Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. GARPs are characterized by six repeated motifs of: V V E K K N/E E. These repeat motifs help form an alpha-helix structure. The function(s) of GARP have not been fully characterized, but studies have suggested that GARP helps limit cGMP turnover by inhibiting phosphodiesterase activity. To date, there have been two splice variants characterized: GARP1 (full-length GARP) and GARP2 (truncated GARP). GARP also interacts with part of the larger cytoplasmic domain of the beta-subunit of the cyclic GMP-gated channel found in the plasma membrane.
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Protein Aliases: cng channel; CNG channel 4; CNG channel beta-1; CNG-4; Cyclic nucleotide-gated cation channel 4; Cyclic nucleotide-gated cation channel beta-1; Cyclic nucleotide-gated cation channel gamma; Cyclic nucleotide-gated cation channel modulatory subunit; cyclic nucleotide-gated channel beta subunit 1; Cyclic nucleotide-gated channel beta-1; GARP; Glutamic acid-rich protein; glutamic-acid-rich protein
Gene Aliases: CNCG2; CNCG3L; CNCG4; CNG4; CNGB1; CNGB1B; GAR1; GARP; GARP2; Gm1959; RCNC2; RCNCb; RCNCbeta; RP45
UniProt ID: (Human) Q14028