ID RAE1_HUMAN Reviewed; 653 AA. AC P24386; A1L4D2; O43732; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 3. DT 27-MAR-2024, entry version 203. DE RecName: Full=Rab proteins geranylgeranyltransferase component A 1; DE AltName: Full=Choroideremia protein; DE AltName: Full=Rab escort protein 1; DE Short=REP-1; DE AltName: Full=TCD protein; GN Name=CHM; Synonyms=REP1, TCD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=7981670; DOI=10.1093/hmg/3.7.1041; RA van Bokhoven H., van den Hurk J.A., Bogerd L., Philippe C., RA Gilgenkrantz S., de Jong P., Ropers H.-H., Cremers F.P.; RT "Cloning and characterization of the human choroideremia gene."; RL Hum. Mol. Genet. 3:1041-1046(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 289-653 (ISOFORM 1). RC TISSUE=Retina; RX PubMed=1549574; DOI=10.1073/pnas.89.6.2135; RA Merry D.E., Janne P.A., Landers J.E., Lewis R.A., Nussbaum R.L.; RT "Isolation of a candidate gene for choroideremia."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2135-2139(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 338-653 (ISOFORM 1). RX PubMed=2215697; DOI=10.1038/347674a0; RA Cremers F.P.M., van de Pol D.J.R., van Kerkhoff L.P.M., Wieringa B., RA Ropers H.-H.; RT "Cloning of a gene that is rearranged in patients with choroideraemia."; RL Nature 347:674-677(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 451-590. RX PubMed=1598901; RA van den Hurk J.A.J.M., van de Pol T.J.R., Molloy C.M., Brunsmann F., RA Ruther K., Zrenner E., Pinckers A.J.L.G., Pawlowitzki I.H., RA Bleeker-Wagemakers E.M., Wieringa B., Ropers H.-H., Cremers F.P.M.; RT "Detection and characterization of point mutations in the choroideremia RT candidate gene by PCR-SSCP analysis and direct DNA sequencing."; RL Am. J. Hum. Genet. 50:1195-1202(1992). RN [7] RP SIMILARITY TO SMG P25A GDI. RX PubMed=1904992; DOI=10.1038/351614b0; RA Fodor E., Lee R.T., O'Donnell J.J.; RT "Analysis of choroideraemia gene."; RL Nature 351:614-614(1991). RN [8] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB5A AND RP RAB7A. RX PubMed=7957092; DOI=10.1002/j.1460-2075.1994.tb06860.x; RA Alexandrov K., Horiuchi H., Steele-Mortimer O., Seabra M.C., Zerial M.; RT "Rab escort protein-1 is a multifunctional protein that accompanies newly RT prenylated rab proteins to their target membranes."; RL EMBO J. 13:5262-5273(1994). RN [9] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF PHE-282 AND VAL-290. RX PubMed=18532927; DOI=10.1042/bj20080662; RA Baron R.A., Seabra M.C.; RT "Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT RT complex and is regulated by geranylgeranyl pyrophosphate."; RL Biochem. J. 415:67-75(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP INTERACTION WITH RABGGTA, VARIANT CHM ARG-507, AND CHARACTERIZATION OF RP VARIANT CHM ARG-507. RX PubMed=21905166; DOI=10.1002/humu.21591; RA Esposito G., De Falco F., Tinto N., Testa F., Vitagliano L., RA Tandurella I.C., Iannone L., Rossi S., Rinaldi E., Simonelli F., Zagari A., RA Salvatore F.; RT "Comprehensive mutation analysis (20 families) of the choroideremia gene RT reveals a missense variant that prevents the binding of REP1 with rab RT geranylgeranyl transferase."; RL Hum. Mutat. 32:1460-1469(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB8A. RX PubMed=26824392; DOI=10.7554/elife.12813; RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S., RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J., RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.; RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates RT a subset of Rab GTPases."; RL Elife 5:0-0(2016). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB3A; RAB3B; RP RAB3C; RAB3D; RAB5B; RAB5C; RAB8A; RAB8B; RAB10; RAB12; RAB35 AND RAB43. RX PubMed=29125462; DOI=10.7554/elife.31012; RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O., RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R., RA Mann M.; RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation RT establishes a connection to ciliogenesis."; RL Elife 6:0-0(2017). RN [15] RP VARIANT CHM LEU-471. RX PubMed=7951216; DOI=10.1093/hmg/3.6.1017; RA Donnelly P., Menet H., Fouanon C., Herbert O., Moisan J.P., Le Roux M.G., RA Pascal O.; RT "Missense mutation in the choroideremia gene."; RL Hum. Mol. Genet. 3:1017-1017(1994). RN [16] RP VARIANT CHM PRO-550. RX PubMed=19427510; DOI=10.1016/j.mrfmmm.2009.02.015; RA Sergeev Y.V., Smaoui N., Sui R., Stiles D., Gordiyenko N., Strunnikova N., RA Macdonald I.M.; RT "The functional effect of pathogenic mutations in Rab escort protein 1."; RL Mutat. Res. 665:44-50(2009). CC -!- FUNCTION: Substrate-binding subunit of the Rab CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab CC proteins and presents the substrate peptide to the catalytic component CC B composed of RABGGTA and RABGGTB, and remains bound to it after the CC geranylgeranyl transfer reaction. The component A is thought to be CC regenerated by transferring its prenylated Rab back to the donor CC membrane. Besides, a pre-formed complex consisting of CHM and the Rab CC GGTase dimer (RGGT or component B) can bind to and prenylate Rab CC proteins; this alternative pathway is proposed to be the predominant CC pathway for Rab protein geranylgeranylation. CC {ECO:0000269|PubMed:18532927, ECO:0000269|PubMed:7957092}. CC -!- SUBUNIT: Monomer (By similarity). Heterotrimer composed of RABGGTA, CC RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the CC catalytic component B, while CHM (component A) mediates Rab protein CC binding (PubMed:21905166). Can associate with the Rab GGTase dimer CC (RGGT or component B) prior to Rab protein binding; the association is CC stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab CC complex is destabilized by GGpp (PubMed:18532927). Interacts with CC RAB1A, RAB1B, RAB5A, RAB7A and RAB27A and mediates their prenylation CC (PubMed:7957092). Interacts with the non-phosphorylated forms of RAB3A, CC RAB3B, RAB3C, RAB3D, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB35, CC and RAB43 (PubMed:26824392, PubMed:29125462). CC {ECO:0000250|UniProtKB:P37727, ECO:0000269|PubMed:18532927, CC ECO:0000269|PubMed:21905166, ECO:0000269|PubMed:26824392, CC ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:7957092}. CC -!- INTERACTION: CC P24386; Q92696: RABGGTA; NbExp=2; IntAct=EBI-2515129, EBI-9104196; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7957092}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P24386-1; Sequence=Displayed; CC Name=2; CC IsoId=P24386-2; Sequence=VSP_042817, VSP_042818; CC -!- DISEASE: Choroideremia (CHM) [MIM:303100]: An X-linked recessive CC disease characterized by a slowly progressive degeneration of the CC choroid, photoreceptors, and retinal pigment epithelium. Affected males CC develop night blindness in their teenage years followed by loss of CC peripheral vision and complete blindness at middle age. Carrier females CC are generally asymptomatic but funduscopic examination often shows CC patchy areas of chorioretinal atrophy. {ECO:0000269|PubMed:19427510, CC ECO:0000269|PubMed:21905166, ECO:0000269|PubMed:7951216}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the REP1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/repmut.htm"; CC -!- WEB RESOURCE: Name=Retinal and hearing impairment genetic mutation CC database choroideremia (Rab escort protein 1) (CHM); Note=Leiden Open CC Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/CHM"; CC -!- WEB RESOURCE: Name=NGRL, Manchester LOVD choroideremia (Rab escort CC protein 1) (CHM); Note=Leiden Open Variation Database (LOVD); CC URL="https://secure.ngrl.org.uk/LOVDv.2.0/home.php?select_db=CHM"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X78121; CAA55011.1; -; mRNA. DR EMBL; AL009175; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL022401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035451; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC130494; AAI30495.1; -; mRNA. DR EMBL; BC130496; AAI30497.1; -; mRNA. DR EMBL; M83773; AAA61032.1; -; mRNA. DR EMBL; X57637; CAA40855.1; -; mRNA. DR EMBL; S37423; AAD13814.1; -; Genomic_DNA. DR EMBL; S37416; AAD13814.1; JOINED; Genomic_DNA. DR EMBL; S37417; AAD13814.1; JOINED; Genomic_DNA. DR EMBL; S37422; AAD13814.1; JOINED; Genomic_DNA. DR CCDS; CCDS14454.1; -. [P24386-1] DR CCDS; CCDS48139.1; -. [P24386-2] DR PIR; I37234; I37234. DR RefSeq; NP_000381.1; NM_000390.3. [P24386-1] DR RefSeq; NP_001138886.1; NM_001145414.3. [P24386-2] DR RefSeq; NP_001307888.1; NM_001320959.1. DR AlphaFoldDB; P24386; -. DR SMR; P24386; -. DR BioGRID; 107545; 57. DR CORUM; P24386; -. DR IntAct; P24386; 70. DR STRING; 9606.ENSP00000350386; -. DR ChEMBL; CHEMBL5169124; -. DR GlyGen; P24386; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P24386; -. DR PhosphoSitePlus; P24386; -. DR BioMuta; CHM; -. DR DMDM; 21431807; -. DR EPD; P24386; -. DR jPOST; P24386; -. DR MassIVE; P24386; -. DR MaxQB; P24386; -. DR PaxDb; 9606-ENSP00000350386; -. DR PeptideAtlas; P24386; -. DR ProteomicsDB; 54199; -. [P24386-1] DR ProteomicsDB; 54200; -. [P24386-2] DR Pumba; P24386; -. DR Antibodypedia; 492; 189 antibodies from 31 providers. DR DNASU; 1121; -. DR Ensembl; ENST00000357749.7; ENSP00000350386.2; ENSG00000188419.14. [P24386-1] DR Ensembl; ENST00000615443.1; ENSP00000484306.1; ENSG00000188419.14. [P24386-2] DR GeneID; 1121; -. DR KEGG; hsa:1121; -. DR MANE-Select; ENST00000357749.7; ENSP00000350386.2; NM_000390.4; NP_000381.1. DR UCSC; uc004eet.3; human. [P24386-1] DR AGR; HGNC:1940; -. DR CTD; 1121; -. DR DisGeNET; 1121; -. DR GeneCards; CHM; -. DR GeneReviews; CHM; -. DR HGNC; HGNC:1940; CHM. DR HPA; ENSG00000188419; Low tissue specificity. DR MalaCards; CHM; -. DR MIM; 300390; gene. DR MIM; 303100; phenotype. DR neXtProt; NX_P24386; -. DR OpenTargets; ENSG00000188419; -. DR Orphanet; 180; Choroideremia. DR PharmGKB; PA26471; -. DR VEuPathDB; HostDB:ENSG00000188419; -. DR eggNOG; KOG4405; Eukaryota. DR GeneTree; ENSGT00950000182994; -. DR HOGENOM; CLU_021695_4_1_1; -. DR InParanoid; P24386; -. DR OMA; LDQNDYY; -. DR OrthoDB; 197300at2759; -. DR PhylomeDB; P24386; -. DR TreeFam; TF320813; -. DR BRENDA; 2.5.1.60; 2681. DR PathwayCommons; P24386; -. DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SignaLink; P24386; -. DR SIGNOR; P24386; -. DR BioGRID-ORCS; 1121; 14 hits in 778 CRISPR screens. DR ChiTaRS; CHM; human. DR GeneWiki; Rab_escort_protein; -. DR GenomeRNAi; 1121; -. DR Pharos; P24386; Tbio. DR PRO; PR:P24386; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P24386; Protein. DR Bgee; ENSG00000188419; Expressed in endothelial cell and 182 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IMP:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:UniProtKB. DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0004663; F:Rab geranylgeranyltransferase activity; TAS:ProtInc. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB. DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1. DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR018203; GDP_dissociation_inhibitor. DR InterPro; IPR001738; Rab_escort. DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1. DR PANTHER; PTHR11787:SF12; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A 1; 1. DR Pfam; PF00996; GDI; 2. DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1. DR PRINTS; PR00893; RABESCORT. DR PRINTS; PR00891; RABGDIREP. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR Genevisible; P24386; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Disease variant; GTPase activation; KW Reference proteome; Sensory transduction; Vision. FT CHAIN 1..653 FT /note="Rab proteins geranylgeranyltransferase component A FT 1" FT /id="PRO_0000056686" FT REGION 606..653 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..653 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 105..110 FT /note="SQDLHE -> RSTLLL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042817" FT VAR_SEQ 111..653 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042818" FT VARIANT 471 FT /note="Q -> L (in CHM; may affect splicing)" FT /evidence="ECO:0000269|PubMed:7951216" FT /id="VAR_008273" FT VARIANT 507 FT /note="H -> R (in CHM; impairs the interaction with FT RABGGTA; dbSNP:rs397514603)" FT /evidence="ECO:0000269|PubMed:21905166" FT /id="VAR_066847" FT VARIANT 550 FT /note="L -> P (in CHM)" FT /evidence="ECO:0000269|PubMed:19427510" FT /id="VAR_066848" FT MUTAGEN 282 FT /note="F->L: Abolishes prenylation of RAB1A and association FT with RGGT." FT /evidence="ECO:0000269|PubMed:18532927" FT MUTAGEN 290 FT /note="V->F: Impairs prenylation of RAB1A and abolishes FT association with RGGT." FT /evidence="ECO:0000269|PubMed:18532927" FT CONFLICT 625..626 FT /note="AS -> RA (in Ref. 5; AAA61032)" FT /evidence="ECO:0000305" SQ SEQUENCE 653 AA; 73476 MW; 7CFFAECE7BA1F3AF CRC64; MADTLPSEFD VIVIGTGLPE SIIAAACSRS GRRVLHVDSR SYYGGNWASF SFSGLLSWLK EYQENSDIVS DSPVWQDQIL ENEEAIALSR KDKTIQHVEV FCYASQDLHE DVEEAGALQK NHALVTSANS TEAADSAFLP TEDESLSTMS CEMLTEQTPS SDPENALEVN GAEVTGEKEN HCDDKTCVPS TSAEDMSENV PIAEDTTEQP KKNRITYSQI IKEGRRFNID LVSKLLYSRG LLIDLLIKSN VSRYAEFKNI TRILAFREGR VEQVPCSRAD VFNSKQLTMV EKRMLMKFLT FCMEYEKYPD EYKGYEEITF YEYLKTQKLT PNLQYIVMHS IAMTSETASS TIDGLKATKN FLHCLGRYGN TPFLFPLYGQ GELPQCFCRM CAVFGGIYCL RHSVQCLVVD KESRKCKAII DQFGQRIISE HFLVEDSYFP ENMCSRVQYR QISRAVLITD RSVLKTDSDQ QISILTVPAE EPGTFAVRVI ELCSSTMTCM KGTYLVHLTC TSSKTAREDL ESVVQKLFVP YTEMEIENEQ VEKPRILWAL YFNMRDSSDI SRSCYNDLPS NVYVCSGPDC GLGNDNAVKQ AETLFQEICP NEDFCPPPPN PEDIILDGDS LQPEASESSA IPEANSETFK ESTNLGNLEE SSE //