DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Structure (London, England : 1993) 2006 imex curation Kühnel K., Veltel S., Schlichting I., Wittinghofer A. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Kühnel K., Veltel S., Schlichting I., Wittinghofer A. DIP original experiment: DIP-66125X Structure (London, England : 1993) 2006 IMEx Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. xrp2_human Protein XRP2 RP2 protein protein human Homo sapiens Human MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI DIP protein O75695 original sequence version: 47 DIP protein O75695 original sequence version: 73 mint Stimulates the GTPase activity of tubulin, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor for ARL3 Defects in RP2 are the cause of retinitis pigmentosa type 2 (RP2) [MIM:312600]; also known as X-linked retinitis pigmentosa 2 (XLRP-2). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well 3C912B52C53A817E arl3_mouse ADP-ribosylation factor-like protein 3 Arl3 protein protein mouse Mus musculus Mouse MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRSYFENTDILIYVIDSADRKRFEETGQELTELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK DIP protein Q9WUL7 original sequence version: 52 DIP protein Q9WUL7 original sequence version: 69 DIP protein Q9WUL7 original sequence version: 139 16B85B2268ADB9DE arl3-rp2-3 1 2 unspecified role unspecified role unspecified role unspecified role Binding Region 1-230 Binding Region 1-230 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 3 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction