVE; P17302; -.
DR MaxQB; P17302; -.
DR PaxDb; 9606-ENSP00000282561; -.
DR PeptideAtlas; P17302; -.
DR ProteomicsDB; 53467; -.
DR Pumba; P17302; -.
DR TopDownProteomics; P17302; -.
DR ABCD; P17302; 3 sequenced antibodies.
DR Antibodypedia; 4382; 1392 antibodies from 49 providers.
DR DNASU; 2697; -.
DR Ensembl; ENST00000282561.4; ENSP00000282561.3; ENSG00000152661.9.
DR Ensembl; ENST00000647564.1; ENSP00000497565.1; ENSG00000152661.9.
DR Ensembl; ENST00000649003.1; ENSP00000497283.1; ENSG00000152661.9.
DR Ensembl; ENST00000650427.1; ENSP00000497367.1; ENSG00000152661.9.
DR GeneID; 2697; -.
DR KEGG; hsa:2697; -.
DR MANE-Select; ENST00000282561.4; ENSP00000282561.3; NM_000165.5; NP_000156.1.
DR UCSC; uc003pyr.4; human.
DR AGR; HGNC:4274; -.
DR CTD; 2697; -.
DR DisGeNET; 2697; -.
DR GeneCards; GJA1; -.
DR HGNC; HGNC:4274; GJA1.
DR HPA; ENSG00000152661; Low tissue specificity.
DR MalaCards; GJA1; -.
DR MIM; 104100; phenotype.
DR MIM; 121014; gene.
DR MIM; 164200; phenotype.
DR MIM; 186100; phenotype.
DR MIM; 218400; phenotype.
DR MIM; 234100; phenotype.
DR MIM; 241550; phenotype.
DR MIM; 257850; phenotype.
DR MIM; 617525; phenotype.
DR neXtProt; NX_P17302; -.
DR OpenTargets; ENSG00000152661; -.
DR Orphanet; 1010; Autosomal dominant palmoplantar keratoderma and congenital alopecia.
DR Orphanet; 1522; Craniometaphyseal dysplasia.
DR Orphanet; 317; Erythrokeratodermia variabilis.
DR Orphanet; 2248; Hypoplastic left heart syndrome.
DR Orphanet; 2710; Oculodentodigital dysplasia.
DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 93404; Syndactyly type 3.
DR PharmGKB; PA28685; -.
DR VEuPathDB; HostDB:ENSG00000152661; -.
DR eggNOG; ENOG502QRAE; Eukaryota.
DR GeneTree; ENSGT01090000260070; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; P17302; -.
DR OMA; WYMYGFT; -.
DR OrthoDB; 5301774at2759; -.
DR PhylomeDB; P17302; -.
DR TreeFam; TF329606; -.
DR PathwayCommons; P17302; -.
DR Reactome; R-HSA-190704; Oligomerization of connexins into connexons.
DR Reactome; R-HSA-190827; Transport of connexins along the secretory pathway.
DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR Reactome; R-HSA-190873; Gap junction degradation.
DR Reactome; R-HSA-191650; Regulation of gap junction activity.
DR Reactome; R-HSA-196025; Formation of annular gap junctions.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9705677; SARS-CoV-2 targets PDZ proteins in cell-cell junction.
DR SignaLink; P17302; -.
DR SIGNOR; P17302; -.
DR BioGRID-ORCS; 2697; 29 hits in 1120 CRISPR screens.
DR ChiTaRS; GJA1; human.
DR GeneWiki; GJA1; -.
DR GenomeRNAi; 2697; -.
DR Pharos; P17302; Tbio.
DR PRO; PR:P17302; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P17302; Protein.
DR Bgee; ENSG00000152661; Expressed in lateral globus pallidus and 204 other cell types or tissues.
DR ExpressionAtlas; P17302; baseline and differential.
DR Genevisible; P17302; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:ARUK-UCL.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0043292; C:contractile fiber; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005921; C:gap junction; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:ARUK-UCL.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005243; F:gap junction channel activity; IDA:BHF-UCL.
DR GO; GO:0086075; F:gap junction channel activity involved in cardiac conduction electrical coupling; NAS:BHF-UCL.
DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IDA:BHF-UCL.
DR GO; GO:0055077; F:gap junction hemi-channel activity; IMP:UniProtKB.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; TAS:BHF-UCL.
DR GO; GO:0003294; P:atrial ventricular junction remodeling; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0046849; P:bone remodeling; ISS:UniProtKB.
DR GO; GO:0003161; P:cardiac conduction system development; NAS:BHF-UCL.
DR GO; GO:0010643; P:cell communication by chemical coupling; IEA:Ensembl.
