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P08050

- CXA1_RAT

UniProt

P08050 - CXA1_RAT

Protein

Gap junction alpha-1 protein

Gene

Gja1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 By similarity.By similarity

    GO - Molecular functioni

    1. connexin binding Source: RGD
    2. gap junction channel activity Source: RGD
    3. PDZ domain binding Source: RGD
    4. protein binding Source: IntAct
    5. protein domain specific binding Source: RGD
    6. SH3 domain binding Source: RGD
    7. signal transducer activity Source: Ensembl

    GO - Biological processi

    1. adult heart development Source: Ensembl
    2. apoptotic process Source: RGD
    3. ATP transport Source: RGD
    4. atrial ventricular junction remodeling Source: Ensembl
    5. blood vessel morphogenesis Source: Ensembl
    6. cardiac conduction Source: Ensembl
    7. cell-cell signaling Source: RGD
    8. cell communication Source: RGD
    9. cell communication by chemical coupling Source: Ensembl
    10. cell communication by electrical coupling Source: Ensembl
    11. cellular response to mechanical stimulus Source: RGD
    12. chronic inflammatory response Source: RGD
    13. embryonic digit morphogenesis Source: Ensembl
    14. endothelium development Source: RGD
    15. epithelial cell maturation Source: Ensembl
    16. gap junction assembly Source: UniProtKB
    17. heart development Source: RGD
    18. heart looping Source: Ensembl
    19. in utero embryonic development Source: Ensembl
    20. lens development in camera-type eye Source: Ensembl
    21. milk ejection Source: Ensembl
    22. negative regulation of cardiac muscle cell proliferation Source: RGD
    23. negative regulation of cell proliferation Source: RGD
    24. negative regulation of DNA biosynthetic process Source: RGD
    25. negative regulation of endothelial cell proliferation Source: RGD
    26. negative regulation of gene expression Source: Ensembl
    27. negative regulation of wound healing Source: RGD
    28. neuron migration Source: Ensembl
    29. neuron projection morphogenesis Source: RGD
    30. osteoblast differentiation Source: Ensembl
    31. positive regulation of behavioral fear response Source: RGD
    32. positive regulation of cell communication by chemical coupling Source: RGD
    33. positive regulation of cytosolic calcium ion concentration Source: RGD
    34. positive regulation of gene expression Source: Ensembl
    35. positive regulation of glomerular filtration Source: RGD
    36. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    37. positive regulation of insulin secretion Source: RGD
    38. positive regulation of protein catabolic process Source: RGD
    39. positive regulation of striated muscle tissue development Source: Ensembl
    40. positive regulation of vasoconstriction Source: RGD
    41. positive regulation of vasodilation Source: RGD
    42. protein oligomerization Source: RGD
    43. regulation of atrial cardiac muscle cell membrane depolarization Source: Ensembl
    44. regulation of bone mineralization Source: Ensembl
    45. regulation of bone remodeling Source: Ensembl
    46. regulation of calcium ion transport Source: RGD
    47. regulation of tight junction assembly Source: RGD
    48. regulation of ventricular cardiac muscle cell membrane depolarization Source: Ensembl
    49. regulation of ventricular cardiac muscle cell membrane repolarization Source: Ensembl
    50. response to fluid shear stress Source: RGD
    51. response to glucose Source: RGD
    52. response to peptide hormone Source: RGD
    53. response to pH Source: RGD
    54. skeletal muscle tissue regeneration Source: Ensembl
    55. transmembrane transport Source: RGD
    56. vascular transport Source: RGD

    Protein family/group databases

    TCDBi1.A.24.1.1. the gap junction-forming connexin (connexin) family.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 20

    Organism-specific databases

    RGDi2690. Gja1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell junctiongap junction 1 Publication

