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0CXA7_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGJA7
DescriptionGap junction alpha-7 protein (connexin 45) (cx45).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005921 gap junction (TAS)
0015285 connexon channel activity (TAS)
0007043 intercellular junction assembly (TAS)
0006936 muscle contraction (TAS)
0006810 transport (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions.ntracellular metabolites and messenger molecules (with molecular weight less than 1-2 kD) from the cytoplasm of one cell to its opposing neighbours. They are found in almost all vertebrate cell types.nd somewhat similar proteins have been cloned from plant species. Invertebrates utilise a different family of molecules.nnexins.hat share a similar predicted secondary structure to the vertebrate connexins.ut have no sequence identity to them . Vertebrate gap junction channels are thought to participate in diverse biological functions. For instance.n the heart they permit the rapid cell-cell transfer of action potentials.nsuring coordinated contraction of the cardiomyocytes. They are also responsible for neurotransmission at specialised electrical synapses. In non-excitable tissues.uch as the liver.hey may allow metabolic cooperation between cells. In the brain.lial cells are extensively-coupled by gap junctions; this allows waves of intracellular Ca2+ to propagate through nervous tissue.nd may contribute to their ability to spatially-buffer local changes in extracellular K+ concentration .The connexin protein family is encoded by at least 13 genes in rodents.ith many homologues cloned from other species. They show overlapping tissue expression patterns.ost tissues expressing more than one connexin type. Their conductances.ermeability to different molecules.hosphorylation and voltage-dependence of their gating.ave been found to vary. Possible communication diversity is increased further by the fact that gap junctions may be formed by the association of different connexin isoforms from apposing cells. However.n vitro studies have shown that not all possible combinations of connexins produce active channels .Hydropathy analysis predicts that all cloned connexins share a common transmembrane (TM) topology. Each connexin is thought to contain 4 TMdomains.ith two extracellular and three cytoplasmic regions. This modelhas been validated for several of the family members by in vitro biochemicalanalysis. Both N- and C-termini are thought to face the cytoplasm.nd thethird TM domain has an amphipathic character.uggesting that it contributesto the lining of the formed-channel. Amino acid sequence identity betweenthe isoforms is ~50-80%.ith the TM domains being well conserved. Bothextracellular loops contain characteristically conserved cysteine residues.hich likely form intramolecular disulphide bonds. By contrast.he singleputative intracellular loop (between TM domains 2 and 3) and the cytoplasmicC-terminus are highly variable among the family members.Six connexins arethought to associate to form a hemi-channel.r connexon. Two connexons theninteract (likely via the extracellular loops of their connexins) to form thecomplete gap junction channel.Two sets of nomenclature have been used to identify the connexins. Thefirst.nd most commonly used.lassifies the connexin molecules accordingto molecular weight.uch as connexin43 (abbreviated to Cx43).ndicatinga connexin of molecular weight close to 43 kD. However.tudies haverevealed cases where clear functional homologues exist across speciesthat have quite different molecular masses; therefore.n alternativenomenclature was proposed based on evolutionary considerations.hichdivides the family into two major subclasses.lpha and beta.ach with anumber of members . Due to their ubiquity and overlapping tissue distributions.t has proved difficult to elucidate the functions of individual connexin isoforms. To circumvent this problem.articular connexin-encoding genes have been subjected to targeted-disruption in mice.nd the phenotype of the resulting animals investigated. Around half the connexin isoforms have been investigated in this manner . Further insight into the functional roles of connexins has come from the discovery that a number of human diseases are caused by mutations in connexin genes. For instance.utations in Cx32 give rise to a form of inherited peripheral neuropathy called X-linked dominant Charcot-Marie-Tooth disease . Similarly.utations in Cx26 are responsible for both autosomal recessive and dominant forms of nonsyndromic deafness. disorder characterised by hearing loss.ith no apparent effects on other organ systems.
