RAB10_MOUSE
ID RAB10_MOUSE Reviewed; 200 AA.
AC P61027; O88386; Q9D7X6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ras-related protein Rab-10;
DE EC=3.6.5.2;
GN Name=Rab10;
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].
RA Zeng Q., Tan Y.H., Hong W.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, Stomach, and Thymus;
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 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 [4]
RP PROTEIN SEQUENCE OF 12-22; 60-70; 96-102; 106-117 AND 148-172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP FUNCTION IN GLUT4 TRANSPORT, AND MUTAGENESIS OF GLN-68.
RX PubMed=17403373; DOI=10.1016/j.cmet.2007.03.001;
RA Sano H., Eguez L., Teruel M.N., Fukuda M., Chuang T.D., Chavez J.A.,
RA Lienhard G.E., McGraw T.E.;
RT "Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated
RT translocation of GLUT4 to the adipocyte plasma membrane.";
RL Cell Metab. 5:293-303(2007).
RN [6]
RP INTERACTION WITH GDI1 AND GDI2.
RX PubMed=19570034; DOI=10.1042/bj20090624;
RA Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.;
RT "GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4
RT translocation.";
RL Biochem. J. 422:229-235(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=20576682; DOI=10.1152/ajprenal.00198.2010;
RA Babbey C.M., Bacallao R.L., Dunn K.W.;
RT "Rab10 associates with primary cilia and the exocyst complex in renal
RT epithelial cells.";
RL Am. J. Physiol. 299:F495-506(2010).
RN [8]
RP IDENTIFICATION BY 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).
RN [9]
RP FUNCTION IN TRANSPORT TO THE PLASMA MEMBRANE, AND INDUCTION BY LPS.
RX PubMed=20643919; DOI=10.1073/pnas.1009428107;
RA Wang D., Lou J., Ouyang C., Chen W., Liu Y., Liu X., Cao X., Wang J.,
RA Lu L.;
RT "Ras-related protein Rab10 facilitates TLR4 signaling by promoting
RT replenishment of TLR4 onto the plasma membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13806-13811(2010).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=21454697; DOI=10.1074/jbc.c111.228908;
RA Sano H., Peck G.R., Kettenbach A.N., Gerber S.A., Lienhard G.E.;
RT "Insulin-stimulated GLUT4 protein translocation in adipocytes requires the
RT Rab10 guanine nucleotide exchange factor Dennd4C.";
RL J. Biol. Chem. 286:16541-16545(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH MYO5A.
RX PubMed=22908308; DOI=10.1083/jcb.201111091;
RA Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S.,
RA Hammer J.A., Xu T., Lippincott-Schwartz J.;
RT "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle
RT translocation in adipocytes.";
RL J. Cell Biol. 198:545-560(2012).
RN [12]
RP INTERACTION WITH TBC1D13.
RX PubMed=22762500; DOI=10.1111/j.1600-0854.2012.01397.x;
RA Davey J.R., Humphrey S.J., Junutula J.R., Mishra A.K., Lambright D.G.,
RA James D.E., Stoeckli J.;
RT "TBC1D13 is a RAB35 specific GAP that plays an important role in GLUT4
RT trafficking in adipocytes.";
RL Traffic 13:1429-1441(2012).
RN [13]
RP PHOSPHORYLATION AT THR-73.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC16A.
RX PubMed=27354378; DOI=10.1083/jcb.201509052;
RA Bruno J., Brumfield A., Chaudhary N., Iaea D., McGraw T.E.;
RT "SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
RT trafficking in adipocytes.";
RL J. Cell Biol. 214:61-76(2016).
RN [15]
RP PHOSPHORYLATION AT THR-73.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30398148; DOI=10.7554/elife.40202;
RA Dhekne H.S., Yanatori I., Gomez R.C., Tonelli F., Diez F., Schuele B.,
RA Steger M., Alessi D.R., Pfeffer S.R.;
RT "A pathway for Parkinson's Disease LRRK2 kinase to block primary cilia and
RT Sonic hedgehog signaling in the brain.";
RL Elife 7:0-0(2018).
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 set of downstream effectors directly responsible
CC for vesicle formation, movement, tethering and fusion (By similarity).
CC That Rab is mainly involved in the biosynthetic transport of proteins
CC from the Golgi to the plasma membrane (By similarity). Regulates, for
CC instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery
CC to the plasma membrane (PubMed:17403373, PubMed:22908308,
CC PubMed:27354378). In parallel, it regulates the transport of TLR4, a
CC toll-like receptor to the plasma membrane and therefore may be
CC important for innate immune response (PubMed:20643919). Also plays a
CC specific role in asymmetric protein transport to the plasma membrane
CC (By similarity). In neurons, it is involved in axonogenesis through
CC regulation of vesicular membrane trafficking toward the axonal plasma
CC membrane (By similarity). In epithelial cells, it regulates transport
CC from the Golgi to the basolateral membrane (By similarity). May play a
CC role in the basolateral recycling pathway and in phagosome maturation
CC (By similarity). May play a role in endoplasmic reticulum dynamics and
CC morphology controlling tubulation along microtubules and tubules fusion
CC (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates
CC ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73,
CC it binds RILPL1 and inhibits ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P35281,
CC ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:17403373,
CC ECO:0000269|PubMed:20643919, ECO:0000269|PubMed:22908308,
CC ECO:0000269|PubMed:27354378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61026};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61026};
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP) (By similarity).
