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Protein

Ras-related protein Rab-10

Gene

RAB10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. According to PubMed:23263280, 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 24GTPCombined sources1 Publication7
Nucleotide bindingi35 – 41GTPCombined sources1 Publication7
Nucleotide bindingi64 – 68GTPCombined sourcesBy similarity1 Publication5
Nucleotide bindingi122 – 125GTPCombined sources1 Publication4
Nucleotide bindingi152 – 154GTPCombined sourcesBy similarity1 Publication3

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GDP binding Source: UniProtKB
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB
  • myosin V binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processProtein transport, Transport
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-6798695 Neutrophil degranulation
R-HSA-8873719 RAB geranylgeranylation
R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-10
Gene namesi
Name:RAB10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000084733.10
HGNCiHGNC:9759 RAB10
MIMi612672 gene
neXtProtiNX_P61026

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23T → N: Probable dominant negative mutant locked in the inactive GDP-bound form; alters the basolateral recycling pathway in epithelial cells and endoplasmic reticulum membrane morphology. 2 Publications1
Mutagenesisi68Q → L: Probable constitutively active mutant unable to hydrolyze GTP; accumulates at the base of the primary cilium and alters the basolateral recycling pathway in epithelial cells. 1 Publication1

Organism-specific databases

DisGeNETi10890
OpenTargetsiENSG00000084733
PharmGKBiPA34100

Polymorphism and mutation databases

BioMutaiRAB10
DMDMi46577638

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001211461 – 200Ras-related protein Rab-10Add BLAST200

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102N6-acetyllysineCombined sources1
Lipidationi199S-geranylgeranyl cysteineBy similarity1
Lipidationi200S-geranylgeranyl cysteineBy similarity1

Keywords - PTMi

Acetylation, Lipoprotein, Prenylation

Proteomic databases

EPDiP61026
MaxQBiP61026
PaxDbiP61026
PeptideAtlasiP61026
PRIDEiP61026
ProteomicsDBi57255
TopDownProteomicsiP61026

PTM databases

iPTMnetiP61026
PhosphoSitePlusiP61026
SwissPalmiP61026

Expressioni

Gene expression databases

BgeeiENSG00000084733
CleanExiHS_RAB10
GenevisibleiP61026 HS

Organism-specific databases

HPAiHPA045611

Interactioni

Subunit structurei

Interacts with MYO5A; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts with GDI1 and maybe with GDI2; negatively regulates RAB10 association with membranes and activation (PubMed:19570034). 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). Interacts (GTP-bound form) with MICALCL, MICAL1, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1 two molecules of RAB10 can bind to one molecule of MICAL1 (PubMed:27552051). Interacts with TBC1D13 (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • myosin V binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116096, 64 interactors
IntActiP61026, 36 interactors
MINTiP61026
STRINGi9606.ENSP00000264710

Structurei

Secondary structure

1200
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi22 – 31Combined sources10
Beta strandi43 – 53Combined sources11
Beta strandi56 – 65Combined sources10
Helixi69 – 71Combined sources3
Helixi72 – 75Combined sources4
Helixi76 – 78Combined sources3
Turni79 – 81Combined sources3
Beta strandi83 – 90Combined sources8
Helixi94 – 98Combined sources5
Helixi100 – 110Combined sources11
Beta strandi116 – 122Combined sources7
Helixi127 – 129Combined sources3
Helixi134 – 143Combined sources10
Beta strandi147 – 150Combined sources4
Turni153 – 156Combined sources4
Beta strandi157 – 159Combined sources3
Helixi160 – 172Combined sources13

3D structure databases

ProteinModelPortaliP61026
SMRiP61026
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi38 – 46Effector regionBy similarity9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0078 Eukaryota
ENOG410XPUI LUCA
GeneTreeiENSGT00890000139330
HOGENOMiHOG000233968
HOVERGENiHBG009351
InParanoidiP61026
KOiK07903
OMAiNKCDWED
OrthoDBiEOG091G0LA6
PhylomeDBiP61026
TreeFamiTF314097

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51419 RAB, 1 hit

Sequencei

Sequence statusi: Complete.

P61026-1 [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)DescriptionActionsGraphical viewLength
Sequence conflicti138E → G in CAB66585 (PubMed:11230166).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086917 mRNA Translation: AAP97147.1
AF297660 mRNA Translation: AAG13413.1
AF106681 mRNA Translation: AAD43034.1
AL136650 mRNA Translation: CAB66585.1
AK023223 mRNA Translation: BAB14474.1
AF498945 mRNA Translation: AAM21093.1
CR457303 mRNA Translation: CAG33584.1
CH471053 Genomic DNA Translation: EAX00710.1
CH471053 Genomic DNA Translation: EAX00711.1
BC000896 mRNA Translation: AAH00896.1
CCDSiCCDS1720.1
RefSeqiNP_057215.3, NM_016131.4
UniGeneiHs.467960

Genome annotation databases

EnsembliENST00000264710; ENSP00000264710; ENSG00000084733
GeneIDi10890
KEGGihsa:10890
UCSCiuc002rgv.4 human

Similar proteinsi

Entry informationi

Entry nameiRAB10_HUMAN
AccessioniPrimary (citable) accession number: P61026
Secondary accession number(s): D6W538
, O88386, Q6IA52, Q9D7X6, Q9H0T3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 18, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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