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Protein

Gap junction alpha-1 protein

Gene

Gja1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication
Connexin 43 is possibly the ATP-induced pore of mouse macrophages.1 Publication

GO - Molecular functioni

  • beta-tubulin binding Source: MGI
  • gap junction channel activity Source: MGI
  • gap junction channel activity involved in cell communication by electrical coupling Source: MGI
  • ion transmembrane transporter activity Source: MGI
  • receptor binding Source: MGI
  • scaffold protein binding Source: BHF-UCL
  • signal transducer activity Source: MGI

GO - Biological processi

  • adult heart development Source: MGI
  • apoptotic process Source: Ensembl
  • ATP transport Source: Ensembl
  • atrial ventricular junction remodeling Source: MGI
  • blood vessel morphogenesis Source: MGI
  • cardiac conduction Source: MGI
  • cell-cell junction organization Source: MGI
  • cell-cell signaling Source: MGI
  • cell communication by chemical coupling Source: MGI
  • cell communication by electrical coupling Source: MGI
  • cellular response to mechanical stimulus Source: Ensembl
  • chronic inflammatory response Source: Ensembl
  • embryonic digit morphogenesis Source: MGI
  • embryonic heart tube development Source: MGI
  • endothelium development Source: Ensembl
  • epicardial cell to mesenchymal cell transition Source: DFLAT
  • epithelial cell maturation Source: MGI
  • establishment of epithelial cell polarity Source: DFLAT
  • heart development Source: MGI
  • heart looping Source: MGI
  • in utero embryonic development Source: MGI
  • ion transmembrane transport Source: MGI
  • lens development in camera-type eye Source: MGI
  • milk ejection Source: MGI
  • negative regulation of cardiac muscle cell proliferation Source: Ensembl
  • negative regulation of DNA biosynthetic process Source: Ensembl
  • negative regulation of endothelial cell proliferation Source: Ensembl
  • negative regulation of gene expression Source: MGI
  • negative regulation of wound healing Source: Ensembl
  • neuron migration Source: MGI
  • neuron projection morphogenesis Source: Ensembl
  • osteoblast differentiation Source: MGI
  • positive regulation of behavioral fear response Source: Ensembl
  • positive regulation of cell communication by chemical coupling Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of gene expression Source: MGI
  • positive regulation of glomerular filtration Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of insulin secretion Source: Ensembl
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of protein catabolic process Source: Ensembl
  • positive regulation of striated muscle tissue development Source: MGI
  • positive regulation of vasoconstriction Source: Ensembl
  • positive regulation of vasodilation Source: Ensembl
  • protein oligomerization Source: Ensembl
  • regulation of atrial cardiac muscle cell membrane depolarization Source: MGI
  • regulation of bicellular tight junction assembly Source: Ensembl
  • regulation of blood vessel remodeling Source: DFLAT
  • regulation of bone mineralization Source: MGI
  • regulation of bone remodeling Source: MGI
  • regulation of calcium ion transport Source: Ensembl
  • regulation of heart contraction Source: MGI
  • regulation of ventricular cardiac muscle cell membrane depolarization Source: MGI
  • regulation of ventricular cardiac muscle cell membrane repolarization Source: MGI
  • response to fluid shear stress Source: Ensembl
  • response to glucose Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • response to pH Source: Ensembl
  • signal transduction Source: MGI
  • skeletal muscle tissue regeneration Source: MGI
  • vascular transport Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_278834. Transport of connexins along the secretory pathway.
REACT_280776. Gap junction degradation.
REACT_284891. Oligomerization of connexins into connexons.
REACT_291802. Formation of annular gap junctions.
REACT_295993. Gap junction assembly.
REACT_307151. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_342354. c-src mediated regulation of Cx43 function and closure of gap junctions.