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. connexon complex Source: RGD
    3. contractile fiber Source: Ensembl
    4. cytoplasm Source: RGD
    5. cytosol Source: Ensembl
    6. early endosome Source: RGD
    7. endoplasmic reticulum membrane Source: Reactome
    8. endosome Source: RGD
    9. fascia adherens Source: RGD
    10. gap junction Source: UniProtKB
    11. Golgi apparatus Source: BHF-UCL
    12. Golgi-associated vesicle membrane Source: Reactome
    13. Golgi membrane Source: Reactome
    14. integral component of plasma membrane Source: UniProtKB
    15. intermediate filament Source: Ensembl
    16. late endosome Source: RGD
    17. lateral plasma membrane Source: Ensembl
    18. lysosome Source: RGD
    19. membrane Source: MGI
    20. membrane raft Source: BHF-UCL
    21. mitochondrial outer membrane Source: RGD
    22. multivesicular body Source: RGD
    23. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Gap junction, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 382381Gap junction alpha-1 proteinPRO_0000057804Add
    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 – 2471PhosphotyrosineBy similarity
    Modified residuei255 – 2551PhosphoserineBy similarity
    Modified residuei262 – 2621PhosphoserineBy similarity
    Modified residuei271 – 2711S-nitrosocysteineBy similarity
    Modified residuei306 – 3061PhosphoserineBy similarity
    Modified residuei314 – 3141PhosphoserineBy similarity
    Modified residuei325 – 3251Phosphoserine; by CK1By similarity
    Modified residuei328 – 3281Phosphoserine; by CK1By similarity
    Modified residuei330 – 3301Phosphoserine; by CK1By similarity
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei368 – 3681Phosphoserine; by PKC/PRKCG1 Publication
    Modified residuei369 – 3691Phosphoserine1 Publication
    Modified residuei373 – 3731Phosphoserine1 Publication

    Post-translational modificationi

    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.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.

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP08050.
    PRIDEiP08050.

    PTM databases

    PhosphoSiteiP08050.

    Expressioni

    Inductioni

    In bladder smooth muscle cells, exhibits night/day variations with low levels during the sleep phase, at circadian time (CT) 4-8 (at protein level). Expression starts to increase around CT12 and forms a plateau during the active phase (CT16-24) (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP08050.
    GenevestigatoriP08050.

    Interactioni

    Subunit structurei

    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). Interacts with UBQLN4.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sgsm3Q8VCZ64EBI-476947,EBI-525155From a different organism.

    Protein-protein interaction databases

    BioGridi246562. 116 interactions.
    DIPiDIP-34793N.
    IntActiP08050. 8 interactions.
    MINTiMINT-1791096.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni256 – 2594
    Beta strandi263 – 2653
    Beta strandi297 – 3004
    Helixi317 – 3259
    Helixi342 – 3487
    Turni349 – 3524
    Beta strandi360 – 3623
    Turni366 – 3705
    Beta strandi379 – 3813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R5SNMR-A255-382[»]
    3CYYX-ray2.40C/D374-382[»]
    DisProtiDP00278.
    ProteinModelPortaliP08050.
    SMRiP08050. Positions 252-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08050.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1312Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini37 – 7640Extracellular1 PublicationAdd
    BLAST
    Topological domaini100 – 15455Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini178 – 20831Extracellular1 PublicationAdd
    BLAST
    Topological domaini232 – 382151Cytoplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3623HelicalCuratedAdd
    BLAST
    Transmembranei77 – 9923HelicalCuratedAdd
    BLAST
    Transmembranei155 – 17723HelicalCuratedAdd
    BLAST
    Transmembranei209 – 23123HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG45368.
    GeneTreeiENSGT00740000115305.
    HOGENOMiHOG000231127.
    HOVERGENiHBG009576.
    InParanoidiP08050.
    KOiK07372.
    OMAiGANVDMH.
    OrthoDBiEOG7P2XSS.
    PhylomeDBiP08050.
    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.