DR GO; GO:0010644; P:cell communication by electrical coupling; IDA:BHF-UCL.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; NAS:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
DR GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
DR GO; GO:0002069; P:columnar/cuboidal epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ARUK-UCL.
DR GO; GO:0140115; P:export across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0016264; P:gap junction assembly; TAS:UniProtKB.
DR GO; GO:0014047; P:glutamate secretion; ISS:ARUK-UCL.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0099111; P:microtubule-based transport; IMP:UniProtKB.
DR GO; GO:0060156; P:milk ejection reflex; IEA:Ensembl.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032277; P:negative regulation of gonadotropin secretion; IMP:ARUK-UCL.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; IMP:ARUK-UCL.
DR GO; GO:0097402; P:neuroblast migration; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1905772; P:positive regulation of mesodermal cell differentiation; IMP:ARUK-UCL.
DR GO; GO:1905332; P:positive regulation of morphogenesis of an epithelium; IMP:ARUK-UCL.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:ARUK-UCL.
DR GO; GO:0045844; P:positive regulation of striated muscle tissue development; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:ARUK-UCL.
DR GO; GO:0008104; P:protein localization; IMP:ARUK-UCL.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0046850; P:regulation of bone remodeling; IEA:Ensembl.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0042908; P:xenobiotic transport; ISS:ARUK-UCL.
DR Gene3D; 1.20.5.1130; Connexin43; 1.
DR Gene3D; 1.20.1440.80; Gap junction channel protein cysteine-rich domain; 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; CONNEXIN; 1.
DR PANTHER; PTHR11984:SF33; GAP JUNCTION ALPHA-1 PROTEIN; 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; Connexin43; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Cell junction; Cell membrane;
KW Disease variant; Disulfide bond; Endoplasmic reticulum; Gap junction;
KW Hypotrichosis; Isopeptide bond; Membrane; Palmoplantar keratoderma;
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_0000057801"
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:0000250|UniProtKB:P23242"
FT REGION 317..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..340
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:0000250|UniProtKB:P23242"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15605363,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14702389,
FT ECO:0000269|PubMed:15605363"
FT MOD_RES 271
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 325
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:12270943"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 328
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:12270943"
FT MOD_RES 330
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:12270943"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 368
FT /note="Phosphoserine; by PKC/PRKCG and PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23242"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT DISULFID 54..192
FT /evidence="ECO:0000269|PubMed:9430691"
FT DISULFID 187..198
FT /evidence="ECO:0000269|PubMed:9430691"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:22411987"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:22411987"
FT VARIANT 2
FT /note="G -> V (in ODDD)"
FT /evidence="ECO:0000269|PubMed:18161618"
FT /id="VAR_058990"
FT VARIANT 7
FT /note="L -> V (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_058991"
FT VARIANT 8
FT /note="G -> V (in PPKCA1; can form functional gap
FT junctions; results in enhanced hemichannel activity that
FT causes increased cell death; dbSNP:rs864309644)"
FT /evidence="ECO:0000269|PubMed:25168385"
FT /id="VAR_075754"
FT VARIANT 11
FT /note="L -> I (in ODDD)"
FT /evidence="ECO:0000269|PubMed:28258662"
FT /id="VAR_078238"
FT VARIANT 11
FT /note="L -> P (in ODDD; dbSNP:rs121912969)"
FT /evidence="ECO:0000269|PubMed:16709485,
FT ECO:0000269|PubMed:21670345"
FT /id="VAR_058992"
FT VARIANT 17
FT /note="Y -> S (in ODDD; dbSNP:rs104893961)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015747"
FT VARIANT 18
FT /note="S -> P (in ODDD; dbSNP:rs104893962)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015748"
FT VARIANT 21
FT /note="G -> R (in ODDD; dbSNP:rs104893963)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015749"
FT VARIANT 22
FT /note="G -> E (in ODDD; dbSNP:rs104893964)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015750"
