TRPC5

Transient receptor potential cation channel, subfamily C, member 5

Identifiers

TRPC5 ; PPP1R159; TRP5

External IDs

OMIM: 300334 MGI: 109524 HomoloGene: 74915 IUPHAR: 490 ChEMBL: 1250411 GeneCards: TRPC5 Gene

Gene ontology
Molecular function	• calcium channel activity • protein binding • store-operated calcium channel activity • inositol 1,4,5 trisphosphate binding
Cellular component	• plasma membrane • integral component of plasma membrane • calcium channel complex
Biological process	• calcium ion transport • nervous system development • axon guidance • ion transmembrane transport • transmembrane transport • calcium ion transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
111.02 – 111.33 Mb

Chr X:
144.38 – 144.69 Mb

PubMed search

Short transient receptor potential channel 5 (TrpC5) also known as transient receptor protein 5 (TRP-5) is a protein that in humans is encoded by the TRPC5 gene.^[1]^[2]^[3] TrpC5 is subtype of the TRPC family of mammalian transient receptor potential ion channels.

Function

TrpC5 is one of the seven mammalian TRPC (transient receptor potential channel) proteins. TrpC5 is a multi-pass membrane protein and is thought to form a receptor-activated non-selective calcium permeant cation channel. The protein is active alone or as a heteromultimeric assembly with TRPC1, TRPC3, and TRPC4. It also interacts with multiple proteins including calmodulin, CABP1, enkurin, Na⁺–H⁺ exchange regulatory factor (NHERF), interferon-induced GTP-binding protein (MX1), ring finger protein 24 (RNF24), and SEC14 domain and spectrin repeat-containing protein 1 (SESTD1).^[1]

TRPC4 and TRPC5 have been implicated in the mechanism of mercury toxicity^[4] and neurological behavior.^[5]

Activation

Homomultimeric TRPC5 and heteromultimeric TRPC5-TRPC1 channels are activated by extracellular reduced thioredoxin.^[6] This channel has also been found to be involved in the action of anaesthetics such as chloroform, halothane and propofol.^[7]

Interactions

TRPC5 has been shown to interact with STMN3,^[8] TRPC1,^[9]^[10] and TRPC4.^[10]

References

↑ 1.0 1.1 "Entrez Gene: transient receptor potential cation channel".
↑ Sossey-Alaoui K, Lyon JA, Jones L, Abidi FE, Hartung AJ, Hane B et al. (September 1999). "Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca2+ entry channel". Genomics 60 (3): 330–40. doi:10.1006/geno.1999.5924. PMID 10493832. CS1 maint: Date and year (link)
↑ Clapham DE, Julius D, Montell C, Schultz G (December 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID 16382100. CS1 maint: Date and year (link)
↑ Xu SZ, Zeng B, Daskoulidou N, Chen GL, Atkin SL, Lukhele B (January 2012). "Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure". Toxicol. Sci. 125 (1): 56–68. doi:10.1093/toxsci/kfr268. PMID 21984481. CS1 maint: Date and year (link)
↑ Riccio A, Li Y, Moon J, Kim KS, Smith KS, Rudolph U et al. (May 15, 2009). "Essential role for TRPC5 in amygdala function and fear-related behavior". Cell 137 (4): 761–72. doi:10.1016/j.cell.2009.03.039. PMC 2719954. PMID 19450521. CS1 maint: Date and year (link)
↑ Xu SZ, Sukumar P, Zeng F, Li J, Jairaman A, English A et al. (January 2008). "TRPC channel activation by extracellular thioredoxin". Nature 451 (7174): 69–72. doi:10.1038/nature06414. PMC 2645077. PMID 18172497. CS1 maint: Date and year (link)
↑ Bahnasi YM, Wright HM, Milligan CJ, Dedman AM, Zeng F, Hopkins PM et al. (April 2008). "Modulation of TRPC5 cation channels by halothane, chloroform and propofol". Br. J. Pharmacol. 153 (7): 1505–12. doi:10.1038/sj.bjp.0707689. PMC 2437913. PMID 18204473. CS1 maint: Date and year (link)
↑ Greka A, Navarro B, Oancea E, Duggan A, Clapham DE (August 2003). "TRPC5 is a regulator of hippocampal neurite length and growth cone morphology". Nat. Neurosci. 6 (8): 837–45. doi:10.1038/nn1092. PMID 12858178. CS1 maint: Date and year (link)
↑ Strübing C, Krapivinsky G, Krapivinsky L, Clapham DE (October 2003). "Formation of novel TRPC channels by complex subunit interactions in embryonic brain". J. Biol. Chem. 278 (40): 39014–9. doi:10.1074/jbc.M306705200. PMID 12857742. Vancouver style error (help) CS1 maint: Date and year (link)
↑ 10.0 10.1 Hofmann T, Schaefer M, Schultz G, Gudermann T (May 2002). "Subunit composition of mammalian transient receptor potential channels in living cells". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7461–6. doi:10.1073/pnas.102596199. PMC 124253. PMID 12032305. CS1 maint: Date and year (link)

External links

TRPC5 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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

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

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins