[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1083/jcb.105.6.2621; PubMed=2826492 [NCBI, ExPASy, EBI, Israel, Japan] Beyer E.C., Paul D.L., Goodenough D.A.; "Connexin43: a protein from rat heart homologous to a gap junction protein from liver."; J. Cell Biol. 105:2621-2629(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Uterus; PubMed=1852114 [NCBI, ExPASy, EBI, Israel, Japan] Lang L.M., Beyer E.C., Schwartz A.L., Gitlin J.D.; "Molecular cloning of a rat uterine gap junction protein and analysis of gene expression during gestation."; Am. J. Physiol. 260:E787-E793(1991).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; Ma L.X., Peng Y.W.; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 2-33. TISSUE=Heart; PubMed=2987225 [NCBI, ExPASy, EBI, Israel, Japan] Nicholson B.J., Gros D.B., Kent S.B.H., Hood L.E., Revel J.-P.; "The Mr 28,000 gap junction proteins from rat heart and liver are different but related."; J. Biol. Chem. 260:6514-6517(1985).
[6]	PARTIAL PROTEIN SEQUENCE OF 2-16. TISSUE=Brain; PubMed=1652440 [NCBI, ExPASy, EBI, Israel, Japan] Dupont E., el Aoumari A., Fromaget C., Briand J.-C., Gros D.; "Affinity purification of a rat-brain junctional protein, connexin 43."; Eur. J. Biochem. 200:263-270(1991).
[7]	DISULFIDE BONDS. DOI=10.1016/0006-291X(91)91037-D; PubMed=1651718 [NCBI, ExPASy, EBI, Israel, Japan] John S.A., Revel J.-P.; "Connexon integrity is maintained by non-covalent bonds: intramolecular disulfide bonds link the extracellular domains in rat connexin-43."; Biochem. Biophys. Res. Commun. 178:1312-1318(1991).
[8]	TOPOLOGY. DOI=10.1016/0022-2836(92)90253-G; PubMed=1371548 [NCBI, ExPASy, EBI, Israel, Japan] Yeager M., Gilula N.B.; "Membrane topology and quaternary structure of cardiac gap junction ion channels."; J. Mol. Biol. 223:929-948(1992).
[9]	PHOSPHORYLATION AT SER-365; SER-368; SER-369 AND SER-373. DOI=10.1016/S0014-5793(02)03441-5; PubMed=12417300 [NCBI, ExPASy, EBI, Israel, Japan] Yogo K., Ogawa T., Akiyama M., Ishida N., Takeya T.; "Identification and functional analysis of novel phosphorylation sites in Cx43 in rat primary granulosa cells."; FEBS Lett. 531:132-136(2002).

Comments

FUNCTION: One 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.
SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts with SGSM3. Interacts with KIAA1432/CIP150 (By similarity).
INTERACTION:
Q16643:DBN1 (xeno); NbExp=1; IntAct=EBI-476947, EBI-351394;
Q9QXS6:Dbn1 (xeno); NbExp=1; IntAct=EBI-476947, EBI-445208;
Q8VCZ6:Rutbc3 (xeno); NbExp=1; IntAct=EBI-476947, EBI-525155;
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
PTM: Contains at least one intramolecular disulfide bond.
SIMILARITY: Belongs to the connexin family. Alpha-type (group II) subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X06656; CAA29855.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY324140; AAP88589.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081842; AAH81842.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24047; A24047.
S00532; S00532.

RefSeq

NP_036699.1; -.

UniGene

Rn.10346

3D structure databases

PDB

1R5S; NMR; -; A=255-382.

[ExPASy / RCSB / EBI]

1R5S; -.

DP00278; -.

Protein-protein interaction databases

IntAct

P08050; -.

PTM databases

PhosphoSite

P08050; -.

Organism-specific databases

RGD

2690; Gja1.

Gene expression databases

ArrayExpress

P08050; -.

