Voltage-dependent Ca+2 channel subunit alpha-2/delta-2 (voltage-gated Ca+2 channel subunit alpha-2/delta-2, [Contains: Voltage-dependent Ca+2 channel subunit alpha-2-2; Voltage-dependent Ca+2 channel subunit delta-2], CACNA2D2, KIAA0558)

Function: - alpha-2/delta subunit of voltage-dependent Ca⁺² - channels regulates Ca+ current density & activation/inactivation kinetics of the Ca⁺² channel - regulatory subunit for P/Q-type Ca⁺² channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) & possibly T-type (CACNA1G) - dimer formed of alpha-2-2 & delta-2 chains, disulfide-linked - voltage-dependent Ca⁺² channels are multisubunit complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) & delta (CACNA2D) subunits in a 1:1:1:1 ratio - may be proteolytically processed into subunits alpha-2-2 & delta-2, disulfide-linked; however, unclear whether cleavage occurs in vivo & has a functional role - overexpression induces apoptosis - binds gabapentin Structure: - N-glycosylated - MIDAS-like motif in the VWFA domain binds divalent metal cations & is required to promote trafficking of alpha-1 (CACNA1) subunit to the plasma membrane by an integrin-like switch (putative) - belongs to the Ca⁺² channel subunit alpha-2/delta family - contains 1 cache domain - contains 1 VWFA domain Compartment: - membrane (putative) - colocalizes with CACNA1A in lipid raft fractions (putative) Alternative splicing: named isoforms=5 Expression: - predominantly present in cerebellar cortex - highly expressed in heart, lung, testis, pancreas & s keletal muscle - also expressed in kidney, liver, placenta & brain Pathology: - expressed various lung tumor cell lines, but absent in normal lung (at protein level)

General

glycoprotein voltage-dependent Ca+2 channel alpha-2/delta

Properties

SIZE: entity length = 1150 aa MW = 130 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-18} VWFA domain {291-469} MOTIF: MIDAS-like {297-301} N-glycosylation site {N418} Cache {485-574} MOTIF: N-glycosylation site {N507} N-glycosylation site {N540} N-glycosylation site {N861} transmembrane domain {1114-1134}

Database Correlations

OMIM 607082 UniProt Q9NY47 PFAM correlations

References

UniProt :accession Q9NY47