ID   RAB18_MOUSE             Reviewed;         206 AA.
AC   P35293; Q543V0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Ras-related protein Rab-18;
DE   Flags: Precursor;
GN   Name=Rab18;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=7706395; DOI=10.1242/jcs.107.12.3437;
RA   Luetcke A., Parton R.G., Murphy C., Olkkonen V.M., Dupree P., Valencia A.,
RA   Simons K., Zerial M.;
RT   "Cloning and subcellular localization of novel rab proteins reveals
RT   polarized and cell type-specific expression.";
RL   J. Cell Sci. 107:3437-3448(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=LAF1; TISSUE=Pituitary;
RX   PubMed=7916717; DOI=10.1016/0378-1119(93)90207-j;
RA   Yu H., Leaf D.S., Moore H.P.;
RT   "Gene cloning and characterization of a GTP-binding Rab protein from mouse
RT   pituitary AtT-20 cells.";
RL   Gene 132:273-278(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2J, and NOD;
RC   TISSUE=Corpora quadrigemina, Head, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
RC   TISSUE=Kidney;
RX   PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT   by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). Rabs cycle between an inactive
CC       GDP-bound form and an active GTP-bound form that is able to recruit to
CC       membranes different sets of downstream effectors directly responsible
CC       for vesicle formation, movement, tethering and fusion (By similarity).
CC       Required for the localization of ZFYVE1 to lipid droplets and for its
CC       function in mediating the formation of endoplasmic reticulum-lipid
CC       droplets (ER-LD) contacts (By similarity). Also required for
CC       maintaining endoplasmic reticulum structure (By similarity). Plays a
CC       role in apical endocytosis/recycling (PubMed:7706395). Plays a key role
CC       in eye and brain development and neurodegeneration (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NP72, ECO:0000269|PubMed:7706395}.
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:0000269|PubMed:7706395}. Lipid droplet
CC       {ECO:0000250|UniProtKB:Q9NP72}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9NP72}.
CC   -!- TISSUE SPECIFICITY: Expression is high in the brain, moderate in the
CC       pituitary, and low in the liver. Detected in all tissues. Highly
CC       enriched on apical endocytic structures in polarized epithelial cells
CC       of kidney proximal tubules. Detected on both the apical and basolateral
CC       domains in epithelial cells of the intestine.
CC       {ECO:0000269|PubMed:7706395, ECO:0000269|PubMed:7916717}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; X80333; CAA56583.1; -; mRNA.
DR   EMBL; L04966; AAC37632.1; -; mRNA.
DR   EMBL; AK045514; BAC32402.1; -; mRNA.
DR   EMBL; AK140901; BAE24512.1; -; mRNA.
DR   EMBL; AK143673; BAE25489.1; -; mRNA.
DR   EMBL; AK146177; BAE26955.1; -; mRNA.
DR   EMBL; AK146397; BAE27140.1; -; mRNA.
DR   EMBL; AK154920; BAE32926.1; -; mRNA.
DR   EMBL; BC056351; AAH56351.1; -; mRNA.
DR   EMBL; M79308; AAK14832.1; -; mRNA.
DR   CCDS; CCDS29044.1; -.
DR   PIR; JN0874; JN0874.
DR   RefSeq; NP_851415.1; NM_181070.6.
DR   AlphaFoldDB; P35293; -.
DR   SMR; P35293; -.
DR   BioGRID; 202536; 582.
DR   IntAct; P35293; 11.
DR   MINT; P35293; -.
DR   STRING; 10090.ENSMUSP00000157011; -.
DR   GlyGen; P35293; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35293; -.
DR   PhosphoSitePlus; P35293; -.
DR   SwissPalm; P35293; -.
DR   EPD; P35293; -.
DR   jPOST; P35293; -.
DR   PaxDb; 10090-ENSMUSP00000095285; -.
DR   PeptideAtlas; P35293; -.
DR   ProteomicsDB; 300289; -.
DR   Pumba; P35293; -.
DR   Antibodypedia; 12749; 235 antibodies from 28 providers.
DR   DNASU; 19330; -.
DR   Ensembl; ENSMUST00000234810.2; ENSMUSP00000157011.2; ENSMUSG00000073639.7.
DR   GeneID; 19330; -.
DR   KEGG; mmu:19330; -.
DR   UCSC; uc008dzo.2; mouse.
DR   AGR; MGI:102790; -.
DR   CTD; 22931; -.
DR   MGI; MGI:102790; Rab18.
DR   VEuPathDB; HostDB:ENSMUSG00000073639; -.
DR   eggNOG; KOG0080; Eukaryota.
DR   GeneTree; ENSGT00940000157325; -.
DR   HOGENOM; CLU_041217_10_7_1; -.
DR   InParanoid; P35293; -.
DR   OrthoDB; 20696at2759; -.
DR   PhylomeDB; P35293; -.
DR   TreeFam; TF313448; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 19330; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Rab18; mouse.
DR   PRO; PR:P35293; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P35293; Protein.
DR   Bgee; ENSMUSG00000073639; Expressed in embryonic brain and 268 other cell types or tissues.
DR   ExpressionAtlas; P35293; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
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; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISO:MGI.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0051170; P:import into nucleus; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0034389; P:lipid droplet organization; ISO:MGI.
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; P35293; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Developmental protein; Endoplasmic reticulum;
KW   GTP-binding; 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_0000121194"
FT   PROPEP          204..206
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370762"
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:0007744|PubMed:21183079"
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;  23035 MW;  D1B0F48666999B77 CRC64;
     MDEDVLTTLK ILIIGESGVG KSSLLLRFTD DTFDPELAAT IGVDFKVKTI SVDGNKAKLA
     IWDTAGQERF RTLTPSYYRG AQGVILVYDV TRRDTFVKLD NWLNELETYC TRNDIVNMLV
     GNKIDKENRE VDRNEGLKFA RKHSMLFIEA SAKTCDGVQC AFEELVEKII QTPGLWESEN
     QNKGVKLSHR EESRGGGACG GYCSVL
//