RAB18_HUMAN
ID RAB18_HUMAN Reviewed; 206 AA.
AC Q9NP72; B3KMC7; B7Z333; D3DRW1; Q53FX8; Q56UN9; Q6FIH1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Ras-related protein Rab-18;
DE Flags: Precursor;
GN Name=RAB18;
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 [GENOMIC DNA].
RA Chikri M.M., Boutin M.P., Vaxillaire M.M., Froguel M.P.;
RT "In silico cloning of the human Rab18 gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10648831; DOI=10.1016/s0014-5793(99)01778-0;
RA Schaefer U., Seibold S., Schneider A., Neugebauer E.;
RT "Isolation and characterisation of the human rab18 gene after stimulation
RT of endothelial cells with histamine.";
RL FEBS Lett. 466:148-154(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=16147880; DOI=10.1080/10425170500061681;
RA Dou T., Ji C., Gu S., Chen F., Xu J., Ye X., Ying K., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel splice variant of human Rab18 gene
RT (RAB18).";
RL DNA Seq. 16:230-234(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Cui W.C., Yu L., Liu Q., Lin W., Han X.F., Zhao S.Y.;
RT "Cloning and expression of a novel human cDNA homologous to murine ras-
RT related protein (rab18) mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus, and 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 [15]
RP PROTEIN SEQUENCE OF 1-21; 59-69 AND 99-123, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=23935497; DOI=10.1371/journal.ppat.1003513;
RA Salloum S., Wang H., Ferguson C., Parton R.G., Tai A.W.;
RT "Rab18 binds to hepatitis C virus NS5A and promotes interaction between
RT sites of viral replication and lipid droplets.";
RL PLoS Pathog. 9:e1003513-e1003513(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP INTERACTION WITH ZFYVE1.
RX PubMed=31293035; DOI=10.1002/cbin.11199;
RA Gao G., Sheng Y., Yang H., Chua B.T., Xu L.;
RT "DFCP1 associates with lipid droplets.";
RL Cell Biol. Int. 0:0-0(2019).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZW10; ZFYVE1 AND BSCL2,
RP AND MUTAGENESIS OF SER-22 AND GLN-67.
RX PubMed=30970241; DOI=10.1016/j.celrep.2019.03.025;
RA Li D., Zhao Y.G., Li D., Zhao H., Huang J., Miao G., Feng D., Liu P.,
RA Li D., Zhang H.;
RT "The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact
RT Formation.";
RL Cell Rep. 27:343-358(2019).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1-184 IN COMPLEX WITH GTP ANALOG.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of human RAB18 in complex with GPPNHP.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [23]
RP VARIANTS WARBM3 GLN-24 AND ARG-93 DEL, AND FUNCTION.
RX PubMed=21473985; DOI=10.1016/j.ajhg.2011.03.012;
RA Bem D., Yoshimura S., Nunes-Bastos R., Bond F.C., Kurian M.A., Rahman F.,
RA Handley M.T., Hadzhiev Y., Masood I., Straatman-Iwanowska A.A.,
RA Cullinane A.R., McNeill A., Pasha S.S., Kirby G.A., Foster K., Ahmed Z.,
RA Morton J.E., Williams D., Graham J.M., Dobyns W.B., Burglen L.,
RA Ainsworth J.R., Gissen P., Muller F., Maher E.R., Barr F.A.,
RA Aligianis I.A.;
RT "Loss-of-function mutations in RAB18 cause Warburg micro syndrome.";
RL Am. J. Hum. Genet. 88:499-507(2011).
RN [24]
RP VARIANT WARBM3 MET-95.
RX PubMed=23420520; DOI=10.1002/humu.22296;
RA Handley M.T., Morris-Rosendahl D.J., Brown S., Macdonald F., Hardy C.,
RA Bem D., Carpanini S.M., Borck G., Martorell L., Izzi C., Faravelli F.,
RA Accorsi P., Pinelli L., Basel-Vanagaite L., Peretz G., Abdel-Salam G.M.,
RA Zaki M.S., Jansen A., Mowat D., Glass I., Stewart H., Mancini G.,
RA Lederer D., Roscioli T., Giuliano F., Plomp A.S., Rolfs A., Graham J.M.,
RA Seemanova E., Poo P., Garcia-Cazorla A., Edery P., Jackson I.J.,
RA Maher E.R., Aligianis I.A.;
RT "Mutation spectrum in RAB3GAP1, RAB3GAP2, and RAB18 and genotype-phenotype
RT correlations in Warburg micro syndrome and Martsolf syndrome.";
RL Hum. Mutat. 34:686-696(2013).
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 (PubMed:30970241). Plays a role in
CC apical endocytosis/recycling (By similarity). Plays a key role in eye
CC and brain development and neurodegeneration (PubMed:21473985).