FT VARIANT 23
FT /note="K -> T (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015751"
FT VARIANT 27
FT /note="S -> P (in ODDD)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_038356"
FT VARIANT 31
FT /note="I -> M (in ODDD)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_038357"
FT VARIANT 40
FT /note="A -> V (in ODDD; dbSNP:rs1554200992)"
FT /evidence="ECO:0000269|PubMed:12457340,
FT ECO:0000269|PubMed:14729836, ECO:0000269|PubMed:16378922,
FT ECO:0000269|PubMed:19338053"
FT /id="VAR_015752"
FT VARIANT 41..44
FT /note="Missing (in ODDD)"
FT /evidence="ECO:0000269|PubMed:21670345"
FT /id="VAR_070439"
FT VARIANT 41
FT /note="V -> L (found in a patient with hidrotic ectodermal
FT dysplasia, abortive features of oculodentodigital dysplasia
FT and extensive hyperkeratosis of the skin; uncertain
FT significance; the patient also carries GJB2 variant H-127)"
FT /evidence="ECO:0000269|PubMed:15757815"
FT /id="VAR_058993"
FT VARIANT 44
FT /note="A -> V (in EKVP3; loss of localization to the plasma
FT membrane, retention in the Golgi apparatus;
FT dbSNP:rs794729675)"
FT /evidence="ECO:0000269|PubMed:25398053"
FT /id="VAR_075755"
FT VARIANT 47
FT /note="D -> H (in ODDD)"
FT /evidence="ECO:0000269|PubMed:24508941"
FT /id="VAR_071009"
FT VARIANT 49
FT /note="Q -> K (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015753"
FT VARIANT 49
FT /note="Q -> P (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_058994"
FT VARIANT 49
FT /note="Q -> QQ (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_058995"
FT VARIANT 52
FT /note="F -> FF (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015754"
FT VARIANT 59
FT /note="P -> H (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16219735"
FT /id="VAR_058996"
FT VARIANT 69
FT /note="S -> Y (in ODDD)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_038358"
FT VARIANT 76
FT /note="R -> H (in HSS; overlapping features with
FT oculodentodigital dysplasia; dbSNP:rs267606844)"
FT /evidence="ECO:0000269|PubMed:14974090"
FT /id="VAR_058997"
FT VARIANT 76
FT /note="R -> S (in ODDD; dbSNP:rs267606845)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015755"
FT VARIANT 86
FT /note="S -> Y (in ODDD; de novo mutation found in a
FT sporadic case)"
FT /evidence="ECO:0000269|PubMed:24508941"
FT /id="VAR_071010"
FT VARIANT 90
FT /note="L -> V (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015756"
FT VARIANT 95
FT /note="H -> R (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16222672"
FT /id="VAR_058998"
FT VARIANT 96
FT /note="V -> A (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_058999"
FT VARIANT 96
FT /note="V -> E (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16813608"
FT /id="VAR_059000"
FT VARIANT 96
FT /note="V -> M (in ODDD; dbSNP:rs28931601)"
FT /evidence="ECO:0000269|PubMed:15108203"
FT /id="VAR_059001"
FT VARIANT 98
FT /note="Y -> C (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015757"
FT VARIANT 102
FT /note="K -> N (in ODDD; dbSNP:rs1554201011)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015758"
FT VARIANT 106
FT /note="L -> P (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_059002"
FT VARIANT 106
FT /note="L -> R (in ODDD)"
FT /evidence="ECO:0000269|PubMed:24508941"
FT /id="VAR_071011"
FT VARIANT 110
FT /note="E -> D (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16378922"
FT /id="VAR_059003"
FT VARIANT 113
FT /note="L -> P (in ODDD)"
FT /evidence="ECO:0000269|PubMed:14729836,
FT ECO:0000269|PubMed:16813608"
FT /id="VAR_038359"
FT VARIANT 130
FT /note="I -> T (in ODDD; dbSNP:rs1554201017)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015759"
FT VARIANT 134
FT /note="K -> E (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015760"
FT VARIANT 134
FT /note="K -> N (in ODDD)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_038360"
FT VARIANT 138
FT /note="G -> R (in ODDD)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015761"
FT VARIANT 143
FT /note="G -> S (in SDTY3; dbSNP:rs28931600)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_038361"
FT VARIANT 147
FT /note="M -> T (in ODDD; dbSNP:rs1057518872)"
FT /evidence="ECO:0000269|PubMed:16378922"
FT /id="VAR_059004"
FT VARIANT 148
FT /note="R -> Q (in ODDD; dbSNP:rs962041031)"
FT /evidence="ECO:0000269|PubMed:14729836"
FT /id="VAR_014095"
FT VARIANT 154
FT /note="T -> A (in ODDD)"
FT /evidence="ECO:0000269|PubMed:17509830,
FT ECO:0000269|PubMed:19338053"
FT /id="VAR_059005"
FT VARIANT 154
FT /note="T -> N (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16813608"
FT /id="VAR_059006"
FT VARIANT 168
FT /note="A -> T (in dbSNP:rs2228961)"
FT /id="VAR_014096"
FT VARIANT 169
FT /note="Missing (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16378922"
FT /id="VAR_059007"
FT VARIANT 194
FT /note="H -> P (in ODDD; atypical form of ODDD characterized
FT by the predominance of the ocular involvement and by the
FT absence of hand and/or foot syndactyly and absence of any
FT neurologic signs; dbSNP:rs104893966)"
FT /evidence="ECO:0000269|PubMed:15637728"
FT /id="VAR_059008"
FT VARIANT 201
FT /note="S -> F (in ODDD)"
FT /evidence="ECO:0000269|PubMed:19338053"
FT /id="VAR_059009"
FT VARIANT 202
FT /note="R -> H (in ODDD; dbSNP:rs750294638)"
FT /evidence="ECO:0000269|PubMed:12457340,
FT ECO:0000269|PubMed:14729836, ECO:0000269|PubMed:19338053"
FT /id="VAR_015762"
FT VARIANT 206
FT /note="K -> R (in ODDD; dbSNP:rs397518464)"
FT /evidence="ECO:0000269|PubMed:23550541"
FT /id="VAR_070440"
FT VARIANT 216
FT /note="V -> L (in ODDD; dbSNP:rs1554201043)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015763"
FT VARIANT 220
FT /note="S -> Y (in ODDD)"
FT /evidence="ECO:0000269|PubMed:16813608"
FT /id="VAR_059010"
FT VARIANT 227
FT /note="E -> D (in EKVP3; loss of localization to the plasma
FT membrane, retention in the Golgi apparatus;
FT dbSNP:rs875989815)"
FT /evidence="ECO:0000269|PubMed:25398053"
FT /id="VAR_075756"
FT VARIANT 239
FT /note="R -> Q (in CMDR; dbSNP:rs764670582)"
FT /evidence="ECO:0000269|PubMed:23951358"
FT /id="VAR_070441"
FT VARIANT 239
FT /note="R -> W (in congenital heart malformations)"
FT /evidence="ECO:0000269|PubMed:15978203"
FT /id="VAR_014100"
FT VARIANT 251
FT /note="S -> T (in congenital heart malformations)"
FT /evidence="ECO:0000269|PubMed:15978203"
FT /id="VAR_059011"
FT VARIANT 253
FT /note="A -> P (in congenital heart malformations)"
FT /evidence="ECO:0000269|PubMed:15978203"
FT /id="VAR_059012"
FT VARIANT 253
FT /note="A -> V (in dbSNP:rs17653265)"
FT /evidence="ECO:0000269|PubMed:12457340"
FT /id="VAR_015764"
FT VARIANT 283
FT /note="P -> L (in congenital heart malformations)"
FT /evidence="ECO:0000269|PubMed:15978203"
FT /id="VAR_014101"
FT VARIANT 290
FT /note="T -> N (in congenital heart malformations)"
FT /evidence="ECO:0000269|PubMed:15978203"
FT /id="VAR_014102"
FT VARIANT 326
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:7715640"
FT /id="VAR_059013"
FT VARIANT 352
FT /note="E -> G (in heart malformations)"
FT /evidence="ECO:0000269|PubMed:7715640"
FT /id="VAR_059014"
FT VARIANT 362
FT /note="R -> Q (in HLHS1; uncertain significance; abolishes
FT phosphorylation by PKA and PKC when associated with Q-376;
FT dbSNP:rs2227885)"
FT /evidence="ECO:0000269|PubMed:11470490"
FT /id="VAR_032924"
FT VARIANT 364
FT /note="S -> P (in heart malformations; shows abnormalities
FT in the regulation of cell-cell communication as compared
FT with cells expressing normal GJA1)"
FT /evidence="ECO:0000269|PubMed:7715640"
FT /id="VAR_059015"
FT VARIANT 365
FT /note="S -> N (in heart malformations)"
FT /evidence="ECO:0000269|PubMed:7715640"
FT /id="VAR_059016"
FT VARIANT 373
FT /note="S -> G"
FT /evidence="ECO:0000269|PubMed:7715640"
FT /id="VAR_059017"
FT VARIANT 376
FT /note="R -> Q (in HLHS1; uncertain significance; abolishes
FT phosphorylation by PKA and PKC when associated with Q-362;
FT dbSNP:rs104893965)"
FT /evidence="ECO:0000269|PubMed:11470490"
FT /id="VAR_032925"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:7Z1T"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:7F92"
FT HELIX 22..44
FT /evidence="ECO:0007829|PDB:7Z1T"
FT TURN 45..50
FT /evidence="ECO:0007829|PDB:7Z1T"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7Z1T"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:7Z1T"
FT HELIX 74..104
FT /evidence="ECO:0007829|PDB:7Z1T"
FT HELIX 152..176
FT /evidence="ECO:0007829|PDB:7Z1T"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7Z1T"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:7Z1T"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:7Z1T"
FT HELIX 203..234
FT /evidence="ECO:0007829|PDB:7Z1T"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2LL2"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2LL2"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2LL2"
SQ SEQUENCE 382 AA; 43008 MW; 7DDDAD8040284176 CRC64;
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
VNVDMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSIFEVAFL LIQWYIYGFS
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
KGKSDPYHAT SGALSPAKDC GSQKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNSKKLAAG HELQPLAIVD
QRPSSRASSR ASSRPRPDDL EI
//