CC That Rab is activated by the DENND4C guanine exchange factor (GEF)
CC (Probable). That Rab is activated by the DENND4C and RABIF guanine
CC exchange factors (GEF) (By similarity). {ECO:0000250|UniProtKB:P61026,
CC ECO:0000269|PubMed:21454697, ECO:0000305}.
CC -!- SUBUNIT: Interacts with MYO5A; mediates the transport to the plasma
CC membrane of SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts
CC with GDI1; negatively regulates RAB10 association with membranes and
CC activation (PubMed:19570034). Interacts (GDP-bound form) with LLGL1;
CC the interaction is direct and promotes RAB10 association with membranes
CC and activation through competition with the Rab inhibitor GDI1 (By
CC similarity). Interacts with EXOC4; probably associates with the exocyst
CC (By similarity). Interacts (GTP-bound form) with MICALCL, MICAL1,
CC MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1 two molecules of
CC RAB10 can bind to one molecule of MICAL1 (By similarity). Interacts
CC with TBC1D13 (PubMed:22762500). Interacts with SEC16A
CC (PubMed:27354378). Interacts with GDI2, CHM and CHML (By similarity).
CC Interacts with LRRK2; interaction facilitates phosphorylation of Thr-73
CC (By similarity). Interacts with RILPL1 and RILPL2 when phosphorylated
CC on Thr-73 (By similarity). Interacts with TBC1D21 (By similarity).
CC {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P35281,
CC ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:19570034,
CC ECO:0000269|PubMed:22762500, ECO:0000269|PubMed:22908308,
CC ECO:0000269|PubMed:27354378}.
CC -!- INTERACTION:
CC P61027; P31150: GDI1; Xeno; NbExp=3; IntAct=EBI-911581, EBI-946999;
CC P61027; P50395: GDI2; Xeno; NbExp=3; IntAct=EBI-911581, EBI-1049143;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305|PubMed:20576682}; Cytoplasmic side
CC {ECO:0000305|PubMed:20576682}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane
CC {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:P24409}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:30398148}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:20576682}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}.
CC Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:27354378).
CC Localizes to the base of the cilium when phosphorylated by LRRK2 on
CC Thr-73 (PubMed:20576682, PubMed:27354378). Transiently associates with
CC phagosomes (By similarity). Localizes to the endoplasmic reticulum at
CC domains of new tubule growth (By similarity).
CC {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026,
CC ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:27354378}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, specifically neurons (at
CC protein level). {ECO:0000269|PubMed:30398148}.
CC -!- INDUCTION: Up-regulated by LPS. {ECO:0000269|PubMed:20643919}.
CC -!- PTM: Phosphorylation of Thr-73 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:P61026}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF035646; AAC29313.1; -; mRNA.
DR EMBL; AK008725; BAB25858.1; -; mRNA.
DR EMBL; AK028320; BAC25878.1; -; mRNA.
DR EMBL; AK087964; BAC40062.1; -; mRNA.
DR EMBL; BC056374; AAH56374.1; -; mRNA.
DR CCDS; CCDS25782.1; -.
DR RefSeq; NP_057885.1; NM_016676.5.
DR AlphaFoldDB; P61027; -.
DR SMR; P61027; -.
DR BioGRID; 202531; 15.
DR DIP; DIP-37720N; -.
DR IntAct; P61027; 24.
DR MINT; P61027; -.
DR STRING; 10090.ENSMUSP00000021001; -.
DR iPTMnet; P61027; -.
DR PhosphoSitePlus; P61027; -.
DR SwissPalm; P61027; -.
DR EPD; P61027; -.
DR jPOST; P61027; -.
DR PaxDb; P61027; -.
DR PeptideAtlas; P61027; -.
DR PRIDE; P61027; -.
DR ProteomicsDB; 300371; -.
DR Antibodypedia; 27788; 250 antibodies from 32 providers.
DR DNASU; 19325; -.
DR Ensembl; ENSMUST00000021001; ENSMUSP00000021001; ENSMUSG00000020671.
DR GeneID; 19325; -.
DR KEGG; mmu:19325; -.
DR UCSC; uc007mwl.2; mouse.
DR CTD; 10890; -.
DR MGI; MGI:105066; Rab10.
DR VEuPathDB; HostDB:ENSMUSG00000020671; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000156975; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61027; -.
DR OMA; HKMLIGN; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P61027; -.
DR TreeFam; TF314097; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 19325; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Rab10; mouse.
DR PRO; PR:P61027; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P61027; protein.
DR Bgee; ENSMUSG00000020671; Expressed in vastus lateralis and 253 other tissues.
DR ExpressionAtlas; P61027; baseline and differential.
DR Genevisible; P61027; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0051021; F:GDP-dissociation inhibitor binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0045055; P:regulated exocytosis; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
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 projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-10"
FT /id="PRO_0000121147"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 18..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT BINDING 35..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61026,
FT ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61026,
FT ECO:0000250|UniProtKB:Q9H0U4"
FT MOD_RES 73
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P61026"
FT MUTAGEN 68
FT /note="Q->L: Probable constitutively active mutant unable
FT to hydrolyze GTP; stimulates translocation of SLC2A4 to the
FT plasma membrane."
FT /evidence="ECO:0000269|PubMed:17403373"
FT CONFLICT 106
FT /note="N -> H (in Ref. 2; BAB25858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22541 MW; 7F02B8E8E46EE1E8 CRC64;
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT VELQGKKIKL
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI SKWLRNIDEH ANEDVERMLL
GNKCDMDDKR VVPKGKGEQI AREHGIRFFE TSAKANINIE KAFLTLAEDI LRKTPVKEPN
SENVDISSGG GVTGWKSKCC
