RAB10_HUMAN
ID RAB10_HUMAN Reviewed; 200 AA.
AC P61026; D6W538; O88386; Q6IA52; Q9D7X6; Q9H0T3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ras-related protein Rab-10;
DE EC=3.6.5.2 {ECO:0000269|PubMed:20937701};
GN Name=RAB10;
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 [MRNA].
RX PubMed=12450215; DOI=10.3727/000000002783992406;
RA He H., Dai F.Y., Yu L., She X., Zhao Y., Jiang J., Chen X., Zhao S.Y.;
RT "Identification and characterization of nine novel human small GTPases
RT showing variable expressions in liver cancer tissues.";
RL Gene Expr. 10:231-242(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wong K., Hong W., Tang B.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16641372; DOI=10.1091/mbc.e05-08-0799;
RA Babbey C.M., Ahktar N., Wang E., Chen C.C., Grant B.D., Dunn K.W.;
RT "Rab10 regulates membrane transport through early endosomes of polarized
RT Madin-Darby canine kidney cells.";
RL Mol. Biol. Cell 17:3156-3175(2006).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-23 AND GLN-68.
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 [14]
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [15]
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 [16]
RP FUNCTION.
RX PubMed=21248164; DOI=10.1152/physrev.00059.2009;
RA Hutagalung A.H., Novick P.J.;
RT "Role of Rab GTPases in membrane traffic and cell physiology.";
RL Physiol. Rev. 91:119-149(2011).
RN [17]
RP SUBCELLULAR LOCATION, 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 [18]
RP FUNCTION IN ENDOPLASMIC RETICULUM MEMBRANE DYNAMICS, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF THR-23.
RX PubMed=23263280; DOI=10.1038/ncb2647;
RA English A.R., Voeltz G.K.;
RT "Rab10 GTPase regulates ER dynamics and morphology.";
RL Nat. Cell Biol. 15:169-178(2013).
RN [19]
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 [20]
RP INTERACTION WITH LRRK2; GDI1 AND GDI2, PHOSPHORYLATION AT THR-73, AND
RP MUTAGENESIS OF 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 [21]
RP INTERACTION WITH GDI1; GDI2; CHM; CHML; RILPL1 AND RILPL2, PHOSPHORYLATION
RP AT THR-73, AND MUTAGENESIS OF 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 [22]
RP INTERACTION WITH TBC1D21, AND TISSUE SPECIFICITY.
RX PubMed=28067790; DOI=10.3390/ijms18010097;
RA Lin Y.H., Ke C.C., Wang Y.Y., Chen M.F., Chen T.M., Ku W.C., Chiang H.S.,
RA Yeh C.H.;
RT "RAB10 Interacts with the Male Germ Cell-Specific GTPase-Activating Protein
RT during Mammalian Spermiogenesis.";
RL Int. J. Mol. Sci. 18:0-0(2017).
RN [23]
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-73.
RX PubMed=29127255; DOI=10.1042/bcj20170803;
RA Fan Y., Howden A.J.M., Sarhan A.R., Lis P., Ito G., Martinez T.N.,
RA Brockmann K., Gasser T., Alessi D.R., Sammler E.M.;
RT "Interrogating Parkinson's disease LRRK2 kinase pathway activity by
RT assessing Rab10 phosphorylation in human neutrophils.";
RL Biochem. J. 475:23-44(2018).
RN [24]
RP FUNCTION, INTERACTION WITH RILPL1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-73, AND MUTAGENESIS OF THR-73.
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).
RN [25]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-73.
RX PubMed=29212815; DOI=10.15252/embj.201798099;
RA Purlyte E., Dhekne H.S., Sarhan A.R., Gomez R., Lis P., Wightman M.,
RA Martinez T.N., Tonelli F., Pfeffer S.R., Alessi D.R.;
RT "Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.";
RL EMBO J. 37:1-18(2018).
RN [26]
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-73.
RX PubMed=29562525; DOI=10.3233/jad-180023;
RA Yan T., Wang L., Gao J., Siedlak S.L., Huntley M.L., Termsarasab P.,
RA Perry G., Chen S.G., Wang X.;
RT "Rab10 Phosphorylation is a Prominent Pathological Feature in Alzheimer's
RT Disease.";
RL J. Alzheimers Dis. 63:157-165(2018).