CC {ECO:0000250|UniProtKB:P35293, ECO:0000250|UniProtKB:Q8MXS1,
CC ECO:0000269|PubMed:21473985, ECO:0000269|PubMed:30970241}.
CC -!- SUBUNIT: Interacts (in GTP-bound form) with ZFYVE1 (PubMed:31293035,
CC PubMed:30970241). Interacts with ZW10 and this interaction is enhanced
CC in the presence of ZFYVE1 (PubMed:30970241). Interacts with BSCL2
CC (PubMed:30970241). {ECO:0000269|PubMed:30970241,
CC ECO:0000269|PubMed:31293035}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hepatitis C virus (HCV)
CC non-structural protein 5A; this interaction may promote the association
CC of NS5A and other viral replicase components with lipid droplets.
CC {ECO:0000269|PubMed:23935497}.
CC -!- INTERACTION:
CC Q9NP72; Q13520: AQP6; NbExp=3; IntAct=EBI-722247, EBI-13059134;
CC Q9NP72; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-722247, EBI-18535450;
CC Q9NP72; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-722247, EBI-529518;
CC Q9NP72; PRO_0000045602 [Q99IB8]; Xeno; NbExp=5; IntAct=EBI-722247, EBI-6927873;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P35293}. Lipid droplet
CC {ECO:0000269|PubMed:23935497, ECO:0000269|PubMed:30970241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NP72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP72-2; Sequence=VSP_043912;
CC Name=3;
CC IsoId=Q9NP72-3; Sequence=VSP_044883;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Warburg micro syndrome 3 (WARBM3) [MIM:614222]: A rare
CC syndrome characterized by microcephaly, microphthalmia, microcornia,
CC congenital cataracts, optic atrophy, cortical dysplasia, in particular
CC corpus callosum hypoplasia, severe intellectual disability, spastic
CC diplegia, and hypogonadism. {ECO:0000269|PubMed:21473985,
CC ECO:0000269|PubMed:23420520}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Highly expressed in testis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ277145; CAB86486.1; -; Genomic_DNA.
DR EMBL; AJ277146; CAB86486.1; JOINED; Genomic_DNA.
DR EMBL; AJ277147; CAB86486.1; JOINED; Genomic_DNA.
DR EMBL; AJ277148; CAB86486.1; JOINED; Genomic_DNA.
DR EMBL; AJ277149; CAB86486.1; JOINED; Genomic_DNA.
DR EMBL; AF137372; AAF61433.1; -; mRNA.
DR EMBL; AY574034; AAU08232.1; -; mRNA.
DR EMBL; AF087860; AAP97170.1; -; mRNA.
DR EMBL; AF498950; AAM21098.1; -; mRNA.
DR EMBL; AF136974; AAG49435.1; -; mRNA.
DR EMBL; AL136734; CAB66668.1; -; mRNA.
DR EMBL; BT009840; AAP88842.1; -; mRNA.
DR EMBL; CR533455; CAG38486.1; -; mRNA.
DR EMBL; AK001555; BAG50939.1; -; mRNA.
DR EMBL; AK295443; BAH12069.1; -; mRNA.
DR EMBL; AK223153; BAD96873.1; -; mRNA.
DR EMBL; AL138920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86054.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86055.1; -; Genomic_DNA.
DR EMBL; BC015014; AAH15014.1; -; mRNA.
DR EMBL; BC029350; AAH29350.1; -; mRNA.
DR CCDS; CCDS58073.1; -. [Q9NP72-3]
DR CCDS; CCDS7155.1; -. [Q9NP72-1]
DR CCDS; CCDS73081.1; -. [Q9NP72-2]
DR RefSeq; NP_001243339.1; NM_001256410.1. [Q9NP72-2]
DR RefSeq; NP_001243340.1; NM_001256411.1.
DR RefSeq; NP_001243341.1; NM_001256412.1. [Q9NP72-3]
DR RefSeq; NP_001243344.1; NM_001256415.1.
DR RefSeq; NP_067075.1; NM_021252.4. [Q9NP72-1]
DR PDB; 1X3S; X-ray; 1.32 A; A=1-182.
DR PDBsum; 1X3S; -.
DR AlphaFoldDB; Q9NP72; -.
DR SMR; Q9NP72; -.
DR BioGRID; 116591; 145.
DR DIP; DIP-60514N; -.
DR IntAct; Q9NP72; 43.
DR MINT; Q9NP72; -.
DR iPTMnet; Q9NP72; -.
DR PhosphoSitePlus; Q9NP72; -.
DR SwissPalm; Q9NP72; -.
DR BioMuta; RAB18; -.
DR DMDM; 12230528; -.
DR EPD; Q9NP72; -.
