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 27-MAR-2024, entry version 218. 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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24891604; DOI=10.1083/jcb.201403026; RA Gerondopoulos A., Bastos R.N., Yoshimura S., Anderson R., Carpanini S., RA Aligianis I., Handley M.T., Barr F.A.; RT "Rab18 and a Rab18 GEF complex are required for normal ER structure."; RL J. Cell Biol. 205:707-720(2014). RN [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes (PubMed:24891604, PubMed:30970241). Rabs cycle CC between an inactive GDP-bound form and an active GTP-bound form that is CC able to recruit to membranes different sets of downstream effectors CC directly responsible for vesicle formation, movement, tethering and CC fusion (PubMed:24891604, PubMed:30970241). Required for the CC localization of ZFYVE1 to lipid droplets and for its function in CC mediating the formation of endoplasmic reticulum-lipid droplets (ER-LD) CC contacts (PubMed:30970241). Also required for maintaining endoplasmic CC reticulum structure (PubMed:24891604). Plays a role in apical CC endocytosis/recycling (By similarity). Plays a key role in eye and CC brain development and neurodegeneration (PubMed:21473985). CC {ECO:0000250|UniProtKB:P35293, ECO:0000269|PubMed:21473985, CC ECO:0000269|PubMed:24891604, 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}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:24891604}. 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}. 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; 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; 166. DR DIP; DIP-60514N; -. DR IntAct; Q9NP72; 47. DR MINT; Q9NP72; -. DR STRING; 9606.ENSP00000478479; -. 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 PeptideAtlas; Q9NP72; -. DR ProteomicsDB; 6488; -. DR ProteomicsDB; 81906; -. [Q9NP72-1] DR ProteomicsDB; 81907; -. [Q9NP72-2] DR Pumba; Q9NP72; -. DR Antibodypedia; 12749; 235 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 AGR; HGNC:14244; -. 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; RVHKMDV; -. DR OrthoDB; 20696at2759; -. 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; 165 hits in 1165 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 196 other cell types or tissues. DR ExpressionAtlas; Q9NP72; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. 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 CDD; cd01863; Rab18; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF80; RAS-RELATED PROTEIN RAB-18; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. 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. DR Genevisible; Q9NP72; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; KW Developmental protein; Direct protein sequencing; Endoplasmic reticulum; KW GTP-binding; Host-virus interaction; Lipid droplet; Lipoprotein; Membrane; KW Methylation; 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; abnormal endoplasmic reticulum FT structure; in fibroblasts ER spread away from the FT perinuclear region into the cell periphery and there is a FT loss of fragmentation of ER tubules; 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; uncertain 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 //