RN [27]
RP FUNCTION (MICROBIAL INFECTION), ACTIVITY REGULATION, UBIQUITINATION AT
RP LYS-102; LYS-136 AND LYS-154, AND MUTAGENESIS OF THR-23 AND GLN-68.
RX PubMed=31540829; DOI=10.1016/j.chom.2019.08.017;
RA Jeng E.E., Bhadkamkar V., Ibe N.U., Gause H., Jiang L., Chan J., Jian R.,
RA Jimenez-Morales D., Stevenson E., Krogan N.J., Swaney D.L., Snyder M.P.,
RA Mukherjee S., Bassik M.C.;
RT "Systematic Identification of Host Cell Regulators of Legionella
RT pneumophila Pathogenesis Using a Genome-wide CRISPR Screen.";
RL Cell Host Microbe 26:551.E6-563.E6(2019).
RN [28]
RP PHOSPHORYLATION AT THR-73.
RX PubMed=30635421; DOI=10.1073/pnas.1817889116;
RA Zhang P., Fan Y., Ru H., Wang L., Magupalli V.G., Taylor S.S., Alessi D.R.,
RA Wu H.;
RT "Crystal structure of the WD40 domain dimer of LRRK2.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:1579-1584(2019).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH MICALCL, X-RAY
RP CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-175 IN COMPLEX WITH MICAL1, AND
RP INTERACTION WITH MICAL3; EHBP1 AND EHBP1L1.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
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:21248164). 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
CC (PubMed:21248164). That Rab is mainly involved in the biosynthetic
CC transport of proteins from the Golgi to the plasma membrane
CC (PubMed:21248164). Regulates, for instance, SLC2A4/GLUT4 glucose
CC transporter-enriched vesicles delivery to the plasma membrane (By
CC similarity). In parallel, it regulates the transport of TLR4, a toll-
CC like receptor to the plasma membrane and therefore may be important for
CC innate immune response (By similarity). Also plays a specific role in
CC asymmetric protein transport to the plasma membrane (PubMed:16641372).
CC In neurons, it is involved in axonogenesis through regulation of
CC vesicular membrane trafficking toward the axonal plasma membrane (By
CC similarity). In epithelial cells, it regulates transport from the Golgi
CC to the basolateral membrane (PubMed:16641372). May play a role in the
CC basolateral recycling pathway and in phagosome maturation (By
CC similarity). May play a role in endoplasmic reticulum dynamics and
CC morphology controlling tubulation along microtubules and tubules fusion
CC (PubMed:23263280). Together with LRRK2, RAB8A, and RILPL1, it regulates
CC ciliogenesis (PubMed:30398148). When phosphorylated by LRRK2 on Thr-73,
CC binds RILPL1 and inhibits ciliogenesis (PubMed:30398148).
CC {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61027,
CC ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164,
CC ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30398148}.
CC -!- FUNCTION: (Microbial infection) Upon Legionella pneumophila infection
CC promotes endoplasmic reticulum recruitment and bacterial replication.
CC Plays a role in remodeling the Legionella-containing vacuole (LCV) into
CC an endoplasmic reticulum-like vacuole. {ECO:0000269|PubMed:31540829}.
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:0000269|PubMed:20937701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:20937701};
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) (Probable). That
CC Rab is activated by the DENND4C and RABIF guanine exchange factors
CC (GEF) (PubMed:20937701, PubMed:31540829). {ECO:0000269|PubMed:20937701,
CC ECO:0000269|PubMed:31540829, 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 and with GDI2; negatively regulates RAB10 association with
CC membranes and activation (PubMed:19570034, PubMed:26824392,
CC PubMed:29125462). Interacts (GDP-bound form) with LLGL1; the
CC interaction is direct and promotes RAB10 association with membranes and
CC 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 (PubMed:27552051). Interacts
CC with TBC1D13 (By similarity). Interacts with SEC16A (By similarity).
CC Interacts with CHM and CHML (PubMed:29125462). Interacts with LRRK2;
CC interaction facilitates phosphorylation of Thr-73 (PubMed:26824392).
