ID   RAB38_HUMAN             Reviewed;         211 AA.
AC   P57729; Q53XK7;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   09-APR-2025, entry version 196.
DE   RecName: Full=Ras-related protein Rab-38;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q13637};
DE   AltName: Full=Melanoma antigen NY-MEL-1;
GN   Name=RAB38 {ECO:0000312|HGNC:HGNC:9776};
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].
RX   PubMed=10910072;
RA   Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A.,
RA   Old L.J., Chen Y.-T.;
RT   "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding
RT   protein and a chromosome condensation protein from a melanoma complementary
RT   DNA library.";
RL   Cancer Res. 60:3584-3591(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=12643545; DOI=10.1021/pr025562r;
RA   Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA   Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA   Appella E.;
RT   "Proteomic analysis of early melanosomes: identification of novel
RT   melanosomal proteins.";
RL   J. Proteome Res. 2:69-79(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [7]
RP   ISOPRENYLATION AT CYS-208.
RX   PubMed=17114793; DOI=10.1074/jbc.m605557200;
RA   Leung K.F., Baron R., Ali B.R., Magee A.I., Seabra M.C.;
RT   "Rab GTPases containing a CAAX motif are processed post-geranylgeranylation
RT   by proteolysis and methylation.";
RL   J. Biol. Chem. 282:1487-1497(2007).
RN   [8]
RP   INTERACTION WITH ANKRD27.
RX   PubMed=19403694; DOI=10.1091/mbc.e08-12-1161;
RA   Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.;
RT   "Varp is a novel Rab32/38-binding protein that regulates Tyrp1 trafficking
RT   in melanocytes.";
RL   Mol. Biol. Cell 20:2900-2908(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA   Seto S., Tsujimura K., Koide Y.;
RT   "Rab GTPases regulating phagosome maturation are differentially recruited
RT   to mycobacterial phagosomes.";
RL   Traffic 12:407-420(2011).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
RA   Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
RT   "BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
RT   nucleotide exchange factor.";
RL   Curr. Biol. 22:2135-2139(2012).
RN   [12] {ECO:0007744|PDB:6S5H}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-207 IN COMPLEX WITH GTP AND
RP   MG(2+), AND COFACTOR.
RA   Diaz-Saez L., a Jung S., Huber K., von Delft F., Arrowsmith C.H.,
RA   Edwards A., Bountra C.;
RT   "Structure of the human RAB38 in complex with GTP.";
RL   Submitted (JUL-2019) to the PDB data bank.
RN   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-111.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different sets of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion (By similarity). RAB38 may be
CC       involved in melanosomal transport and docking. Involved in the proper
CC       sorting of TYRP1. Involved in peripheral melanosomal distribution of
CC       TYRP1 in melanocytes; the function, which probably is implicating
CC       vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (By
CC       similarity). Plays a role in the maturation of phagosomes that engulf
CC       pathogens, such as S.aureus and M.tuberculosis (PubMed:21255211). Plays
CC       an important role in the control of melanin production and melanosome
CC       biogenesis (PubMed:23084991). In concert with RAB32, regulates the
CC       proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to
CC       melanosomes in melanocytes (By similarity).
CC       {ECO:0000250|UniProtKB:Q13637, ECO:0000250|UniProtKB:Q8QZZ8,
CC       ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:Q13637};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:Q13637};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.12};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) including the BLOC-3 complex composed of HPS1 and HPS4 which
CC       promote the exchange of bound GDP for free GTP. Regulated by GTPase
CC       activating proteins (GAPs) including SGSM2 which increase the GTP
CC       hydrolysis activity (By similarity). Inhibited by GDP dissociation
CC       inhibitors (GDIs) (Probable). {ECO:0000250|UniProtKB:Q8QZZ8,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Interacts with ANKRD27 (PubMed:19403694).
CC       {ECO:0000269|PubMed:19403694}.
CC   -!- INTERACTION:
CC       P57729; P01023: A2M; NbExp=3; IntAct=EBI-6552718, EBI-640741;
CC       P57729; P50570-2: DNM2; NbExp=3; IntAct=EBI-6552718, EBI-10968534;
CC       P57729; P14136: GFAP; NbExp=3; IntAct=EBI-6552718, EBI-744302;
CC       P57729; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-6552718, EBI-1055254;
CC       P57729; Q5S007: LRRK2; NbExp=4; IntAct=EBI-6552718, EBI-5323863;
CC       P57729; P51608: MECP2; NbExp=3; IntAct=EBI-6552718, EBI-1189067;
CC       P57729; P19404: NDUFV2; NbExp=3; IntAct=EBI-6552718, EBI-713665;
CC       P57729; Q16637: SMN2; NbExp=3; IntAct=EBI-6552718, EBI-395421;
CC       P57729; O14656-2: TOR1A; NbExp=3; IntAct=EBI-6552718, EBI-25847109;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome
CC       {ECO:0000269|PubMed:12643545}. Cytoplasmic vesicle, phagosome
CC       {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}. Melanosome membrane {ECO:0000269|PubMed:23084991}.
CC       Note=Recruited to phagosomes containing S.aureus or M.tuberculosis
CC       (PubMed:21255211). The BLOC-3 complex, a heterodimer of HPS1 and HPS4
CC       promotes its membrane localization (PubMed:23084991).
CC       {ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
CC   -!- TISSUE SPECIFICITY: Expressed in melanocytes.
CC   -!- PTM: Although at least one in vitro system can process and methylate
CC       the prenylated C-terminal, in an in vitro system that normally express
CC       Rab-38 and in vivo the prenylated C-terminal is not proteolytically
CC       processed and not methylated. {ECO:0000269|PubMed:17114793}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AF235022; AAG30731.1; -; mRNA.
DR   EMBL; BT009842; AAP88844.1; -; mRNA.
DR   EMBL; DQ178619; ABA03166.1; -; Genomic_DNA.
DR   EMBL; BC015808; AAH15808.1; -; mRNA.
DR   CCDS; CCDS8281.1; -.
DR   RefSeq; NP_071732.1; NM_022337.3.
DR   PDB; 6HDU; X-ray; 1.79 A; A/B/C/D=1-181.
DR   PDB; 6S5H; X-ray; 2.00 A; A=1-207.
DR   PDBsum; 6HDU; -.
DR   PDBsum; 6S5H; -.
DR   AlphaFoldDB; P57729; -.
DR   SMR; P57729; -.
DR   BioGRID; 117198; 35.
DR   DIP; DIP-60520N; -.
DR   IntAct; P57729; 35.
DR   STRING; 9606.ENSP00000243662; -.
DR   iPTMnet; P57729; -.
DR   PhosphoSitePlus; P57729; -.
DR   SwissPalm; P57729; -.
DR   BioMuta; RAB38; -.
DR   DMDM; 12230516; -.
DR   jPOST; P57729; -.
DR   MassIVE; P57729; -.
DR   PaxDb; 9606-ENSP00000243662; -.
DR   PeptideAtlas; P57729; -.
DR   ProteomicsDB; 57021; -.
DR   Pumba; P57729; -.
DR   Antibodypedia; 31470; 238 antibodies from 31 providers.
DR   DNASU; 23682; -.
DR   Ensembl; ENST00000243662.11; ENSP00000243662.5; ENSG00000123892.12.
DR   GeneID; 23682; -.
DR   KEGG; hsa:23682; -.
DR   MANE-Select; ENST00000243662.11; ENSP00000243662.5; NM_022337.3; NP_071732.1.
DR   UCSC; uc001pcj.3; human.
DR   AGR; HGNC:9776; -.
DR   CTD; 23682; -.
DR   DisGeNET; 23682; -.
DR   GeneCards; RAB38; -.
DR   HGNC; HGNC:9776; RAB38.
DR   HPA; ENSG00000123892; Tissue enhanced (esophagus, skin).
DR   MIM; 606281; gene.
DR   neXtProt; NX_P57729; -.
DR   OpenTargets; ENSG00000123892; -.
DR   PharmGKB; PA34129; -.
DR   VEuPathDB; HostDB:ENSG00000123892; -.
DR   eggNOG; KOG4423; Eukaryota.
DR   GeneTree; ENSGT00940000157301; -.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; P57729; -.
DR   OMA; MHYKSTI; -.
DR   OrthoDB; 245989at2759; -.
DR   PhylomeDB; P57729; -.
DR   TreeFam; TF324491; -.
DR   PathwayCommons; P57729; -.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; P57729; -.
DR   SIGNOR; P57729; -.
DR   BioGRID-ORCS; 23682; 8 hits in 1145 CRISPR screens.
DR   ChiTaRS; RAB38; human.
DR   GeneWiki; RAB38; -.
DR   GenomeRNAi; 23682; -.
DR   Pharos; P57729; Tbio.
DR   PRO; PR:P57729; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P57729; protein.
DR   Bgee; ENSG00000123892; Expressed in gingival epithelium and 123 other cell types or tissues.
DR   ExpressionAtlas; P57729; baseline and differential.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0042470; C:melanosome; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane contact site; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0035650; F:AP-1 adaptor complex binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0035651; F:AP-3 adaptor complex binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0036461; F:BLOC-2 complex binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
DR   GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0090383; P:phagosome acidification; IMP:UniProtKB.
DR   GO; GO:0060155; P:platelet dense granule organization; IEA:Ensembl.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IEA:Ensembl.
DR   GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR   GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IEA:Ensembl.
DR   GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase-mediated signal transduction; NAS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd04107; Rab32_Rab38; 1.
DR   FunFam; 3.40.50.300:FF:000222; RAB32, member RAS oncogene family; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030697; Rab29/Rab38/Rab32.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47981; RAB FAMILY; 1.
DR   PANTHER; PTHR47981:SF43; RAS-RELATED PROTEIN RAB; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasmic vesicle; GTP-binding; Hydrolase;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Palmitate; Prenylation; Protein transport; Proteomics identification;
KW   Reference proteome; Transport.
FT   CHAIN           1..211
FT                   /note="Ras-related protein Rab-38"
FT                   /id="PRO_0000121251"
FT   MOTIF           38..46
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         36
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         65
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   BINDING         161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:6S5H"
FT   SITE            208
FT                   /note="Not methylated"
FT   LIPID           205
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           208
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:17114793"
FT   VARIANT         111
FT                   /note="K -> T (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036415"
FT   STRAND          6..17
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   STRAND          43..54
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   STRAND          57..66
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           68..72
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           95..111
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           143..150
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:6HDU"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:6HDU"
SQ   SEQUENCE   211 AA;  23712 MW;  0D16B42A1B237539 CRC64;
     MQAPHKEHLY KLLVIGDLGV GKTSIIKRYV HQNFSSHYRA TIGVDFALKV LHWDPETVVR
     LQLWDIAGQE RFGNMTRVYY REAMGAFIVF DVTRPATFEA VAKWKNDLDS KLSLPNGKPV
     SVVLLANKCD QGKDVLMNNG LKMDQFCKEH GFVGWFETSA KENINIDEAS RCLVKHILAN
     ECDLMESIEP DVVKPHLTST KVASCSGCAK S
//