ID RAB17_MOUSE Reviewed; 214 AA.
AC P35292; Q921D2; Q9D723;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 197.
DE RecName: Full=Ras-related protein Rab-17;
GN Name=Rab17;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8486736; DOI=10.1083/jcb.121.3.553;
RA Luetcke A., Jansson S., Parton R.G., Chavrier P., Valencia A., Huber L.A.,
RA Lehtonen E., Zerial M.;
RT "Rab17, a novel small GTPase, is specific for epithelial cells and is
RT induced during cell polarization.";
RL J. Cell Biol. 121:553-564(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.
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 [5]
RP FUNCTION IN TRANSCYTOSIS, SUBCELLULAR LOCATION, TOPOLOGY, ISOPRENYLATION AT
RP CYS-211 AND CYS-212, AND MUTAGENESIS OF 211-CYS-CYS-212.
RX PubMed=9624171; DOI=10.1074/jbc.273.25.15734;
RA Hunziker W., Peters P.J.;
RT "Rab17 localizes to recycling endosomes and regulates receptor-mediated
RT transcytosis in epithelial cells.";
RL J. Biol. Chem. 273:15734-15741(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9490718; DOI=10.1083/jcb.140.5.1039;
RA Zacchi P., Stenmark H., Parton R.G., Orioli D., Lim F., Giner A.,
RA Mellman I., Zerial M., Murphy C.;
RT "Rab17 regulates membrane trafficking through apical recycling endosomes in
RT polarized epithelial cells.";
RL J. Cell Biol. 140:1039-1053(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
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).
RN [8]
RP FUNCTION IN MELANOSOME TRANSPORT, AND SUBCELLULAR LOCATION.
RX PubMed=21291502; DOI=10.1111/j.1600-0854.2011.01172.x;
RA Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N.,
RA Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T.,
RA Sturm R.A., Stow J.L.;
RT "The recycling endosome protein Rab17 regulates melanocytic filopodia
RT formation and melanosome trafficking.";
RL Traffic 12:627-643(2011).
RN [9]
RP FUNCTION IN DENDRITOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLN-77.
RX PubMed=22291024; DOI=10.1074/jbc.m111.314385;
RA Mori Y., Matsui T., Furutani Y., Yoshihara Y., Fukuda M.;
RT "Small GTPase Rab17 regulates dendritic morphogenesis and postsynaptic
RT development of hippocampal neurons.";
RL J. Biol. Chem. 287:8963-8973(2012).
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. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC transcytosis, the directed movement of endocytosed material through the
CC cell and its exocytosis from the plasma membrane at the opposite side.
CC Mainly observed in epithelial cells, transcytosis mediates for
CC instance, the transcellular transport of immunoglobulins from the
CC basolateral surface to the apical surface. Most probably controls
CC membrane trafficking through apical recycling endosomes in a post-
CC endocytic step of transcytosis. Required for melanosome transport and
CC release from melanocytes, it also regulates dendrite and dendritic
CC spine development. May also play a role in cell migration.
CC {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024,
CC ECO:0000269|PubMed:9490718, ECO:0000269|PubMed:9624171}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024,
CC ECO:0000269|PubMed:9490718, ECO:0000269|PubMed:9624171}; Lipid-anchor
CC {ECO:0000305|PubMed:9624171}; Cytoplasmic side
CC {ECO:0000305|PubMed:9624171}. Melanosome {ECO:0000269|PubMed:21291502}.
CC Cell projection, dendrite {ECO:0000269|PubMed:22291024}. Note=According
CC to a report the protein is localized at the basolateral and apical
CC plasma membrane of kidney epithelial cells (PubMed:8486736). It was
CC later shown to localize to the apical recycling endosome in epithelial
CC cells (PubMed:21291502). In neurons, localizes to the cell body and
CC dendritic shaft and spine (PubMed:22291024).
CC {ECO:0000269|PubMed:21291502, ECO:0000269|PubMed:22291024,
CC ECO:0000269|PubMed:8486736}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, and intestine mainly by
CC epithelial cells. Expressed in hippocampus (at protein level).
CC {ECO:0000269|PubMed:22291024, ECO:0000269|PubMed:8486736}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 5 dpc and gradually increases
CC from P5 to adulthood (at protein level). {ECO:0000269|PubMed:22291024}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X70804; CAA50071.1; -; mRNA.