Names & Taxonomyi

Protein namesi
Recommended name:
Gap junction alpha-1 protein
Alternative name(s):
Connexin-43
Short name:
Cx43
Gap junction 43 kDa heart protein
Gene namesi
Name:Gja1
Synonyms:Cxn-43
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:95713. Gja1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1312CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3623HelicalSequence AnalysisAdd
BLAST
Topological domaini37 – 7640ExtracellularSequence AnalysisAdd
BLAST
Transmembranei77 – 9923HelicalSequence AnalysisAdd
BLAST
Topological domaini100 – 15455CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei155 – 17723HelicalSequence AnalysisAdd
BLAST
Topological domaini178 – 20831ExtracellularSequence AnalysisAdd
BLAST
Transmembranei209 – 23123HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 382151CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • connexon complex Source: Ensembl
  • contractile fiber Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • early endosome Source: Ensembl
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • fascia adherens Source: MGI
  • focal adhesion Source: MGI
  • gap junction Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: BHF-UCL
  • intermediate filament Source: BHF-UCL
  • lateral plasma membrane Source: MGI
  • lysosome Source: Ensembl
  • membrane Source: MGI
  • membrane raft Source: Ensembl
  • mitochondrial outer membrane Source: Ensembl
  • multivesicular body Source: Ensembl
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Gap junction, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice die shortly after birth.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 382381Gap junction alpha-1 proteinPRO_0000057802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 192By similarity
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Disulfide bondi187 ↔ 198By similarity
Cross-linki237 – 237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei247 – 2471Phosphotyrosine1 Publication
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei271 – 2711S-nitrosocysteine1 Publication
Modified residuei314 – 3141PhosphoserineBy similarity
Modified residuei325 – 3251Phosphoserine; by CK1By similarity
Modified residuei328 – 3281Phosphoserine; by CK1By similarity
Modified residuei330 – 3301Phosphoserine; by CK1By similarity
Modified residuei365 – 3651PhosphoserineBy similarity
Modified residuei368 – 3681Phosphoserine; by PKC/PRKCGBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity (By similarity).By similarity
Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the level of functional Cx43 gap junctions at the plasma membrane. May be desumoylated by SENP1 or SENP2 (By similarity).By similarity
S-nitrosylation at Cys-271 is enriched at the muscle endothelial gap junction in arteries, it augments channel permeability and may regulate of smooth muscle cell to endothelial cell communication.1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP23242.
PaxDbiP23242.
PRIDEiP23242.

PTM databases

PhosphoSiteiP23242.

Expressioni

Tissue specificityi

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).3 Publications

Developmental stagei

At 7.5 dpc, expressed in the embryo, but not in the extraembryonic region containing the ectoplacental cone.1 Publication

Inductioni

In bladder smooth muscle cells, exhibits night/day variations with low levels during the sleep phase, at circadian time (CT) 4-12 (at protein level). Downregulation during the night allows increase in bladder capacity, avoiding disturbance of sleep by micturition. Expression starts to increase around CT12 and forms a plateau during the active phase (CT16-24) (at protein level). Circadian transcription is activated by NR1D1. Up-regulated by SP1 and SP3.1 Publication

Gene expression databases

BgeeiP23242.
CleanExiMM_GJA1.
ExpressionAtlasiP23242. baseline and differential.
GenevisibleiP23242. MM.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Gjb3P282312EBI-298630,EBI-1767245
Gjc1P282292EBI-298630,EBI-1767271
Kcnj8Q636644EBI-298630,EBI-6991142From a different organism.
PrkcdP288674EBI-298630,EBI-1551324
PrkceP160543EBI-298630,EBI-298451
Tjp1P394473EBI-298630,EBI-79508
YwhaqP682543EBI-298630,EBI-400675

Protein-protein interaction databases

BioGridi199923. 6 interactions.
DIPiDIP-29207N.
IntActiP23242. 16 interactions.
MINTiMINT-1326689.
STRINGi10090.ENSMUSP00000064536.

Structurei

3D structure databases

ProteinModelPortaliP23242.
SMRiP23242. Positions 3-234, 252-382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 382119Interaction with UBQLN41 PublicationAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45368.
GeneTreeiENSGT00800000124029.
HOVERGENiHBG009576.
InParanoidiP23242.
KOiK07372.
OMAiGANVDMH.
OrthoDBiEOG7P2XSS.
PhylomeDBiP23242.
TreeFamiTF329606.

