GJA4

Identifiers

GJA4, CX37, gap junction protein alpha 4

External IDs

MGI: 95715 HomoloGene: 1556 GeneCards: GJA4

Targeted by Drug

carbenoxolone, flufenamic acid, caprylic alcohol^[1]

Gene ontology
Molecular function	• protein binding
Cellular component	• integral component of membrane • gap junction • cell junction • plasma membrane • integral component of plasma membrane • connexin complex • membrane
Biological process	• cell communication • cell-cell signaling • blood vessel development • response to pain • calcium ion transport • cell-cell junction assembly • endothelium development • transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2701


14612

Ensembl


ENSG00000187513


ENSMUSG00000050234

UniProt


P35212


P28235

RefSeq (mRNA)


NM_002060


NM_008120

RefSeq (protein)


NP_002051.2


NP_032146.1

Location (UCSC)

Chr 1: 34.79 – 34.8 Mb

Chr 4: 127.31 – 127.31 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Gap junction alpha-4 protein is a protein that in humans is encoded by the GJA4 gene.^[4]^[5]^[6]

References

↑ "Drugs that physically interact with Gap junction alpha-4 protein view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Richard G, Smith LE, Bailey RA, Itin P, Hohl D, Epstein EH Jr, DiGiovanna JJ, Compton JG, Bale SJ (Dec 1998). "Mutations in the human connexin gene GJB3 cause erythrokeratodermia variabilis". Nat Genet. 20 (4): 366–9. doi:10.1038/3840. PMID 9843209.
↑ Reed KE, Westphale EM, Larson DM, Wang HZ, Veenstra RD, Beyer EC (Apr 1993). "Molecular cloning and functional expression of human connexin37, an endothelial cell gap junction protein". J Clin Invest. 91 (3): 997–1004. doi:10.1172/JCI116321. PMC 288052. PMID 7680674.
↑ "Entrez Gene: GJA4 gap junction protein, alpha 4, 37kDa".

Andrew L Harris; Darren Locke (2009). Connexins, A Guide. New York: Springer. p. 574. ISBN 978-1-934115-46-6.
Beyer EC, Paul DL, Goodenough DA (1990). "Connexin family of gap junction proteins". J. Membr. Biol. 116 (3): 187–94. doi:10.1007/BF01868459. PMID 2167375.
Haefliger JA, Bruzzone R, Jenkins NA, et al. (1992). "Four novel members of the connexin family of gap junction proteins. Molecular cloning, expression, and chromosome mapping". J. Biol. Chem. 267 (3): 2057–64. PMID 1370487.
Risek B, Guthrie S, Kumar N, Gilula NB (1990). "Modulation of gap junction transcript and protein expression during pregnancy in the rat". J. Cell Biol. 110 (2): 269–82. doi:10.1083/jcb.110.2.269. PMC 2116004. PMID 1688855.
Willecke K, Jungbluth S, Dahl E, et al. (1991). "Six genes of the human connexin gene family coding for gap junctional proteins are assigned to four different human chromosomes". Eur. J. Cell Biol. 53 (2): 275–80. PMID 1964417.
Van Camp G, Coucke P, Speleman F, et al. (1996). "The gene for human gap junction protein connexin37 (GJA4) maps to chromosome 1p35.1, in the vicinity of D1S195". Genomics. 30 (2): 402–3. PMID 8586454.
Krutovskikh V, Mironov N, Yamasaki H (1996). "Human connexin 37 is polymorphic but not mutated in tumours". Carcinogenesis. 17 (8): 1761–3. doi:10.1093/carcin/17.8.1761. PMID 8761439.
Simon AM, Goodenough DA, Li E, Paul DL (1997). "Female infertility in mice lacking connexin 37". Nature. 385 (6616): 525–9. doi:10.1038/385525a0. PMID 9020357.
Krenacs T, Rosendaal M (1998). "Connexin43 gap junctions in normal, regenerating, and cultured mouse bone marrow and in human leukemias: their possible involvement in blood formation". Am. J. Pathol. 152 (4): 993–1004. PMC 1858239. PMID 9546360.
van Rijen HV, van Kempen MJ, Postma S, Jongsma HJ (1998). "Tumour necrosis factor alpha alters the expression of connexin43, connexin40, and connexin37 in human umbilical vein endothelial cells". Cytokine. 10 (4): 258–64. doi:10.1006/cyto.1997.0287. PMID 9617570.
Boerma M, Forsberg L, Van Zeijl L, et al. (1999). "A genetic polymorphism in connexin 37 as a prognostic marker for atherosclerotic plaque development". J. Intern. Med. 246 (2): 211–8. doi:10.1046/j.1365-2796.1999.00564.x. PMID 10447790.
Saito T, Krutovskikh V, Marion MJ, et al. (2000). "Human hemangiosarcomas have a common polymorphism but no mutations in the connexin37 gene". Int. J. Cancer. 86 (1): 67–70. doi:10.1002/(SICI)1097-0215(20000401)86:1<67::AID-IJC10>3.0.CO;2-1. PMID 10728596.
Suzuki Y, Taira H, Tsunoda T, et al. (2001). "Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites". EMBO Rep. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Tsai MY, Lan KC, Huang KE, et al. (2004). "Significance of mRNA levels of connexin37, connexin43, and connexin45 in luteinized granulosa cells of controlled hyperstimulated follicles". Fertil. Steril. 80 (6): 1437–43. doi:10.1016/j.fertnstert.2003.05.015. PMID 14667880.
Seul KH, Kang KY, Lee KS, et al. (2004). "Adenoviral delivery of human connexin37 induces endothelial cell death through apoptosis". Biochem. Biophys. Res. Commun. 319 (4): 1144–51. doi:10.1016/j.bbrc.2004.05.097. PMID 15194487.
Kameritsch P, Khandoga N, Nagel W, et al. (2005). "Nitric oxide specifically reduces the permeability of Cx37-containing gap junctions to small molecules". J. Cell. Physiol. 203 (1): 233–42. doi:10.1002/jcp.20218. PMID 15481066.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

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

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

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 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

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

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

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

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: 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

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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GJA4

References

Further reading