DR EMBL; AK009707; BAB26452.1; -; mRNA.
DR EMBL; AK075591; BAC35842.1; -; mRNA.
DR EMBL; BC013170; AAH13170.1; -; mRNA.
DR EMBL; BC051071; AAH51071.1; -; mRNA.
DR EMBL; M79307; AAK14831.1; -; mRNA.
DR CCDS; CCDS15156.1; -.
DR PIR; A46434; A46434.
DR RefSeq; NP_001153197.2; NM_001159725.2.
DR RefSeq; NP_033024.1; NM_008998.4.
DR RefSeq; XP_006529326.1; XM_006529263.2.
DR AlphaFoldDB; P35292; -.
DR SMR; P35292; -.
DR BioGRID; 202535; 2.
DR IntAct; P35292; 27.
DR MINT; P35292; -.
DR STRING; 10090.ENSMUSP00000027529; -.
DR iPTMnet; P35292; -.
DR PhosphoSitePlus; P35292; -.
DR jPOST; P35292; -.
DR PaxDb; 10090-ENSMUSP00000027529; -.
DR PeptideAtlas; P35292; -.
DR ProteomicsDB; 300288; -.
DR ABCD; P35292; 20 sequenced antibodies.
DR Antibodypedia; 34483; 306 antibodies from 31 providers.
DR DNASU; 19329; -.
DR Ensembl; ENSMUST00000027529.12; ENSMUSP00000027529.6; ENSMUSG00000026304.14.
DR Ensembl; ENSMUST00000131428.8; ENSMUSP00000122178.2; ENSMUSG00000026304.14.
DR GeneID; 19329; -.
DR KEGG; mmu:19329; -.
DR UCSC; uc007bzn.2; mouse.
DR AGR; MGI:104640; -.
DR CTD; 64284; -.
DR MGI; MGI:104640; Rab17.
DR VEuPathDB; HostDB:ENSMUSG00000026304; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000161839; -.
DR InParanoid; P35292; -.
DR OMA; SCCKVGP; -.
DR OrthoDB; 5483572at2759; -.
DR PhylomeDB; P35292; -.
DR TreeFam; TF300199; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19329; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Rab17; mouse.
DR PRO; PR:P35292; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P35292; Protein.
DR Bgee; ENSMUSG00000026304; Expressed in submandibular gland and 122 other cell types or tissues.
DR ExpressionAtlas; P35292; baseline and differential.
DR Genevisible; P35292; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA: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; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0032401; P:establishment of melanosome localization; IMP:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IMP:UniProtKB.
DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0045056; P:transcytosis; IMP:UniProtKB.
DR CDD; cd01860; Rab5_related; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR PANTHER; PTHR47979:SF124; RAS-RELATED PROTEIN RAB-5C-LIKE; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
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.
PE 1: Evidence at protein level;
KW Cell projection; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..214
FT /note="Ras-related protein Rab-17"
FT /id="PRO_0000121192"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 47..55
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:9624171"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:9624171"
FT MUTAGEN 77
FT /note="Q->L: Probable constitutively active mutant unable
FT to hydrolyze GTP; increases dendrite number and length."
FT /evidence="ECO:0000269|PubMed:22291024"
FT MUTAGEN 211..212
FT /note="CC->AA: Loss of association with membranes and
FT redistribution to the cytosol."
FT /evidence="ECO:0000269|PubMed:9624171"
FT CONFLICT 19
FT /note="V -> L (in Ref. 3; BAC35842)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="T -> K (in Ref. 2; BAB26452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23640 MW; 11052D3EC730EFAB CRC64;
MAQAAGLPQA STASGQPYVS KLVLLGSSSV GKTSLALRYM KQDFSNVLPT VGCAFFTKVL
DLGSSSLKLE IWDTAGQEKY QSVCHLYFRG ANAALLVYDI TRKDSFHKAQ QWLEDLEKEF
QPGEVVVMLV GNKTDLGEER EVTFQEGKEF AESKSLLFME TSAKLNYQVS EIFNTVAQEL
LQRAGDTGSS RPQEGEAVAL NQEPPIRQRQ CCAR
//