CC Interacts (when phosphorylated on Thr-73) with RILPL1 and RILPL2
CC (PubMed:30398148, PubMed:29125462). Interacts with TBC1D21
CC (PubMed:28067790). {ECO:0000250|UniProtKB:P24409,
CC ECO:0000250|UniProtKB:P35281, ECO:0000250|UniProtKB:P61027,
CC ECO:0000269|PubMed:19570034, ECO:0000269|PubMed:22908308,
CC ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27552051,
CC ECO:0000269|PubMed:28067790, ECO:0000269|PubMed:29125462,
CC ECO:0000269|PubMed:30398148}.
CC -!- INTERACTION:
CC P61026; Q5S007: LRRK2; NbExp=7; IntAct=EBI-726075, EBI-5323863;
CC P61026; Q96CV9: OPTN; NbExp=3; IntAct=EBI-726075, EBI-748974;
CC P61026; Q9ULR3: PPM1H; NbExp=4; IntAct=EBI-726075, EBI-8796752;
CC P61026; Q14964: RAB39A; NbExp=2; IntAct=EBI-726075, EBI-3048577;
CC P61026; Q969X0: RILPL2; NbExp=2; IntAct=EBI-726075, EBI-717552;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:23263280}. Golgi apparatus,
CC trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome
CC membrane {ECO:0000269|PubMed:16641372}. 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:23263280}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:29212815}.
CC Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:22908308).
CC Localizes to the base of the cilium when phosphorylated by LRRK2 on
CC Thr-73 (PubMed:20576682, PubMed:30398148). Transiently associates with
CC phagosomes (By similarity). Localizes to the endoplasmic reticulum at
CC domains of new tubule growth (PubMed:23263280).
CC {ECO:0000250|UniProtKB:P24409, ECO:0000269|PubMed:20576682,
CC ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:23263280,
CC ECO:0000269|PubMed:30398148}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus (PubMed:29562525).
CC Expressed in neutrophils (at protein level) (PubMed:29127255).
CC Expressed in the testis (at protein level) (PubMed:28067790).
CC {ECO:0000269|PubMed:28067790, ECO:0000269|PubMed:29127255,
CC ECO:0000269|PubMed:29562525}.
CC -!- PTM: Ubiquitinated upon Legionella pneumophila infection.
CC Ubiquitination does not lead to proteasomal degradation.
CC {ECO:0000269|PubMed:31540829}.
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:0000269|PubMed:26824392, ECO:0000269|PubMed:29125462}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF086917; AAP97147.1; -; mRNA.
DR EMBL; AF297660; AAG13413.1; -; mRNA.
DR EMBL; AF106681; AAD43034.1; -; mRNA.
DR EMBL; AL136650; CAB66585.1; -; mRNA.
DR EMBL; AK023223; BAB14474.1; -; mRNA.
DR EMBL; AF498945; AAM21093.1; -; mRNA.
DR EMBL; CR457303; CAG33584.1; -; mRNA.
DR EMBL; CH471053; EAX00710.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00711.1; -; Genomic_DNA.
DR EMBL; BC000896; AAH00896.1; -; mRNA.
DR CCDS; CCDS1720.1; -.
DR RefSeq; NP_057215.3; NM_016131.4.
DR PDB; 5LPN; X-ray; 2.80 A; A/C=1-175.
DR PDB; 5SZJ; X-ray; 2.66 A; A=1-200.
DR PDBsum; 5LPN; -.
DR PDBsum; 5SZJ; -.
DR AlphaFoldDB; P61026; -.
DR SASBDB; P61026; -.
DR SMR; P61026; -.
DR BioGRID; 116096; 144.
DR IntAct; P61026; 66.
DR MINT; P61026; -.
DR STRING; 9606.ENSP00000264710; -.
DR ChEMBL; CHEMBL4105971; -.
DR iPTMnet; P61026; -.
DR PhosphoSitePlus; P61026; -.
DR SwissPalm; P61026; -.
DR BioMuta; RAB10; -.
DR DMDM; 46577638; -.
DR EPD; P61026; -.
DR jPOST; P61026; -.
