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Protein

Ras-related protein Rab-10

Gene

Rab10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. Finally, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion.By similarity3 Publications

Enzyme regulationi

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP) (By similarity). That Rab is activated by the DENND4C guanine exchange factor (GEF).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 238GTPBy similarity
Nucleotide bindingi64 – 685GTPBy similarity
Nucleotide bindingi122 – 1254GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-10
Gene namesi
Name:Rab10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:105066. Rab10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681Q → L: Probable constitutively active mutant unable to hydrolyze GTP; stimulates translocation of SLC2A4 to the plasma membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Ras-related protein Rab-10PRO_0000121147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysineBy similarity
Lipidationi199 – 1991S-geranylgeranyl cysteineBy similarity
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

EPDiP61027.
PaxDbiP61027.
PRIDEiP61027.

PTM databases

iPTMnetiP61027.
PhosphoSiteiP61027.
SwissPalmiP61027.

Expressioni

Inductioni

Up-regulated by LPS.1 Publication

Gene expression databases

BgeeiP61027.
CleanExiMM_RAB10.
ExpressionAtlasiP61027. baseline and differential.
GenevisibleiP61027. MM.

Interactioni

Subunit structurei

Interacts with MYO5A; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles. Interacts with GDI1 and maybe with GDI2; negatively regulates RAB10 association with membranes and activation. Interacts (GDP-bound form) with LLGL1; the interaction is direct and promotes RAB10 association with membranes and activation through competition with the Rab inhibitor GDI1 (By similarity). Interacts with EXOC4; probably associates with the exocyst (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GDI1P311503EBI-911581,EBI-946999From a different organism.
GDI2P503953EBI-911581,EBI-1049143From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202531. 3 interactions.
DIPiDIP-37720N.
IntActiP61027. 21 interactions.
MINTiMINT-1862700.
STRINGi10090.ENSMUSP00000021001.

Structurei

3D structure databases

ProteinModelPortaliP61027.
SMRiP61027. Positions 9-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 469Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61027.
KOiK07903.
OMAiREHSIRF.
OrthoDBiEOG7VB2H4.
PhylomeDBiP61027.
TreeFamiTF314097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT
60 70 80 90 100
VELQGKKIKL QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI
110 120 130 140 150
SKWLRNIDEH ANEDVERMLL GNKCDMDDKR VVPKGKGEQI AREHGIRFFE
160 170 180 190 200
TSAKANINIE KAFLTLAEDI LRKTPVKEPN SENVDISSGG GVTGWKSKCC
Length:200
Mass (Da):22,541
Last modified:April 26, 2004 - v1
Checksum:i7F02B8E8E46EE1E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061N → H in BAB25858 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035646 mRNA. Translation: AAC29313.1.
AK008725 mRNA. Translation: BAB25858.1.
AK028320 mRNA. Translation: BAC25878.1.
AK087964 mRNA. Translation: BAC40062.1.
BC056374 mRNA. Translation: AAH56374.1.
CCDSiCCDS25782.1.
RefSeqiNP_057885.1. NM_016676.5.
UniGeneiMm.378993.
Mm.486858.

Genome annotation databases

EnsembliENSMUST00000021001; ENSMUSP00000021001; ENSMUSG00000020671.
GeneIDi19325.
KEGGimmu:19325.
UCSCiuc007mwl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035646 mRNA. Translation: AAC29313.1.
AK008725 mRNA. Translation: BAB25858.1.
AK028320 mRNA. Translation: BAC25878.1.
AK087964 mRNA. Translation: BAC40062.1.
BC056374 mRNA. Translation: AAH56374.1.
CCDSiCCDS25782.1.
RefSeqiNP_057885.1. NM_016676.5.
UniGeneiMm.378993.
Mm.486858.

3D structure databases

ProteinModelPortaliP61027.
SMRiP61027. Positions 9-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202531. 3 interactions.
DIPiDIP-37720N.
IntActiP61027. 21 interactions.
MINTiMINT-1862700.
STRINGi10090.ENSMUSP00000021001.

PTM databases

iPTMnetiP61027.
PhosphoSiteiP61027.
SwissPalmiP61027.

Proteomic databases

EPDiP61027.
PaxDbiP61027.
PRIDEiP61027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021001; ENSMUSP00000021001; ENSMUSG00000020671.
GeneIDi19325.
KEGGimmu:19325.
UCSCiuc007mwl.2. mouse.

Organism-specific databases

CTDi10890.
MGIiMGI:105066. Rab10.

Phylogenomic databases

eggNOGiKOG0078. Eukaryota.
ENOG410XPUI. LUCA.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP61027.
KOiK07903.
OMAiREHSIRF.
OrthoDBiEOG7VB2H4.
PhylomeDBiP61027.
TreeFamiTF314097.

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSiRab10. mouse.
PROiP61027.
SOURCEiSearch...

Gene expression databases

BgeeiP61027.
CleanExiMM_RAB10.
ExpressionAtlasiP61027. baseline and differential.
GenevisibleiP61027. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zeng Q., Tan Y.H., Hong W.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Brain, Stomach and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 12-22; 60-70; 96-102; 106-117 AND 148-172, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane."
    Sano H., Eguez L., Teruel M.N., Fukuda M., Chuang T.D., Chavez J.A., Lienhard G.E., McGraw T.E.
    Cell Metab. 5:293-303(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLUT4 TRANSPORT, MUTAGENESIS OF GLN-68.
  6. "GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4 translocation."
    Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.
    Biochem. J. 422:229-235(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GDI1 AND GDI2.
  7. "Rab10 associates with primary cilia and the exocyst complex in renal epithelial cells."
    Babbey C.M., Bacallao R.L., Dunn K.W.
    Am. J. Physiol. 299:F495-506(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane."
    Wang D., Lou J., Ouyang C., Chen W., Liu Y., Liu X., Cao X., Wang J., Lu L.
    Proc. Natl. Acad. Sci. U.S.A. 107:13806-13811(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSPORT TO THE PLASMA MEMBRANE, INDUCTION BY LPS.
  10. "Insulin-stimulated GLUT4 protein translocation in adipocytes requires the Rab10 guanine nucleotide exchange factor Dennd4C."
    Sano H., Peck G.R., Kettenbach A.N., Gerber S.A., Lienhard G.E.
    J. Biol. Chem. 286:16541-16545(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  11. "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYO5A.

Entry informationi

Entry nameiRAB10_MOUSE
AccessioniPrimary (citable) accession number: P61027
Secondary accession number(s): O88386, Q9D7X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.