Family and domain databases

InterProiIPR000500. Connexin.
IPR002261. Connexin43.
IPR013124. Connexin43_C.
IPR019570. Connexin_CCC.
IPR017990. Connexin_CS.
IPR013092. Connexin_N.
[Graphical view]
PANTHERiPTHR11984. PTHR11984. 1 hit.
PfamiPF00029. Connexin. 1 hit.
PF03508. Connexin43. 1 hit.
PF10582. Connexin_CCC. 1 hit.
[Graphical view]
PRINTSiPR00206. CONNEXIN.
PR01132. CONNEXINA1.
SMARTiSM00037. CNX. 1 hit.
SM01089. Connexin_CCC. 1 hit.
[Graphical view]
PROSITEiPS00407. CONNEXINS_1. 1 hit.
PS00408. CONNEXINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS
60 70 80 90 100
AFRCNTQQPG CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM
110 120 130 140 150
RKEEKLNKKE EELKVAQTDG VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG
160 170 180 190 200
LLRTYIISIL FKSVFEVAFL LIQWYIYGFS LSAVYTCKRD PCPHQVDCFL
210 220 230 240 250
SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV KGRSDPYHAT
260 270 280 290 300
TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
310 320 330 340 350
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD SQNAKKVAAG
360 370 380
HELQPLAIVD QRPSSRASSR ASSRPRPDDL EI
Length:382
Mass (Da):43,004
Last modified:January 23, 2007 - v2
Checksum:i018DCB461FA69490
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211G → V in BAC26375 (PubMed:16141072).Curated
Sequence conflicti320 – 3201M → T in AAA53027 (PubMed:1318884).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61896 Genomic DNA. Translation: AAA37444.1.
M63801 mRNA. Translation: AAA53027.1.
X62836 Genomic DNA. Translation: CAA44640.1.
X61576 mRNA. Translation: CAA43778.1.
AK029291 mRNA. Translation: BAC26375.1.
AK036979 mRNA. Translation: BAC29656.1.
AK145692 mRNA. Translation: BAE26592.1.
AK165986 mRNA. Translation: BAE38502.1.
CT010327 mRNA. Translation: CAJ18535.1.
CH466540 Genomic DNA. Translation: EDL05108.1.
BC006894 mRNA. Translation: AAH06894.1.
CCDSiCCDS23851.1.
PIRiA39802.
RefSeqiNP_034418.1. NM_010288.3.
XP_006512604.1. XM_006512541.1.
XP_011241420.1. XM_011243118.1.
XP_011241421.1. XM_011243119.1.
UniGeneiMm.378921.

Genome annotation databases

EnsembliENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
GeneIDi14609.
KEGGimmu:14609.
UCSCiuc007fcc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61896 Genomic DNA. Translation: AAA37444.1.
M63801 mRNA. Translation: AAA53027.1.
X62836 Genomic DNA. Translation: CAA44640.1.
X61576 mRNA. Translation: CAA43778.1.
AK029291 mRNA. Translation: BAC26375.1.
AK036979 mRNA. Translation: BAC29656.1.
AK145692 mRNA. Translation: BAE26592.1.
AK165986 mRNA. Translation: BAE38502.1.
CT010327 mRNA. Translation: CAJ18535.1.
CH466540 Genomic DNA. Translation: EDL05108.1.
BC006894 mRNA. Translation: AAH06894.1.
CCDSiCCDS23851.1.
PIRiA39802.
RefSeqiNP_034418.1. NM_010288.3.
XP_006512604.1. XM_006512541.1.
XP_011241420.1. XM_011243118.1.
XP_011241421.1. XM_011243119.1.
UniGeneiMm.378921.

3D structure databases

ProteinModelPortaliP23242.
SMRiP23242. Positions 3-234, 252-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199923. 6 interactions.
DIPiDIP-29207N.
IntActiP23242. 16 interactions.
MINTiMINT-1326689.
STRINGi10090.ENSMUSP00000064536.

PTM databases

PhosphoSiteiP23242.

Proteomic databases

MaxQBiP23242.
PaxDbiP23242.
PRIDEiP23242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
GeneIDi14609.
KEGGimmu:14609.
UCSCiuc007fcc.2. mouse.

Organism-specific databases

CTDi2697.
MGIiMGI:95713. Gja1.

Phylogenomic databases

eggNOGiNOG45368.
GeneTreeiENSGT00800000124029.
HOVERGENiHBG009576.
InParanoidiP23242.
KOiK07372.
OMAiGANVDMH.
OrthoDBiEOG7P2XSS.
PhylomeDBiP23242.
TreeFamiTF329606.

Enzyme and pathway databases

ReactomeiREACT_278834. Transport of connexins along the secretory pathway.
REACT_280776. Gap junction degradation.
REACT_284891. Oligomerization of connexins into connexons.
REACT_291802. Formation of annular gap junctions.
REACT_295993. Gap junction assembly.
REACT_307151. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_342354. c-src mediated regulation of Cx43 function and closure of gap junctions.