DR MassIVE; P61026; -.
DR MaxQB; P61026; -.
DR PaxDb; P61026; -.
DR PeptideAtlas; P61026; -.
DR PRIDE; P61026; -.
DR ProteomicsDB; 57255; -.
DR TopDownProteomics; P61026; -.
DR Antibodypedia; 27788; 250 antibodies from 32 providers.
DR DNASU; 10890; -.
DR Ensembl; ENST00000264710.5; ENSP00000264710.4; ENSG00000084733.11.
DR GeneID; 10890; -.
DR KEGG; hsa:10890; -.
DR MANE-Select; ENST00000264710.5; ENSP00000264710.4; NM_016131.5; NP_057215.3.
DR UCSC; uc002rgv.4; human.
DR CTD; 10890; -.
DR DisGeNET; 10890; -.
DR GeneCards; RAB10; -.
DR HGNC; HGNC:9759; RAB10.
DR HPA; ENSG00000084733; Low tissue specificity.
DR MIM; 612672; gene.
DR neXtProt; NX_P61026; -.
DR OpenTargets; ENSG00000084733; -.
DR PharmGKB; PA34100; -.
DR VEuPathDB; HostDB:ENSG00000084733; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000156975; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61026; -.
DR OMA; HKMLIGN; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P61026; -.
DR TreeFam; TF314097; -.
DR PathwayCommons; P61026; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P61026; -.
DR SIGNOR; P61026; -.
DR BioGRID-ORCS; 10890; 309 hits in 1089 CRISPR screens.
DR ChiTaRS; RAB10; human.
DR GeneWiki; RAB10; -.
DR GenomeRNAi; 10890; -.
DR Pharos; P61026; Tbio.
DR PRO; PR:P61026; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P61026; protein.
DR Bgee; ENSG00000084733; Expressed in epithelial cell of pancreas and 192 other tissues.
DR Genevisible; P61026; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
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:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP: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; IMP:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:UniProtKB.
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: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; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
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; ISS: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 3D-structure; Acetylation; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Membrane;
KW Neurodegeneration; 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_0000121146"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 18..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5LPN, ECO:0007744|PDB:5SZJ"
FT BINDING 35..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5LPN, ECO:0007744|PDB:5SZJ"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4,
FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5LPN,
FT ECO:0007744|PDB:5SZJ"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:27552051,
FT ECO:0007744|PDB:5LPN, ECO:0007744|PDB:5SZJ"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4,
FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:5LPN,
FT ECO:0007744|PDB:5SZJ"
FT MOD_RES 73
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255,
FT ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:29562525,
FT ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
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:0000269|PubMed:31540829"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:31540829"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:31540829"
FT MUTAGEN 23
FT /note="T->N: Probable dominant negative mutant locked in
FT the inactive GDP-bound form; alters the basolateral
FT recycling pathway in epithelial cells and endoplasmic
FT reticulum membrane morphology. Reduces endoplasmic
FT reticulum recruitment to the Legionella-containing
FT vacuole."
FT /evidence="ECO:0000269|PubMed:20576682,
FT ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:31540829"
FT MUTAGEN 68
FT /note="Q->L: Probable constitutively active mutant unable
FT to hydrolyze GTP; accumulates at the base of the primary
FT cilium and alters the basolateral recycling pathway in
FT epithelial cells. No effect on endoplasmic reticulum
FT recruitment to the Legionella-containing vacuole."
FT /evidence="ECO:0000269|PubMed:20576682,
FT ECO:0000269|PubMed:31540829"
FT MUTAGEN 73
FT /note="T->A: Loss of phosphorylation. No effect on GDI1 and
FT GDI2 binding. Increases localization to the cytosol."
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148"
FT MUTAGEN 73
FT /note="T->E: Phosphomimetic mutant. Loss of GDI1 and GDI2
FT binding. Increases localization to the Golgi complex."
FT /evidence="ECO:0000269|PubMed:26824392,
FT ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:30398148"
FT CONFLICT 138
FT /note="E -> G (in Ref. 4; CAB66585)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5LPN"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5SZJ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5SZJ"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:5SZJ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5SZJ"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:5SZJ"
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