  IPR000500:Connexins
InterPro domains unassigned to SynO:
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions.ntracellular metabolites and messenger molecules (with molecular weight less than 1-2 kD) from the cytoplasm of one cell to its opposing neighbours. They are found in almost all vertebrate cell types.nd somewhat similar proteins have been cloned from plant species. Invertebrates utilise a different family of molecules.nnexins.hat share a similar predicted secondary structure to the vertebrate connexins.ut have no sequence identity to them . Vertebrate gap junction channels are thought to participate in diverse biological functions. For instance.n the heart they permit the rapid cell-cell transfer of action potentials.nsuring coordinated contraction of the cardiomyocytes. They are also responsible for neurotransmission at specialised electrical synapses. In non-excitable tissues.uch as the liver.hey may allow metabolic cooperation between cells. In the brain.lial cells are extensively-coupled by gap junctions; this allows waves of intracellular Ca2+ to propagate through nervous tissue.nd may contribute to their ability to spatially-buffer local changes in extracellular K+ concentration .The connexin protein family is encoded by at least 13 genes in rodents.ith many homologues cloned from other species. They show overlapping tissue expression patterns.ost tissues expressing more than one connexin type. Their conductances.ermeability to different molecules.hosphorylation and voltage-dependence of their gating.ave been found to vary. Possible communication diversity is increased further by the fact that gap junctions may be formed by the association of different connexin isoforms from apposing cells. However.n vitro studies have shown that not all possible combinations of connexins produce active channels .Hydropathy analysis predicts that all cloned connexins share a common transmembrane (TM) topology. Each connexin is thought to contain 4 TMdomains.ith two extracellular and three cytoplasmic regions. This modelhas been validated for several of the family members by in vitro biochemicalanalysis. Both N- and C-termini are thought to face the cytoplasm.nd thethird TM domain has an amphipathic character.uggesting that it contributesto the lining of the formed-channel. Amino acid sequence identity betweenthe isoforms is ~50-80%.ith the TM domains being well conserved. Bothextracellular loops contain characteristically conserved cysteine residues.hich likely form intramolecular disulphide bonds. By contrast.he singleputative intracellular loop (between TM domains 2 and 3) and the cytoplasmicC-terminus are highly variable among the family members.Six connexins arethought to associate to form a hemi-channel.r connexon. Two connexons theninteract (likely via the extracellular loops of their connexins) to form thecomplete gap junction channel.Two sets of nomenclature have been used to identify the connexins. Thefirst.nd most commonly used.lassifies the connexin molecules accordingto molecular weight.uch as connexin43 (abbreviated to Cx43).ndicatinga connexin of molecular weight close to 43 kD. However.tudies haverevealed cases where clear functional homologues exist across speciesthat have quite different molecular masses; therefore.n alternativenomenclature was proposed based on evolutionary considerations.hichdivides the family into two major subclasses.lpha and beta.ach with anumber of members . Due to their ubiquity and overlapping tissue distributions.t has proved difficult to elucidate the functions of individual connexin isoforms. To circumvent this problem.articular connexin-encoding genes have been subjected to targeted-disruption in mice.nd the phenotype of the resulting animals investigated. Around half the connexin isoforms have been investigated in this manner . Further insight into the functional roles of connexins has come from the discovery that a number of human diseases are caused by mutations in connexin genes. For instance.utations in Cx32 give rise to a form of inherited peripheral neuropathy called X-linked dominant Charcot-Marie-Tooth disease . Similarly.utations in Cx26 are responsible for both autosomal recessive and dominant forms of nonsyndromic deafness. disorder characterised by hearing loss.ith no apparent effects on other organ systems.This domain is found in the N-terminal region of these proteins.
  IPR013092:Connexin, N-terminal
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions.ntracellular metabolites and messenger molecules (with molecular weight less than 1-2 kD) from the cytoplasm of one cell to its opposing neighbours. They are found in almost all vertebrate cell types.nd somewhat similar proteins have been cloned from plant species. Invertebrates utilise a different family of molecules.nnexins.hat share a similar predicted secondary structure to the vertebrate connexins.ut have no sequence identity to them . Vertebrate gap junction channels are thought to participate in diverse biological functions. For instance.n the heart they permit the rapid cell-cell transfer of action potentials.nsuring coordinated contraction of the cardiomyocytes. They are also responsible for neurotransmission at specialised electrical synapses. In non-excitable tissues.uch as the liver.hey may allow metabolic cooperation between cells. In the brain.lial cells are extensively-coupled by gap junctions; this allows waves of intracellular Ca2+ to propagate through nervous tissue.nd may contribute to their ability to spatially-buffer local changes in extracellular K+ concentration .The connexin protein family is encoded by at least 