GJC2

gap junction protein, gamma 2, 47kDa

Identifiers

GJC2; PMLDAR; MGC105119; HLD2; Cx47; SPG44; GJA12

External IDs

OMIM: 608803 MGI: 2153060 HomoloGene: 10715 GeneCards: GJC2 Gene

Gene Ontology
Molecular function	• gap junction channel activity • receptor binding • endonuclease activity
Cellular component	• gap junction • connexon complex • integral to membrane • cell junction • plasma membrane
Biological process	• cytolysis • cell communication • cell-cell signaling • pathogenesis • response to bacterium
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
226.4 – 226.41 Mb

Chr 11:
58.99 – 59 Mb

PubMed search

[1]

[2]

Gap junction gamma-2 (GJC2), also known as connexin-46.6 (Cx46.6) and connexin-47 (Cx47) and gap junction alpha-12 (GJA12), is a protein that in humans is encoded by the GJC2 gene.^[1]

1 Function
2 Clinical significance
3 References
4 Further reading

Function

This gene encodes a gap junction protein. Gap junction proteins are members of a large family of homologous connexins and comprise 4 transmembrane, 2 extracellular, and 3 cytoplasmic domains. This gene plays a key role in central myelination and is involved in peripheral myelination in humans.^[1]

Clinical significance

Defects in this gene are the cause of autosomal recessive Pelizaeus-Merzbacher-like disease-1.^[1]

References

^ ^a ^b ^c "Entrez Gene: gap junction protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57165.

Ostergaard P, Simpson MA, Brice G, et al. (2011). "Rapid identification of mutations in GJC2 in primary lymphoedema using whole exome sequencing combined with linkage analysis with delineation of the phenotype.". J. Med. Genet. 48 (4): 251–5. doi:10.1136/jmg.2010.085563. PMID 21266381.
Odermatt B, Wellershaus K, Wallraff A, et al. (2003). "Connexin 47 (Cx47)-deficient mice with enhanced green fluorescent protein reporter gene reveal predominant oligodendrocytic expression of Cx47 and display vacuolized myelin in the CNS.". J. Neurosci. 23 (11): 4549–59. PMID 12805295.
Menichella DM, Goodenough DA, Sirkowski E, et al. (2003). "Connexins are critical for normal myelination in the CNS.". J. Neurosci. 23 (13): 5963–73. PMID 12843301.
Salviati L, Trevisson E, Baldoin MC, et al. (2007). "A novel deletion in the GJA12 gene causes Pelizaeus-Merzbacher-like disease.". Neurogenetics 8 (1): 57–60. doi:10.1007/s10048-006-0065-x. PMID 17031678.
Ferrell RE, Baty CJ, Kimak MA, et al. (2010). "GJC2 missense mutations cause human lymphedema.". Am. J. Hum. Genet. 86 (6): 943–8. doi:10.1016/j.ajhg.2010.04.010. PMID 20537300.
Uhlenberg B, Schuelke M, Rüschendorf F, et al. (2004). "Mutations in the gene encoding gap junction protein alpha 12 (connexin 46.6) cause Pelizaeus-Merzbacher-like disease.". Am. J. Hum. Genet. 75 (2): 251–60. doi:10.1086/422763. PMC 1216059. PMID 15192806. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1216059.
Orthmann-Murphy JL, Salsano E, Abrams CK, et al. (2009). "Hereditary spastic paraplegia is a novel phenotype for GJA12/GJC2 mutations.". Brain 132 (Pt 2): 426–38. doi:10.1093/brain/awn328. PMID 19056803.
Wang J, Wang H, Wang Y, et al. (2010). "Two novel gap junction protein alpha 12 gene mutations in two Chinese patients with Pelizaeus-Merzbacher-like disease.". Brain Dev. 32 (3): 236–43. doi:10.1016/j.braindev.2009.03.013. PMID 19423250.
Henneke M, Combes P, Diekmann S, et al. (2008). "GJA12 mutations are a rare cause of Pelizaeus-Merzbacher-like disease.". Neurology 70 (10): 748–54. doi:10.1212/01.wnl.0000284828.84464.35. PMID 18094336.
Orthmann-Murphy JL, Enriquez AD, Abrams CK, Scherer SS (2007). "Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus-Merzbacher-like disease.". Mol. Cell. Neurosci. 34 (4): 629–41. doi:10.1016/j.mcn.2007.01.010. PMID 17344063.
Ruf N, Uhlenberg B (2009). "Analysis of human alternative first exons and copy number variation of the GJA12 gene in patients with Pelizaeus-Merzbacher-like disease.". Am. J. Med. Genet. B Neuropsychiatr. Genet. 150B (2): 226–32. doi:10.1002/ajmg.b.30792. PMID 18521858.
Wolf NI, Cundall M, Rutland P, et al. (2007). "Frameshift mutation in GJA12 leading to nystagmus, spastic ataxia and CNS dys-/demyelination.". Neurogenetics 8 (1): 39–44. doi:10.1007/s10048-006-0062-0. PMID 16969684.
Ishikawa T, Sato K, Shimazaki R, et al. (2010). "[A case of autosomal recessive hypomyelinating leukodystrophy without GJA12 mutation presenting a novel phenotype].". Rinsho Shinkeigaku 50 (1): 7–11. PMID 20120347.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Voltage-gated	L-type/Ca_vα (1.1, 1.2, 1.3, 1.4) · N-type/Ca_vα2.2 · P-type/Ca_vα(2.1) · Q-type/Ca_vα2.1 · R-type/Ca_vα2.3 · T-type/Ca_vα(3.1, 3.2, 3.3) α₂δ-subunits (1, 2) · β-subunits (β1, β2, β3, β4) · γ-subunits (γ1, γ2, γ3, γ4) Cation channels of sperm (1, 2, 3, 4) · Two-pore channel (1, 2)

