Protein Details: Volume-regulated anion channel subunit LRRC8D

Protein ID

ICDB_Pro_1148

Protein Name

Volume-regulated anion channel subunit LRRC8D

Gene Name

LRRC8D; LRRC5; UNQ213/PRO239

Organism

Homo sapiens (Human)

Length

858 amino acids

AlphaFoldDB

AF-Q7L1W4-F1-model_v4.pdb

Function

Non-essential component of the volume-regulated anion channel (VRAC; also named VSOAC channel); an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes . The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine . Plays a redundant role in the efflux of amino acids; such as aspartate; in response to osmotic stress . LRRC8A and LRRC8D are required for the uptake of the drug cisplatin . Channel activity requires LRRC8A plus at least one other family member (LRRC8B; LRRC8C; LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition . Also acts as a regulator of glucose-sensing in pancreatic beta cells: VRAC currents; generated in response to hypotonicity- or glucose-induced beta cell swelling; depolarize cells; thereby causing electrical excitation; leading to increase glucose sensitivity and insulin secretion (By similarity). VRAC channels containing LRRC8D inhibit transport of immunoreactive cyclic dinucleotide GMP-AMP (2-3-cGAMP); an immune messenger produced in response to DNA virus in the cytosol . Mediates the import of the antibiotic blasticidin-S into the cell .

Sequence

MFTLAEVASLNDIQPTYRILKPWWDVFMDYLAVVMLMVAIFAGTMQLTKDQVVCLPVLPSPVNSKAHTPPGNAEVTTNIPKMEAATNQDQDGRTTNDISFGTSAVTPDIPLRATYPRTDFALPNQEAKKEKKDPTGRKTNLDFQQYVFINQMCYHLALPWYSKYFPYLALIHTIILMVSSNFWFKYPKTCSKVEHFVSILGKCFESPWTTKALSETACEDSEENKQRITGAQTLPKHVSTSSDEGSPSASTPMINKTGFKFSAEKPVIEVPSMTILDKKDGEQAKALFEKVRKFRAHVEDSDLIYKLYVVQTVIKTAKFIFILCYTANFVNAISFEHVCKPKVEHLIGYEVFECTHNMAYMLKKLLISYISIICVYGFICLYTLFWLFRIPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQHISRNAQDKQELHLFMLSGVPDAVFDLTDLDVLKLELIPEAKIPAKISQMTNLQELHLCHCPAKVEQTAFSFLRDHLRCLHVKFTDVAEIPAWVYLLKNLRELYLIGNLNSENNKMIGLESLRELRHLKILHVKSNLTKVPSNITDVAPHLTKLVIHNDGTKLLVLNSLKKMMNVAELELQNCELERIPHAIFSLSNLQELDLKSNNIRTIEEIISFQHLKRLTCLKLWHNKIVTIPPSITHVKNLESLYFSNNKLESLPVAVFSLQKLRCLDVSYNNISMIPIEIGLLQNLQHLHITGNKVDILPKQLFKCIKLRTLNLGQNCITSLPEKVGQLSQLTQLELKGNCLDRLPAQLGQCRMLKKSGLVVEDHLFDTLPLEVKEALNQDINIPFANGI

PDB Structures

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

Disease

Nail Disorder;Nonsyndromic Congenital;3 and Nonsyndromic Congenital Nail Disorder

Location

DOI ID

RefSeq

NP_001127951.1; NP_060573.2; XP_011539991.1; XP_016857088.1; XP_016857089.1; XP_016857090.1; XP_016857091.1

Feature