GermOnline

ENSRNOG00000000805; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0005921;	Cellular component: gap junction (inferred from direct assay from UniProtKB).
GO:0030660;	Cellular component: Golgi-associated vesicle membrane (inferred from experiment from Reactome).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0016264;	Biological process: gap junction assembly (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000500; Connexin.
IPR013124; Connexin43_C.
IPR013092; Connexin_N.
Graphical view of domain structure.

PANTHER

PTHR11984; Connexin; 1.

Pfam

PF00029; Connexin; 1.
PF03508; Connexin43; 1.
Pfam graphical view of domain structure.

SMART

SM00037; CNX; 1.
SMART graphical view of domain structure.

PROSITE

PS00407; CONNEXINS_1; 1.
PS00408; CONNEXINS_2; 1.

BLOCKS

P08050.

Genome annotation databases

Ensembl

ENSRNOG00000000805; Rattus norvegicus. [Contig view]

GeneID

24392; -.

KEGG

rno:24392; -.

Phylogenomic databases

HOVERGEN

P08050; -.

Other

ProtoNet

P08050.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell junction; Cell membrane; Direct protein sequencing; Gap junction; Membrane; Phosphoprotein; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 382`	`381`	`Gap junction alpha-1 protein.`	`PRO_0000057804`
`TOPO_DOM`	`2 13`	`12`	`Cytoplasmic (Probable).`
`TRANSMEM`	`14 36`	`23`	`Probable.`
`TOPO_DOM`	`37 76`	`40`	`Extracellular (Probable).`
`TRANSMEM`	`77 99`	`23`	`Probable.`
`TOPO_DOM`	`100 154`	`55`	`Cytoplasmic (Probable).`
`TRANSMEM`	`155 177`	`23`	`Probable.`
`TOPO_DOM`	`178 208`	`31`	`Extracellular (Probable).`
`TRANSMEM`	`209 231`	`23`	`Probable.`
`TOPO_DOM`	`232 382`	`151`	`Cytoplasmic (Probable).`
`MOD_RES`	`247 247`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`306 306`		`Phosphoserine (By similarity).`
`MOD_RES`	`313 313`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`314 314`		`Phosphoserine (By similarity).`
`MOD_RES`	`326 326`		`Phosphothreonine (By similarity).`
`MOD_RES`	`328 328`		`Phosphoserine (By similarity).`
`MOD_RES`	`330 330`		`Phosphoserine (By similarity).`
`MOD_RES`	`365 365`		`Phosphoserine.`
`MOD_RES`	`368 368`		`Phosphoserine.`
`MOD_RES`	`369 369`		`Phosphoserine.`
`MOD_RES`	`373 373`		`Phosphoserine.`
`DISULFID`	`54 192`		`By similarity.`
`DISULFID`	`187 198`		`By similarity.`
`CONFLICT`	`2 2`		`G -> A (in Ref. 5; AA sequence).`
`CONFLICT`	`16 16`		`A -> T (in Ref. 2).`
`CONFLICT`	`28 28`		`V -> I (in Ref. 5; AA sequence).`
`TURN`	`256 259`	`4`
`STRAND`	`263 265`	`3`
`STRAND`	`297 300`	`4`
`HELIX`	`317 325`	`9`
`HELIX`	`342 348`	`7`
`TURN`	`349 352`	`4`
`STRAND`	`360 362`	`3`
`TURN`	`366 370`	`5`
`STRAND`	`376 380`	`5`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 43031 Da [This is the MW of the unprocessed precursor]

CRC64: 0196416EA6A69490 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG 

        70         80         90        100        110        120 
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG 

       130        140        150        160        170        180 
VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS 

       190        200        210        220        230        240 
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV 

       250        260        270        280        290        300 
KGRSDPYHAT TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN 

       310        320        330        340        350        360 
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNAKKVAAG HELQPLAIVD 

       370        380 
QRPSSRASSR ASSRPRPDDL EI

P08050 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools