Rab escort protein 1 (REP1) also known as rab proteins geranylgeranyltransferase component A 1 is an enzyme that in humans is encoded by the CHMgene.[5][6]
This gene encodes component A of the RAB geranylgeranyl transferase holoenzyme. In the dimeric holoenzyme, this subunit binds unprenylated Rab GTPases and then presents them to the catalytic Rab GGTase subunit for the geranylgeranyl transfer reaction. Rab GTPases need to be geranylgeranyled on either one or two cysteine residues in their C-terminus to localize to the correct intracellular membrane.[6]
Mutations in this gene are a cause of choroideremia; also known as tapetochoroidal dystrophy (TCD). This X-linked disease is characterized by progressive dystrophy of the choroid, retinal pigment epithelium and retina.[6]
^ abcGRCh38: Ensembl release 89: ENSG00000188419 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000025531 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Molloy CM, van de Pol TJ, Brohet RM, Ropers HH, Cremers FP (May 1992). "Three RFLPs for pZ11 (DXS540) in the choroideremia gene at Xq21.2". Nucleic Acids Res. 20 (6): 1434. doi:10.1093/nar/20.6.1434. PMC312214. PMID 1373238.
^ abc"Entrez Gene: CHM choroideremia (Rab escort protein 1)".
^ abCremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (Jan 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.
^Rak A, Pylypenko O, Niculae A, Goody RS, Alexandrov K (Jan 2003). "Crystallization and preliminary X-ray diffraction analysis of monoprenylated Rab7 GTPase in complex with Rab escort protein 1". J. Struct. Biol. 141 (1): 93–5. doi:10.1016/S1047-8477(02)00634-2. PMID 12576024.
^Alexandrov K, Simon I, Iakovenko A, Holz B, Goody RS, Scheidig AJ (Apr 1998). "Moderate discrimination of REP-1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates". FEBS Lett. 425 (3): 460–4. doi:10.1016/S0014-5793(98)00290-7. PMID 9563513. S2CID 39125409.
^Pereira-Leal JB, Strom M, Godfrey RF, Seabra MC (Jan 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. 301 (1): 92–7. doi:10.1016/S0006-291X(02)02963-7. PMID 12535645.
Further readingedit
Sankila EM, Tolvanen R, van den Hurk JA, Cremers FP, de la Chapelle A (1993). "Aberrant splicing of the CHM gene is a significant cause of choroideremia". Nat. Genet. 1 (2): 109–13. doi:10.1038/ng0592-109. PMID 1302003. S2CID 23500961.
Merry DE, Jänne PA, Landers JE, Lewis RA, Nussbaum RL (1992). "Isolation of a candidate gene for choroideremia". Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2135–9. Bibcode:1992PNAS...89.2135M. doi:10.1073/pnas.89.6.2135. PMC48611. PMID 1549574.
van den Hurk JA, van de Pol TJ, Molloy CM, Brunsmann F, Rüther K, Zrenner E, Pinckers AJ, Pawlowitzki IH, Bleeker-Wagemakers EM, Wieringa B (1992). "Detection and characterization of point mutations in the choroideremia candidate gene by PCR-SSCP analysis and direct DNA sequencing". Am. J. Hum. Genet. 50 (6): 1195–202. PMC1682553. PMID 1598901.
Fodor E, Lee RT, O'Donnell JJ (1991). "Analysis of choroideraemia gene". Nature. 351 (6328): 614. Bibcode:1991Natur.351..614F. doi:10.1038/351614b0. PMID 1904992. S2CID 5447515.
Cremers FP, van de Pol DJ, van Kerkhoff LP, Wieringa B, Ropers HH (1990). "Cloning of a gene that is rearranged in patients with choroideraemia". Nature. 347 (6294): 674–7. Bibcode:1990Natur.347..674C. doi:10.1038/347674a0. PMID 2215697. S2CID 4347627.
Cremers FP, Sankila EM, Brunsmann F, Jay M, Jay B, Wright A, Pinckers AJ, Schwartz M, van de Pol DJ, Wieringa B (1990). "Deletions in patients with classical choroideremia vary in size from 45 kb to several megabases". Am. J. Hum. Genet. 47 (4): 622–8. PMC1683797. PMID 2220804.
Donnelly P, Menet H, Fouanon C, Herbert O, Moisan JP, Le Roux MG, Pascal O (1994). "Missense mutation in the choroideremia gene". Hum. Mol. Genet. 3 (6): 1017. doi:10.1093/hmg/3.6.1017. PMID 7951216.