DR jPOST; Q9NP72; -.
DR MassIVE; Q9NP72; -.
DR MaxQB; Q9NP72; -.
DR PaxDb; Q9NP72; -.
DR PeptideAtlas; Q9NP72; -.
DR PRIDE; Q9NP72; -.
DR ProteomicsDB; 6488; -.
DR ProteomicsDB; 81906; -. [Q9NP72-1]
DR ProteomicsDB; 81907; -. [Q9NP72-2]
DR Antibodypedia; 12749; 204 antibodies from 28 providers.
DR DNASU; 22931; -.
DR Ensembl; ENST00000356940.11; ENSP00000349415.7; ENSG00000099246.18. [Q9NP72-1]
DR Ensembl; ENST00000621805.5; ENSP00000478479.1; ENSG00000099246.18. [Q9NP72-2]
DR Ensembl; ENST00000682082.1; ENSP00000507542.1; ENSG00000099246.18. [Q9NP72-1]
DR Ensembl; ENST00000682389.1; ENSP00000507154.1; ENSG00000099246.18. [Q9NP72-3]
DR GeneID; 22931; -.
DR KEGG; hsa:22931; -.
DR MANE-Select; ENST00000356940.11; ENSP00000349415.7; NM_021252.5; NP_067075.1.
DR UCSC; uc001itv.5; human. [Q9NP72-1]
DR CTD; 22931; -.
DR DisGeNET; 22931; -.
DR GeneCards; RAB18; -.
DR GeneReviews; RAB18; -.
DR HGNC; HGNC:14244; RAB18.
DR HPA; ENSG00000099246; Low tissue specificity.
DR MalaCards; RAB18; -.
DR MIM; 602207; gene.
DR MIM; 614222; phenotype.
DR neXtProt; NX_Q9NP72; -.
DR OpenTargets; ENSG00000099246; -.
DR Orphanet; 2510; Micro syndrome.
DR PharmGKB; PA34106; -.
DR VEuPathDB; HostDB:ENSG00000099246; -.
DR GeneTree; ENSGT00940000157325; -.
DR InParanoid; Q9NP72; -.
DR OMA; HRTLFIE; -.
DR OrthoDB; 1247169at2759; -.
DR PhylomeDB; Q9NP72; -.
DR TreeFam; TF313448; -.
DR PathwayCommons; Q9NP72; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q9NP72; -.
DR BioGRID-ORCS; 22931; 163 hits in 1084 CRISPR screens.
DR ChiTaRS; RAB18; human.
DR EvolutionaryTrace; Q9NP72; -.
DR GeneWiki; RAB18; -.
DR GenomeRNAi; 22931; -.
DR Pharos; Q9NP72; Tbio.
DR PRO; PR:Q9NP72; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NP72; protein.
DR Bgee; ENSG00000099246; Expressed in adrenal tissue and 194 other tissues.
DR ExpressionAtlas; Q9NP72; baseline and differential.
DR Genevisible; Q9NP72; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Developmental protein; Direct protein sequencing; GTP-binding;
KW Host-virus interaction; Lipid droplet; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..203
FT /note="Ras-related protein Rab-18"
FT /id="PRO_0000121193"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370761"
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 BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PubMed:22223895"
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"
FT VAR_SEQ 62
FT /note="W -> WVTLHQQTANFFLKSQIGNSPILKWAMWQY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16147880"
FT /id="VSP_043912"
FT VAR_SEQ 63..126
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044883"
FT VARIANT 24
FT /note="L -> Q (in WARBM3; dbSNP:rs387906832)"
FT /evidence="ECO:0000269|PubMed:21473985"
FT /id="VAR_066495"
FT VARIANT 93
FT /note="Missing (in WARBM3; dbSNP:rs587776875)"
FT /evidence="ECO:0000269|PubMed:21473985"
FT /id="VAR_066496"
FT VARIANT 95
FT /note="T -> M (in WARBM3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23420520"
FT /id="VAR_086022"
FT VARIANT 113
FT /note="N -> S (in dbSNP:rs12268932)"
FT /id="VAR_051713"
FT VARIANT 198
FT /note="A -> T (in dbSNP:rs11015859)"
FT /id="VAR_034432"
FT MUTAGEN 22
FT /note="S->N: Loss of localization to lipid droplets and
FT interaction with ZFYVE1."
FT /evidence="ECO:0000269|PubMed:30970241"
FT MUTAGEN 67
FT /note="Q->L: No loss of localization to lipid droplets and
FT interaction with ZFYVE1."
FT /evidence="ECO:0000269|PubMed:30970241"
FT CONFLICT 61
FT /note="I -> L (in Ref. 11; BAD96873)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1X3S"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1X3S"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1X3S"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1X3S"
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