    P08050-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS    50
    AFRCNTQQPG CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM 100
    RKEEKLNKKE EELKVAQTDG VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG 150
    LLRTYIISIL FKSVFEVAFL LIQWYIYGFS LSAVYTCKRD PCPHQVDCFL 200
    SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV KGRSDPYHAT 250
    TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN 300
    YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNAKKVAAG 350
    HELQPLAIVD QRPSSRASSR ASSRPRPDDL EI 382
    Length:382
    Mass (Da):43,031
    Last modified:January 23, 2007 - v2
    Checksum:i0196416EA6A69490
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → A AA sequence (PubMed:2987225)Curated
    Sequence conflicti16 – 161A → T no nucleotide entry (PubMed:1852114)Curated
    Sequence conflicti28 – 281V → I AA sequence (PubMed:2987225)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06656 mRNA. Translation: CAA29855.1.
    AY324140 mRNA. Translation: AAP88589.1.
    BC081842 mRNA. Translation: AAH81842.1.
    PIRiA24047.
    S00532.
    RefSeqiNP_036699.1. NM_012567.2.
    XP_006256564.1. XM_006256502.1.
    XP_006256565.1. XM_006256503.1.
    UniGeneiRn.10346.

    Genome annotation databases

    EnsembliENSRNOT00000001054; ENSRNOP00000001054; ENSRNOG00000000805.
    GeneIDi24392.
    KEGGirno:24392.
    UCSCiRGD:2690. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06656 mRNA. Translation: CAA29855.1 .
    AY324140 mRNA. Translation: AAP88589.1 .
    BC081842 mRNA. Translation: AAH81842.1 .
    PIRi A24047.
    S00532.
    RefSeqi NP_036699.1. NM_012567.2.
    XP_006256564.1. XM_006256502.1.
    XP_006256565.1. XM_006256503.1.
    UniGenei Rn.10346.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R5S NMR - A 255-382 [» ]
    3CYY X-ray 2.40 C/D 374-382 [» ]
    DisProti DP00278.
    ProteinModelPortali P08050.
    SMRi P08050. Positions 252-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246562. 116 interactions.
    DIPi DIP-34793N.
    IntActi P08050. 8 interactions.
    MINTi MINT-1791096.

    Protein family/group databases

    TCDBi 1.A.24.1.1. the gap junction-forming connexin (connexin) family.

    PTM databases

    PhosphoSitei P08050.

    Proteomic databases

    PaxDbi P08050.
    PRIDEi P08050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000001054 ; ENSRNOP00000001054 ; ENSRNOG00000000805 .
    GeneIDi 24392.
    KEGGi rno:24392.
    UCSCi RGD:2690. rat.

    Organism-specific databases

    CTDi 2697.
    RGDi 2690. Gja1.

    Phylogenomic databases

    eggNOGi NOG45368.
    GeneTreei ENSGT00740000115305.
    HOGENOMi HOG000231127.
    HOVERGENi HBG009576.
    InParanoidi P08050.
    KOi K07372.
    OMAi GANVDMH.
    OrthoDBi EOG7P2XSS.
    PhylomeDBi P08050.
    TreeFami TF329606.

    Miscellaneous databases

    EvolutionaryTracei P08050.
    NextBioi 603181.
    PROi P08050.

    Gene expression databases

    ArrayExpressi P08050.
    Genevestigatori P08050.

    Family and domain databases

    InterProi IPR000500. Connexin.
    IPR002261. Connexin43.
    IPR013124. Connexin43_C.
    IPR019570. Connexin_CCC.
    IPR017990. Connexin_CS.
    IPR013092. Connexin_N.
    [Graphical view ]
    PANTHERi PTHR11984. PTHR11984. 1 hit.
    Pfami PF00029. Connexin. 1 hit.
    PF03508. Connexin43. 1 hit.
    PF10582. Connexin_CCC. 1 hit.
    [Graphical view ]
    PRINTSi PR00206. CONNEXIN.
    PR01132. CONNEXINA1.
    SMARTi SM00037. CNX. 1 hit.
    SM01089. Connexin_CCC. 1 hit.
    [Graphical view ]
    PROSITEi PS00407. CONNEXINS_1. 1 hit.
    PS00408. CONNEXINS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-365; SER-368; SER-369 AND SER-373.
    10. Cited for: INTERACTION WITH UBQLN4.
    11. "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: INDUCTION.
    12. "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] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 255-381, INTERACTION WITH TJP1 AND SRC.
    13. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 374-382 IN COMPLEX WITH TJP1, SUBCELLULAR LOCATION, INTERACTION WITH TJP1.

    Entry informationi

    Entry nameiCXA1_RAT
    AccessioniPrimary (citable) accession number: P08050
    Secondary accession number(s): Q53ZE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3