Gap junction alpha-1 protein - Rattus norvegicus (Rat)

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P08050 (CXA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Gap junction alpha-1 protein

Alternative name(s):
Connexin-43
Short name=Cx43
Gap junction 43 kDa heart protein

Gene names

Name:	Gja1
Synonyms:	Cxn-43

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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 structure	A connexon is composed of a hexamer of connexins. Interacts with SGSM3. Interacts with KIAA1432/CIP150. Interacts with CNST and CSNK1D By similarity. Interacts (via C-terminus) with TJP1. Interacts (via C-terminus) with SRC (via SH3 domain). Ref.10 Ref.11
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › gap junction Ref.11.
Post-translational modification	Contains at least one intramolecular disulfide bond. 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. Ref.9
Sequence similarities	Belongs to the connexin family. Alpha-type (group II) subfamily.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Gap junction Membrane
Domain	Transmembrane Transmembrane helix
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP transport Inferred from mutant phenotype. Source: RGD apoptotic process Inferred from mutant phenotype. Source: RGD cell-cell signaling Inferred from direct assay. Source: RGD gap junction assembly Traceable author statement. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay. Source: RGD neuron projection morphogenesis Inferred from mutant phenotype. Source: RGD positive regulation of protein catabolic process Inferred from direct assay. Source: RGD protein oligomerization Inferred from direct assay. Source: RGD regulation of calcium ion transport Inferred from mutant phenotype. Source: RGD response to pH Inferred from direct assay. Source: RGD response to peptide hormone stimulus Inferred from expression pattern. Source: RGD vascular transport Inferred from mutant phenotype. Source: RGD
Cellular component	Golgi-associated vesicle membrane Traceable author statement. Source: Reactome connexon complex Inferred from direct assay. Source: RGD early endosome Inferred from direct assay. Source: RGD endoplasmic reticulum membrane Traceable author statement. Source: Reactome fascia adherens Inferred from direct assay. Source: RGD integral to plasma membrane Traceable author statement. Source: UniProtKB lysosome Inferred from direct assay. Source: RGD membrane fraction Inferred from direct assay. Source: MGI membrane raft Inferred from direct assay. Source: BHF-UCL mitochondrial outer membrane Inferred from direct assay. Source: RGD multivesicular body Inferred from direct assay. Source: RGD
Molecular function	PDZ domain binding Inferred from physical interaction. Source: RGD SH3 domain binding Inferred from physical interaction. Source: RGD gap junction channel activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sgsm3	Q8VCZ6	4	EBI-476947,EBI-525155	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5 Ref.6

Chain

2 – 382

381

Gap junction alpha-1 protein

PRO_0000057804

Regions

Topological domain

2 – 13

Cytoplasmic Probable

Transmembrane

14 – 36

Helical; Probable

Topological domain

37 – 76

Extracellular Probable

Transmembrane

77 – 99

Helical; Probable

Topological domain

100 – 154

Cytoplasmic Probable

Transmembrane

155 – 177

Helical; Probable

Topological domain

178 – 208

Extracellular Probable

Transmembrane

209 – 231

Helical; Probable

Topological domain

232 – 382

151

Cytoplasmic Probable

Amino acid modifications

Modified residue

247

Phosphotyrosine By similarity

Modified residue

306

Phosphoserine By similarity

Modified residue

313

Phosphotyrosine By similarity

Modified residue

314

Phosphoserine By similarity

Modified residue

325

Phosphoserine; by CK1 By similarity

Modified residue

326

Phosphothreonine By similarity

Modified residue

328

Phosphoserine; by CK1 By similarity

Modified residue

330

Phosphoserine; by CK1 By similarity

Modified residue

365

Phosphoserine Ref.9

Modified residue

368

Phosphoserine; by PKC/PRKCG Probable

Modified residue

369

Phosphoserine Ref.9

Modified residue

373

Phosphoserine Ref.9

Disulfide bond

54 ↔ 192

By similarity

Disulfide bond

187 ↔ 198

By similarity

Experimental info

Sequence conflict

G → A AA sequence Ref.5

Sequence conflict

A → T no nucleotide entry Ref.2

Sequence conflict

V → I AA sequence Ref.5

Secondary structure

382

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08050 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0196416EA6A69490
Show »