13 genes in rodents.ith many homologues cloned from other species. They show overlapping tissue expression patterns.ost tissues expressing more than one connexin type. Their conductances.ermeability to different molecules.hosphorylation and voltage-dependence of their gating.ave been found to vary. Possible communication diversity is increased further by the fact that gap junctions may be formed by the association of different connexin isoforms from apposing cells. However.n vitro studies have shown that not all possible combinations of connexins produce active channels .Hydropathy analysis predicts that all cloned connexins share a common transmembrane (TM) topology. Each connexin is thought to contain 4 TMdomains.ith two extracellular and three cytoplasmic regions. This modelhas been validated for several of the family members by in vitro biochemicalanalysis. Both N- and C-termini are thought to face the cytoplasm.nd thethird TM domain has an amphipathic character.uggesting that it contributesto the lining of the formed-channel. Amino acid sequence identity betweenthe isoforms is ~50-80%.ith the TM domains being well conserved. Bothextracellular loops contain characteristically conserved cysteine residues.hich likely form intramolecular disulphide bonds. By contrast.he singleputative intracellular loop (between TM domains 2 and 3) and the cytoplasmicC-terminus are highly variable among the family members.Six connexins arethought to associate to form a hemi-channel.r connexon. Two connexons theninteract (likely via the extracellular loops of their connexins) to form thecomplete gap junction channel.Two sets of nomenclature have been used to identify the connexins. Thefirst.nd most commonly used.lassifies the connexin molecules accordingto molecular weight.uch as connexin43 (abbreviated to Cx43).ndicatinga connexin of molecular weight close to 43 kD. However.tudies haverevealed cases where clear functional homologues exist across speciesthat have quite different molecular masses; therefore.n alternativenomenclature was proposed based on evolutionary considerations.hichdivides the family into two major subclasses.lpha and beta.ach with anumber of members . Due to their ubiquity and overlapping tissue distributions.t has proved difficult to elucidate the functions of individual connexin isoforms. To circumvent this problem.articular connexin-encoding genes have been subjected to targeted-disruption in mice.nd the phenotype of the resulting animals investigated. Around half the connexin isoforms have been investigated in this manner . Further insight into the functional roles of connexins has come from the discovery that a number of human diseases are caused by mutations in connexin genes. For instance.utations in Cx32 give rise to a form of inherited peripheral neuropathy called X-linked dominant Charcot-Marie-Tooth disease . Similarly.utations in Cx26 are responsible for both autosomal recessive and dominant forms of nonsyndromic deafness. disorder characterised by hearing loss.ith no apparent effects on other organ systems.Gap junction alpha-6 protein (also called connexin45.r Cx45) is a connexinof 396 amino acid residues. It is one of four isoforms expressed in theheart (together with Cx43.x40 and Cx37). All four isoforms show differingdistribution patterns within the human heart: Cx45 tends to be detectableonly at rather low levels.ith a trend toward higher levels in the atriathan the ventricles. Cx45 is also thought to be involved in the formation ofgap junctions between the bone-forming cells.steoblasts; the extent oftheir cell-cell coupling may act to modulate their gene expression.
  IPR002265:Gap junction alpha-6 protein (Cx45)
IPR013092:Connexin 
Evalue:-146.585021972656 
Location:2-253IPR002265:CONNEXINA6 
Evalue:0 
Location:321-333IPR002265:CONNEXINA6 
Evalue:0 
Location:297-308IPR002265:CONNEXINA6 
Evalue:0 
Location:310-320
SequencesProtein: CXA7_HUMAN (396 aa)
mRNA: NM_005497
Local Annotation
Synapse Ontology
supporting cells of the nervous system. Glial cells in the brain and spinal cord far outnumber nerve cells. They not only provide physical support, but also respond to injury, regulate the chemical composition surrounding cells, participate in the blood-brain and blood-spinal-cord barriers, form the myelin insulation of nervous pathways, help guide neuronal migration during development, and exchange metabolites with neurons. They may also produce substances that help and hinder regeneration in the spinal cord. The major types of glial cells in the CNS are astrocytes, oligodendrocytes, and microglia.
sdb:0008 Glia  (Evidence:domains)
A neuromuscular junction is the junction of the axon terminal of a motoneuron with the motor end plate, the highly-excitable region of muscle fiber plasma membrane responsible for initiation of action potentials across the muscle's surface.
sdb:0024 neuromuscular junction  (Evidence:domains)
KO assignmentK07616
  Level 3 annotation:
    gap junction protein, alpha 7
  Level 2 annotation:
    Membrane and intracellular structural molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 540 residues, 40237112-40238731Exon2: 27 residues, 40240287-40240363Exon3: 66 residues, 40262955-40263147Exon4: 2 residues, -Jump to CXA7_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4294 39509646-39556540 ~-47K 15975(HDAC5)(-)Loci: 4295 39682565-39700993 ~-18K 15992(SLC4A1)(-)Loci: 4296 39752520-39757666 ~-5K 15997(-)Loci: 3010 40098011-40104116 ~-6K 16007(+)Loci: 4297 40237112-40263147 ~-26K 16016(GJA7)(-)Loci: 4298 40338518-40348394 ~-10K 16022(GFAP)(-)Loci: 3009 39437557-39441961 ~-4K 15971(NAGS)(+)Link out to UCSC