RAB18_MOUSE
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 03-AUG-2022, entry version 192.
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, Pancreas,
RC 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: 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:0000269|PubMed:7706395}. Lipid droplet
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; 12.
DR IntAct; P35293; 11.
DR MINT; P35293; -.
DR STRING; 10090.ENSMUSP00000095285; -.
DR iPTMnet; P35293; -.
DR PhosphoSitePlus; P35293; -.
DR SwissPalm; P35293; -.
DR EPD; P35293; -.
DR jPOST; P35293; -.
DR PaxDb; P35293; -.
DR PeptideAtlas; P35293; -.
DR PRIDE; P35293; -.
DR ProteomicsDB; 300289; -.
DR Antibodypedia; 12749; 204 antibodies from 28 providers.
DR DNASU; 19330; -.
DR Ensembl; ENSMUST00000234810; ENSMUSP00000157011; ENSMUSG00000073639.
DR GeneID; 19330; -.
DR KEGG; mmu:19330; -.
DR UCSC; uc008dzo.2; mouse.
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; 1247169at2759; -.
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 73 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 264 other tissues.
DR ExpressionAtlas; P35293; baseline and differential.
DR Genevisible; P35293; MM.
DR GO; GO:0016324; C:apical plasma 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 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 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_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