Miscellaneous databases

ChiTaRSiGja1. mouse.
NextBioi286404.
PROiP23242.
SOURCEiSearch...

Gene expression databases

BgeeiP23242.
CleanExiMM_GJA1.
ExpressionAtlasiP23242. baseline and differential.
GenevisibleiP23242. MM.

Family and domain databases

InterProiIPR000500. Connexin.
IPR002261. Connexin43.
IPR013124. Connexin43_C.
IPR019570. Connexin_CCC.
IPR017990. Connexin_CS.
IPR013092. Connexin_N.
[Graphical view]
PANTHERiPTHR11984. PTHR11984. 1 hit.
PfamiPF00029. Connexin. 1 hit.
PF03508. Connexin43. 1 hit.
PF10582. Connexin_CCC. 1 hit.
[Graphical view]
PRINTSiPR00206. CONNEXIN.
PR01132. CONNEXINA1.
SMARTiSM00037. CNX. 1 hit.
SM01089. Connexin_CCC. 1 hit.
[Graphical view]
PROSITEiPS00407. CONNEXINS_1. 1 hit.
PS00408. CONNEXINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence that the gap junction protein connexin-43 is the ATP-induced pore of mouse macrophages."
    Beyer E.C., Steinberg T.H.
    J. Biol. Chem. 266:7971-7974(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Developmental regulation of gap junction gene expression during mouse embryonic development."
    Nishi M., Kumar N.M., Gilula N.B.
    Dev. Biol. 146:117-130(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Ovary.
  3. "Molecular cloning and functional expression of mouse connexin40, a second gap junction gene preferentially expressed in lung."
    Hennemann J., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E., Schwarz J., Nicholson B.J., Willecke K.
    J. Cell Biol. 117:1299-1310(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6.
  4. "Structure, sequence and expression of the mouse Cx43 gene encoding connexin 43."
    Sullivan R., Ruangvoravat C., Joo D., Morgan J., Wang B.L., Wang X.K., Lo C.W.
    Gene 130:191-199(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blastocyst, Head, Lung and Vagina.
  6. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  9. "Changes in the expression of connexin 43, a cardiac gap junctional protein, during mouse heart development."
    Fromaget C., el Aoumari A., Dupont E., Briand J.-P., Gros D.
    J. Mol. Cell. Cardiol. 22:1245-1258(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Mutations in GJA1 (connexin 43) are associated with non-syndromic autosomal recessive deafness."
    Liu X.Z., Xia X.J., Adams J., Chen Z.Y., Welch K.O., Tekin M., Ouyang X.M., Kristiansen A., Pandya A., Balkany T., Arnos K.S., Nance W.E.
    Hum. Mol. Genet. 10:2945-2951(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation."
    Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.
    Biochemistry 44:2385-2396(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM3.
  12. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  13. "A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43."
    Li X., Su V., Kurata W.E., Jin C., Lau A.F.
    J. Biol. Chem. 283:5748-5759(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UBQLN4.
  14. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  15. "Consortin, a trans-Golgi network cargo receptor for the plasma membrane targeting and recycling of connexins."
    del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D., Chavrier P., Meda P., Petit C.
    Hum. Mol. Genet. 19:262-275(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNST.
  16. "Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75."
    Su V., Nakagawa R., Koval M., Lau A.F.
    J. Biol. Chem. 285:40979-40990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UBQLN4.
  17. "Compartmentalized connexin 43 s-nitrosylation/denitrosylation regulates heterocellular communication in the vessel wall."
    Straub A.C., Billaud M., Johnstone S.R., Best A.K., Yemen S., Dwyer S.T., Looft-Wilson R., Lysiak J.J., Gaston B., Palmer L., Isakson B.E.
    Arterioscler. Thromb. Vasc. Biol. 31:399-407(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-271.
  18. "Involvement of urinary bladder Connexin43 and the circadian clock in coordination of diurnal micturition rhythm."
    Negoro H., Kanematsu A., Doi M., Suadicani S.O., Matsuo M., Imamura M., Okinami T., Nishikawa N., Oura T., Matsui S., Seo K., Tainaka M., Urabe S., Kiyokage E., Todo T., Okamura H., Tabata Y., Ogawa O.
    Nat. Commun. 3:809-809(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCXA1_MOUSE
AccessioniPrimary (citable) accession number: P23242
Secondary accession number(s): Q544I7, Q8CE05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.