ID   RAB18_PONAB             Reviewed;         206 AA.
AC   Q5R5H5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Ras-related protein Rab-18;
DE   Flags: Precursor;
GN   Name=RAB18;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the localization of ZFYVE1 to lipid droplets and
CC       for its function in mediating the formation of endoplasmic reticulum-
CC       lipid droplets (ER-LD) contacts (By similarity). Plays a role in apical
CC       endocytosis/recycling (By similarity). Plays a key role in eye and
CC       brain development and neurodegeneration (By similarity).
CC       {ECO:0000250|UniProtKB:Q8MXS1, ECO:0000250|UniProtKB:Q9NP72}.
CC   -!- SUBUNIT: Interacts (in GTP-bound form) with ZFYVE1 (By similarity).
CC       Interacts with ZW10 and this interaction is enhanced in the presence of
CC       ZFYVE1 (By similarity). Interacts with BSCL2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NP72}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P35293}. Lipid droplet
CC       {ECO:0000250|UniProtKB:Q9NP72}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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; CR860884; CAH92991.1; -; mRNA.
DR   RefSeq; NP_001127616.1; NM_001134144.1.
DR   AlphaFoldDB; Q5R5H5; -.
DR   SMR; Q5R5H5; -.
DR   STRING; 9601.ENSPPYP00000002529; -.
DR   Ensembl; ENSPPYT00000002604; ENSPPYP00000002529; ENSPPYG00000002172.
DR   GeneID; 100174695; -.
DR   KEGG; pon:100174695; -.
DR   CTD; 22931; -.
DR   eggNOG; KOG0080; Eukaryota.
DR   GeneTree; ENSGT00940000157325; -.
DR   HOGENOM; CLU_041217_10_7_1; -.
DR   InParanoid; Q5R5H5; -.
DR   OMA; HRTLFIE; -.
DR   OrthoDB; 1247169at2759; -.
DR   TreeFam; TF313448; -.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Developmental protein; GTP-binding;
KW   Lipid droplet; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Palmitate; Phosphoprotein; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..203
FT                   /note="Ras-related protein Rab-18"
FT                   /id="PRO_0000121195"
FT   PROPEP          204..206
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370763"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP72"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35293"
FT   MOD_RES         203
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           199
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  22977 MW;  D1B0F4866547DF77 CRC64;
     MDEDVLTTLK ILIIGESGVG KSSLLLRFTD DTFDPELAAT IGVDFKVKTI SVDGNKAKLA
     IWDTAGQERF RTLTPSYYRG AQGVILVYDV TRRDTFVKLD NWLNELETYC TRNDIVNMLV
     GNKIDKENRE VDRNEGLKFA RKHSMLFIEA SAKTCDGVQC AFEELVEKII QTPGLWESEN
     QNKGVKLSHR EEGQGGGACG GYCSVL