Alexandrov K, Horiuchi H, Steele-Mortimer O, Seabra MC, Zerial M (1994). "Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes". EMBO J. 13 (22): 5262–73. doi:10.1002/j.1460-2075.1994.tb06860.x. PMC395482. PMID 7957092.
van Bokhoven H, van den Hurk JA, Bogerd L, Philippe C, Gilgenkrantz S, de Jong P, Ropers HH, Cremers FP (1995). "Cloning and characterization of the human choroideremia gene". Hum. Mol. Genet. 3 (7): 1041–6. doi:10.1093/hmg/3.7.1041. PMID 7981670.
Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.
Seabra MC, Brown MS, Goldstein JL (1993). "Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase". Science. 259 (5093): 377–81. Bibcode:1993Sci...259..377S. doi:10.1126/science.8380507. PMID 8380507.
Schwartz M, Rosenberg T, van den Hurk JA, van de Pol DJ, Cremers FP (1993). "Identification of mutations in Danish choroideremia families". Hum. Mutat. 2 (1): 43–7. doi:10.1002/humu.1380020108. PMID 8477262. S2CID 40191966.
Overmeyer JH, Wilson AL, Erdman RA, Maltese WA (1998). "The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein". Mol. Biol. Cell. 9 (1): 223–35. doi:10.1091/mbc.9.1.223. PMC25245. PMID 9437002.
Alexandrov K, Simon I, Iakovenko A, Holz B, Goody RS, Scheidig AJ (1998). "Moderate discrimination of REP-1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates". FEBS Lett. 425 (3): 460–4. doi:10.1016/S0014-5793(98)00290-7. PMID 9563513. S2CID 39125409.
Raffaniello RD, Raufman JP (1999). "Cytosolic RAB3D is associated with RAB escort protein (REP), not RAB-GDP dissociation inhibitor (GDI), in dispersed chief cells from guinea pig stomach". J. Cell. Biochem. 72 (4): 540–8. doi:10.1002/(SICI)1097-4644(19990315)72:4<540::AID-JCB9>3.0.CO;2-D. PMID 10022613. S2CID 35820873.
Thomä NH, Iakovenko A, Kalinin A, Waldmann H, Goody RS, Alexandrov K (2001). "Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II". Biochemistry. 40 (1): 268–74. doi:10.1021/bi002034p. PMID 11141079.
Syed N, Smith JE, John SK, Seabra MC, Aguirre GD, Milam AH (2001). "Evaluation of retinal photoreceptors and pigment epithelium in a female carrier of choroideremia". Ophthalmology. 108 (4): 711–20. doi:10.1016/S0161-6420(00)00643-6. PMID 11297488.
Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K (2002). "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase". J. Struct. Biol. 136 (2): 158–61. doi:10.1006/jsbi.2001.4433. PMID 11886217.
External linksedit
GeneReviews/NCBI/NIH/UW entry on Choroideremia
Rab+escort+protein+1,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article on a gene on the human X chromosome and/or its associated protein is a stub. You can help Wikipedia by expanding it.
escort, protein, rep1, also, known, proteins, geranylgeranyltransferase, component, enzyme, that, humans, encoded, gene, chmidentifiersaliaseschm, dxs540, ggta, escort, proteinexternal, idsomim, 300390, 892979, homologene, genecards, chmgene, location, human, . Rab escort protein 1 REP1 also known as rab proteins geranylgeranyltransferase component A 1 is an enzyme that in humans is encoded by the CHM gene 5 6 CHMIdentifiersAliasesCHM DXS540 GGTA HSD 32 REP 1 TCD Rab escort protein 1 CHM Rab escort proteinExternal IDsOMIM 300390 MGI 892979 HomoloGene 334 GeneCards CHMGene location Human Chr X chromosome human 1 BandXq21 2Start85 861 180 bp 1 End86 047 561 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX X E1Start111 950 290 bp 2 End112 095 214 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inendothelial cellBrodmann area 23middle temporal gyrusgerminal epitheliumvisceral pleuraislet of Langerhanspostcentral gyrusparietal pleuraAchilles tendonentorhinal cortexTop expressed inciliary bodyRegion I of hippocampus properretinal pigment epitheliumirislateral geniculate nucleussacculemedial geniculate nucleusmedial dorsal nucleuspiriform cortexprimary motor cortexMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionRab geranylgeranyltransferase