Ligand-gated	Inositol trisphosphate receptor (1, 2, 3) · Ryanodine receptor (1, 2, 3)

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel (α, β, γ, δ)

Proton gated	Amiloride-sensitive cation channel (1, 2, 3, 4)

Voltage-gated	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Na_vβ (1, 2, 3, 4)

K⁺: Potassium channel

Voltage-gated	K_vα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (2.1, 2.2) · (3.1, 3.2, 3.3, 3.4) · (4.1, 4.2, 4.3) · (5.1) · (6.1, 6.2, 6.3, 6.4) K_vα7-12 (7.1, 7.2, 7.3, 7.4, 7.5) · (8.1, 8.2) · (9.1, 9.2, 9.3) · (10.1, 10.2) · (11.1/hERG, 11.2, 11.3) · (12.1, 12.2, 12.3) K_vβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene

Calcium-activated	BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3, SK4) · K_Ca (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1)

Inward-rectifier	K_ATP · K_ir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/K_ir (3.1, 3.2, 3.3, 3.4) · K_ir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)

Tandem pore domain	K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)

Other

Cl^-: Chloride channel	ANO1 · Bestrophin (1, 2) · CFTR · CLCA (1, 2, 3, 4) · CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) · CLIC (1, 2, 3, 4, 5, 6, L1) · CLNS (1A, 1B)

H⁺: Voltage-gated	HVCN1

M⁺: TRP cation channel	TRPA (1) · TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) · TRPM (1, 2, 3, 4, 5, 6, 7, 8) · TRPML (1, 2, 3) · TRPN · TRPP (1, 2) · TRPV (1, 2, 3, 4, 5, 6)

Cyclic nucleotide-gated (FC)	α (1, 2, 3, 4) · β (1, 2, 3) · HCN (1, 2, 3, 4)

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) · Voltage-dependent anion channel (1, 2, 3) · General bacterial porin family

Gap junction	Connexin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) · B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) · C (GJC1, GJC2, GJC3) · D (GJD2, GJD3, GJD4)) Innexin

General	Ligand-gated ion channel · Voltage-gated ion channel · Stretch-activated ion channel

see also disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

GJC2

Contents

Function

Clinical significance

References

Further reading