FASTA

382

43,031

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Connexin43: a protein from rat heart homologous to a gap junction protein from liver." Beyer E.C., Paul D.L., Goodenough D.A. J. Cell Biol. 105:2621-2629(1987) [PubMed: 2826492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of a rat uterine gap junction protein and analysis of gene expression during gestation." Lang L.M., Beyer E.C., Schwartz A.L., Gitlin J.D. Am. J. Physiol. 260:E787-E793(1991) [PubMed: 1852114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Uterus.
[3]	Ma L.X., Peng Y.W. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[5]	"The Mr 28,000 gap junction proteins from rat heart and liver are different but related." Nicholson B.J., Gros D.B., Kent S.B.H., Hood L.E., Revel J.-P. J. Biol. Chem. 260:6514-6517(1985) [PubMed: 2987225] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-33. Tissue: Heart.
[6]	"Affinity purification of a rat-brain junctional protein, connexin 43." Dupont E., el Aoumari A., Fromaget C., Briand J.-C., Gros D. Eur. J. Biochem. 200:263-270(1991) [PubMed: 1652440] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Tissue: Brain.
[7]	"Connexon integrity is maintained by non-covalent bonds: intramolecular disulfide bonds link the extracellular domains in rat connexin-43." John S.A., Revel J.-P. Biochem. Biophys. Res. Commun. 178:1312-1318(1991) [PubMed: 1651718] [Abstract] Cited for: DISULFIDE BONDS.
[8]	"Membrane topology and quaternary structure of cardiac gap junction ion channels." Yeager M., Gilula N.B. J. Mol. Biol. 223:929-948(1992) [PubMed: 1371548] [Abstract] Cited for: TOPOLOGY.
[9]	"Identification and functional analysis of novel phosphorylation sites in Cx43 in rat primary granulosa cells." Yogo K., Ogawa T., Akiyama M., Ishida N., Takeya T. FEBS Lett. 531:132-136(2002) [PubMed: 12417300] [Abstract] Cited for: PHOSPHORYLATION AT SER-365; SER-368; SER-369 AND SER-373.
[10]	"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1." Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C. J. Biol. Chem. 279:54695-54701(2004) [PubMed: 15492000] [Abstract] Cited for: STRUCTURE BY NMR OF 255-381, INTERACTION WITH TJP1 AND SRC.
[11]	"Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites." Chen J., Pan L., Wei Z., Zhao Y., Zhang M. EMBO J. 27:2113-2123(2008) [PubMed: 18636092] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 374-382 IN COMPLEX WITH TJP1, SUBCELLULAR LOCATION, INTERACTION WITH TJP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06656 mRNA. Translation: CAA29855.1.
AY324140 mRNA. Translation: AAP88589.1.
BC081842 mRNA. Translation: AAH81842.1.

IPI

IPI00231746.

PIR

A24047.
S00532.

RefSeq

NP_036699.1. NM_012567.2.

UniGene

Rn.10346.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R5S	NMR	-	A	255-381	[»]
3CYY	X-ray	2.40	C/D	374-382	[»]

ProteinModelPortal

P08050.

SMR

P08050. Positions 252-382.

DisProt

DP00278.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34793N.

IntAct

P08050. 4 interactions.

STRING

P08050.

Protein family/group databases

TCDB

1.A.24.1.1. gap junction-forming connexin family.

PTM databases

PhosphoSite

P08050.

Proteomic databases

PRIDE

P08050.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000001054; ENSRNOP00000001054; ENSRNOG00000000805.

GeneID

24392.

KEGG

rno:24392.

UCSC

NM_012567. rat.

Organism-specific databases

CTD

2697.

RGD

2690. Gja1.

Phylogenomic databases

eggNOG

maNOG05724.

HOVERGEN

HBG009576.

InParanoid

P08050.

OMA

TDGANVD.

OrthoDB

EOG402WSC.

Enzyme and pathway databases

Reactome

REACT_12587. Transport of connexins along the secretory pathway.
REACT_97881. Membrane Trafficking.

Gene expression databases

ArrayExpress

P08050.

Genevestigator

P08050.

GermOnline

ENSRNOG00000000805. Rattus norvegicus.

Family and domain databases

InterPro

IPR000500. Connexin.
IPR002261. Connexin43.
IPR013124. Connexin43_C.
IPR019570. Connexin_CCC.
IPR017990. Connexin_CS.
IPR013092. Connexin_N.
[Graphical view]

K07372.

PANTHER

PTHR11984. Connexin. 1 hit.

Pfam

PF00029. Connexin. 1 hit.
PF03508. Connexin43. 1 hit.
PF10582. Connexin_CCC. 1 hit.
[Graphical view]

PRINTS

PR00206. CONNEXIN.
PR01132. CONNEXINA1.

SMART

SM00037. CNX. 1 hit.
SM01089. Connexin_CCC. 1 hit.
[Graphical view]

PROSITE

PS00407. CONNEXINS_1. 1 hit.
PS00408. CONNEXINS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

603181.

Entry information

Entry name

CXA1_RAT

Accession

Primary (citable) accession number: P08050
Secondary accession number(s): Q53ZE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents