ID   RAB18_CAEBR             Reviewed;         202 AA.
AC   P90726; A8XLT7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Ras-related protein Rab-18;
GN   Name=rab-18; ORFNames=CBG15153;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9001248; DOI=10.1128/mcb.17.2.946;
RA   Zorio D.A.R., Lea K., Blumenthal T.;
RT   "Cloning of Caenorhabditis U2AF65: an alternatively spliced RNA containing
RT   a novel exon.";
RL   Mol. Cell. Biol. 17:946-953(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Plays a role in apical endocytosis/recycling. May be
CC       implicated in transport between the plasma membrane and early endosomes
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; U79145; AAB38279.1; -; Genomic_DNA.
DR   EMBL; HE601055; CAP33591.1; -; Genomic_DNA.
DR   RefSeq; XP_002642883.1; XM_002642837.1.
DR   AlphaFoldDB; P90726; -.
DR   SMR; P90726; -.
DR   STRING; 6238.CBG15153; -.
DR   EnsemblMetazoa; CBG15153.1; CBG15153.1; WBGene00035481.
DR   GeneID; 8584876; -.
DR   KEGG; cbr:CBG_15153; -.
DR   CTD; 8584876; -.
DR   WormBase; CBG15153; CBP18335; WBGene00035481; Cbr-rab-18.
DR   eggNOG; KOG0080; Eukaryota.
DR   HOGENOM; CLU_041217_10_7_1; -.
DR   InParanoid; P90726; -.
DR   OMA; HRTLFIE; -.
DR   OrthoDB; 1247169at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Lipoprotein; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..202
FT                   /note="Ras-related protein Rab-18"
FT                   /id="PRO_0000121199"
FT   REGION          183..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..48
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        187..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         202
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           200
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           202
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  22723 MW;  E1989ED6D6093A78 CRC64;
     MSDDSSSPLT TLKILIIGES GVGKSSLMLR FVDDVFDPEQ AATIGVDFRV TSMTIDGNRV
     KLAIWDTAGQ ERFRTLTPSY YRGAQGVICV YDVTSRSSFE KLKHWMTEVD TYCTNDNVIK
     MMVANKIDMP NRTVTREEGL KFAKRHRTLF IEASAKTKEG VQCTFEELIE KIIQTPDLWD
     NDRPTFRLGQ PTDTSSGNLC GC