activity GTPase activator activity GDP dissociation inhibitor activityCellular componentcytoplasm Rab protein geranylgeranyltransferase complex cytosol nucleusBiological processpositive regulation of GTPase activity intracellular protein transport protein geranylgeranylation response to stimulus visual perception protein targeting to membrane regulation of catalytic activity small GTPase mediated signal transduction regulation of apoptotic process post translational protein modification vesicle mediated transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez112112662EnsemblENSG00000188419ENSMUSG00000025531UniProtP24386Q9QXG2RefSeq mRNA NM 000390NM 001037312NM 001145414NM 001320959NM 001362517NM 001362518NM 001362519NM 152579NM 018818NM 001370788NM 001370789NM 001370790RefSeq protein NP 000381NP 001138886NP 001307888NP 001349446NP 001349447NP 001349448n aLocation UCSC Chr X 85 86 86 05 MbChr X 111 95 112 1 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 Clinical significance 4 See also 5 References 6 Further reading 7 External linksFunction editThis gene encodes component A of the RAB geranylgeranyl transferase holoenzyme In the dimeric holoenzyme this subunit binds unprenylated Rab GTPases and then presents them to the catalytic Rab GGTase subunit for the geranylgeranyl transfer reaction Rab GTPases need to be geranylgeranyled on either one or two cysteine residues in their C terminus to localize to the correct intracellular membrane 6 Interactions editCHM gene has been shown to interact with RAB1A 7 RAB7A 8 9 and RAB3A 7 10 Clinical significance editMutations in this gene are a cause of choroideremia also known as tapetochoroidal dystrophy TCD This X linked disease is characterized by progressive dystrophy of the choroid retinal pigment epithelium and retina 6 See also editRab G protein References edit a b c GRCh38 Ensembl release 89 ENSG00000188419 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000025531 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Molloy CM van de Pol TJ Brohet RM Ropers HH Cremers FP May 1992 Three RFLPs for pZ11 DXS540 in the choroideremia gene at Xq21 2 Nucleic Acids Res 20 6 1434 doi 10 1093 nar 20 6 1434 PMC 312214 PMID 1373238 a b c Entrez Gene CHM choroideremia Rab escort protein 1 a b Cremers FP Armstrong SA Seabra MC Brown MS Goldstein JL Jan 1994 REP 2 a Rab escort protein encoded by the choroideremia like gene J Biol Chem 269 3 2111 7 doi 10 1016 S0021 9258 17 42142 9 PMID 8294464 Rak A Pylypenko O Niculae A Goody RS Alexandrov K Jan 2003 Crystallization and preliminary X ray diffraction analysis of monoprenylated Rab7 GTPase in complex with Rab escort protein 1 J Struct Biol 141 1 93 5 doi 10 1016 S1047 8477 02 00634 2 PMID 12576024 Alexandrov K Simon I Iakovenko A Holz B Goody RS Scheidig AJ Apr 1998 Moderate discrimination of REP 1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates FEBS Lett 425 3 460 4 doi 10 1016 S0014 5793 98 00290 7 PMID 9563513 S2CID 39125409 Pereira Leal JB Strom M Godfrey RF Seabra MC Jan 2003 Structural determinants of Rab and Rab Escort Protein interaction Rab family motifs define a conserved binding surface Biochem Biophys Res Commun 301 1 92 7 doi 10 1016 S0006 291X 02 02963 7 PMID 12535645 Further reading editSankila EM Tolvanen R van den Hurk JA Cremers FP de la Chapelle A 1993 Aberrant splicing of the CHM gene is a significant cause of choroideremia Nat Genet 1 2 109 13 doi 10 1038 ng0592 109 PMID 1302003 S2CID 23500961 Merry DE Janne PA Landers JE Lewis RA Nussbaum RL 1992 Isolation of a candidate gene for choroideremia Proc Natl Acad Sci U S A 89 6 2135 9 Bibcode 1992PNAS 89 2135M doi 10 1073 pnas 89 6 2135 PMC 48611 PMID 1549574 van den Hurk JA van de Pol TJ Molloy CM Brunsmann F Ruther K Zrenner E Pinckers AJ Pawlowitzki IH Bleeker Wagemakers EM Wieringa B 1992 Detection and characterization of point mutations in the choroideremia candidate gene by PCR SSCP analysis and direct DNA sequencing Am J Hum Genet 50 6 1195 202 PMC 1682553 PMID 1598901 Fodor E Lee RT O Donnell JJ 1991 Analysis of choroideraemia gene Nature 351 6328 614 Bibcode 1991Natur 351 614F doi 10 1038 351614b0 PMID 1904992 S2CID 5447515 Cremers FP van de Pol DJ van Kerkhoff LP Wieringa B Ropers HH 1990 Cloning of a gene that is rearranged in patients with choroideraemia Nature 347 6294 674 7 Bibcode 1990Natur 347 674C doi 10 1038 347674a0 PMID 2215697 S2CID 4347627 Cremers FP Sankila EM Brunsmann F Jay M Jay B Wright A Pinckers AJ Schwartz M van de Pol DJ Wieringa B 1990 Deletions in patients with classical choroideremia vary in size from 45 kb to several megabases Am J Hum Genet 47 4 622 8 PMC 1683797 PMID 2220804 Donnelly P Menet H Fouanon C Herbert O Moisan JP Le Roux MG Pascal O 1994 Missense mutation in the choroideremia gene Hum Mol Genet 3 6 1017 doi 10 1093 hmg 3 6 1017 PMID 7951216 Alexandrov K Horiuchi H Steele Mortimer O Seabra MC Zerial M 1994 Rab escort protein 1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes EMBO J 13 22 5262 73 doi 10 1002 j 1460 2075 1994 tb06860 x PMC 395482 PMID 7957092 van Bokhoven H van den Hurk JA Bogerd L Philippe C Gilgenkrantz S de Jong P Ropers HH Cremers FP 1995 Cloning and characterization of the human choroideremia gene Hum Mol Genet 3 7 1041 6 doi 10 1093 hmg 3 7 1041 PMID 7981670 Cremers FP Armstrong SA Seabra MC Brown MS Goldstein JL 1994 REP 2 a Rab escort protein encoded by the choroideremia like gene J Biol Chem 269 3 2111 7 doi 10 1016 S0021 9258 17 42142 9 PMID 8294464 Seabra MC Brown MS Goldstein JL 1993 Retinal degeneration in choroideremia deficiency of rab geranylgeranyl transferase Science 259 5093 377 81 Bibcode 1993Sci 259 377S doi 10 1126 science 8380507 PMID 8380507 Schwartz M Rosenberg T van den Hurk JA van de Pol DJ Cremers FP 1993 Identification of mutations in Danish choroideremia families Hum Mutat 2 1 43 7 doi 10 1002 humu 1380020108 PMID 8477262 S2CID 40191966 Overmeyer JH Wilson AL Erdman RA Maltese WA 1998 The putative switch 2 domain of the Ras related GTPase Rab1B plays an essential role in the interaction with Rab escort protein Mol Biol Cell 9 1 223 35 doi 10 1091 mbc 9 1 223 PMC 25245 PMID 9437002 Alexandrov K Simon I Iakovenko A Holz B Goody RS Scheidig AJ 1998 Moderate discrimination of REP 1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates FEBS Lett 425 3 460 4 doi 10 1016 S0014 5793 98 00290 7 PMID 9563513 S2CID 39125409 Raffaniello RD Raufman JP 1999 Cytosolic RAB3D is associated with RAB escort protein REP not RAB GDP dissociation inhibitor GDI in dispersed chief cells from guinea pig stomach J Cell Biochem 72 4 540 8 doi 10 1002 SICI 1097 4644 19990315 72 4 lt 540 AID JCB9 gt 3 0 CO 2 D PMID 10022613 S2CID 35820873 Thoma NH Iakovenko A Kalinin A Waldmann H Goody RS Alexandrov K 2001 Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II Biochemistry 40 1 268 74 doi 10 1021 bi002034p PMID 11141079 Syed N Smith JE John SK Seabra MC Aguirre GD Milam AH 2001 Evaluation of retinal photoreceptors and pigment epithelium in a female carrier of choroideremia Ophthalmology 108 4 711 20 doi 10 1016 S0161 6420 00 00643 6 PMID 11297488 Rak A Reents R Pylypenko O Niculae A Sidorovitch V Thoma NH Waldmann H Schlichting I Goody RS Alexandrov K 2002 Crystallization and preliminary X ray diffraction analysis of the Rab escort protein 1 in complex with Rab geranylgeranyltransferase J Struct Biol 136 2 158 61 doi 10 1006 jsbi 2001 4433 PMID 11886217 External links editGeneReviews NCBI NIH UW entry on Choroideremia Rab escort protein 1 human at the U S National Library of Medicine Medical Subject Headings MeSH nbsp This article on a gene on the human X chromosome and or its associated protein is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Rab escort protein 1 amp oldid 1170232632, wikipedia, wiki, book, books, library,
