RAE1_HUMAN
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 03-AUG-2022, entry version 194.
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="http://grenada.lumc.nl/LOVD2/Usher_montpellier/home.php?select_db=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";
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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; 43.
DR CORUM; P24386; -.
DR IntAct; P24386; 70.
DR STRING; 9606.ENSP00000350386; -.
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; P24386; -.
DR PeptideAtlas; P24386; -.
DR PRIDE; P24386; -.
DR ProteomicsDB; 54199; -. [P24386-1]
DR ProteomicsDB; 54200; -. [P24386-2]
DR Antibodypedia; 492; 175 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 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; QMYPNEE; -.
DR OrthoDB; 1017439at2759; -.
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 704 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 180 other tissues.
DR Genevisible; P24386; HS.
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: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; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; PTHR11787; 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; SSF51905; SSF51905; 1.
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
