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Protein

Ras-related protein Rab-13

Gene

Rab13

Organism
Rattus norvegicus (Rat)
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis.3 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). That Rab may be activated by DENND1C, a guanine exchange factor (By similarity). Activated in response to insulin.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: GO_Central
  2. GTPase activity Source: GO_Central
  3. GTP binding Source: UniProtKB
  4. protein kinase A catalytic subunit binding Source: UniProtKB

GO - Biological processi

  1. cellular response to insulin stimulus Source: UniProtKB
  2. cortical actin cytoskeleton organization Source: UniProtKB
  3. endocytic recycling Source: UniProtKB
  4. endosomal transport Source: UniProtKB
  5. endothelial cell chemotaxis Source: UniProtKB
  6. establishment of protein localization to plasma membrane Source: UniProtKB
  7. establishment of Sertoli cell barrier Source: UniProtKB
  8. glucose homeostasis Source: UniProtKB
  9. intracellular protein transport Source: GO_Central
  10. metabolic process Source: GOC
  11. neuron projection development Source: UniProtKB
  12. positive regulation of glucose import Source: UniProtKB
  13. protein kinase A signaling Source: UniProtKB
  14. protein localization to cell leading edge Source: UniProtKB
  15. protein localization to plasma membrane Source: UniProtKB
  16. Rab protein signal transduction Source: GO_Central
  17. tight junction assembly Source: UniProtKB
  18. trans-Golgi network to recycling endosome transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_347820. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-13
Gene namesi
Name:Rab13
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi620880. Rab13.

Subcellular locationi

Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Golgi apparatustrans-Golgi network membrane By similarity. Recycling endosome membrane By similarity. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclesecretory vesicle membrane By similarity
Note: Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells.By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. endocytic vesicle Source: UniProtKB
  3. endosome Source: GO_Central
  4. extracellular vesicular exosome Source: Ensembl
  5. insulin-responsive compartment Source: UniProtKB
  6. lamellipodium Source: UniProtKB
  7. lateral plasma membrane Source: UniProtKB
  8. neuron projection Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. recycling endosome Source: UniProtKB
  11. recycling endosome membrane Source: UniProtKB-SubCell
  12. tight junction Source: UniProtKB
  13. trans-Golgi network Source: UniProtKB
  14. transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Ras-related protein Rab-13PRO_0000121184Add
BLAST
Propeptidei201 – 2033Removed in mature formSequence AnalysisPRO_0000370759

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei200 – 2001Cysteine methyl esterSequence Analysis
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP35286.
PRIDEiP35286.

PTM databases

PhosphoSiteiP35286.

Expressioni

Tissue specificityi

Highest levels found in lung, kidney, whole brain and spinal cord. Expressed in all tissues tested including Sertoli and germ cells (at protein level). Also detected in osteoclasts.2 Publications

Gene expression databases

GenevestigatoriP35286.

Interactioni

Subunit structurei

Interacts (GTP-bound form) with MICALL2; competes with RAB8A and is involved in tight junctions assembly. Interacts (GTP-bound form) with MICALL1. Interacts with PRKACA; downstream effector of RAB13 involved in tight junction assembly. Interacts with GRB2; may recruit RAB13 to the leading edge of migrating endothelial cells where it can activate RHOA. Interacts (isoprenylated form) with PDE6D; dissociates RAB13 from membranes. Interacts with CCDC64B/BICDR2. Interacts with LEPROT and LEPROTL1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Leprotl1Q6PDU43EBI-917332,EBI-8702651

Protein-protein interaction databases

IntActiP35286. 4 interactions.
MINTiMINT-2982767.
STRINGi10116.ENSRNOP00000022626.

Structurei

3D structure databases

ProteinModelPortaliP35286.
SMRiP35286. Positions 8-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP35286.
KOiK06109.
OMAiKVQREQA.
OrthoDBiEOG7VB2H4.
PhylomeDBiP35286.
TreeFamiTF314097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35286-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNSTYIST IGIDFKIRTV
60 70 80 90 100
EIEGKRIKLQ VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ
110 120 130 140 150
NWMKSIKENA SAGVERLLLG NKCDMEAKRK VQREQAERLA REHRIRFFET
160 170 180 190 200
SAKSSVNVDE AFSSLARDIL LKTGGRRSGN SSKPSSTDLK VSDKKNSNKC

SLG
Length:203
Mass (Da):22,901
Last modified:April 25, 2004 - v2
Checksum:iB6687462C6EA95A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761A → S in AAA41993 (PubMed:1313420).Curated
Sequence conflicti113 – 1131G → E in AAA41993 (PubMed:1313420).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525280 mRNA. Translation: AAM82588.1.
M83678 mRNA. Translation: AAA41993.1.
PIRiD42148.
RefSeqiNP_112354.1. NM_031092.1.
UniGeneiRn.9819.

Genome annotation databases

EnsembliENSRNOT00000022627; ENSRNOP00000022626; ENSRNOG00000016733.
GeneIDi81756.
KEGGirno:81756.
UCSCiRGD:620880. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525280 mRNA. Translation: AAM82588.1.
M83678 mRNA. Translation: AAA41993.1.
PIRiD42148.
RefSeqiNP_112354.1. NM_031092.1.
UniGeneiRn.9819.

3D structure databases

ProteinModelPortaliP35286.
SMRiP35286. Positions 8-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP35286. 4 interactions.
MINTiMINT-2982767.
STRINGi10116.ENSRNOP00000022626.

PTM databases

PhosphoSiteiP35286.

Proteomic databases

PaxDbiP35286.
PRIDEiP35286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022627; ENSRNOP00000022626; ENSRNOG00000016733.
GeneIDi81756.
KEGGirno:81756.
UCSCiRGD:620880. rat.

Organism-specific databases

CTDi5872.
RGDi620880. Rab13.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP35286.
KOiK06109.
OMAiKVQREQA.
OrthoDBiEOG7VB2H4.
PhylomeDBiP35286.
TreeFamiTF314097.

Enzyme and pathway databases

ReactomeiREACT_347820. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

NextBioi615526.
PROiP35286.

Gene expression databases

GenevestigatoriP35286.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "RAB13 participates in ectoplasmic specialization dynamics in the rat testis."
    Mruk D.D., Lau A.S.
    Biol. Reprod. 80:590-601(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
  2. "Rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain."
    Elferink L.A., Anzai K., Scheller R.H.
    J. Biol. Chem. 267:5768-5775(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-203.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2."
    Sakane A., Honda K., Sasaki T.
    Mol. Cell. Biol. 30:1077-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURITE OUTGROWTH.
  4. "Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation in muscle cells."
    Sun Y., Bilan P.J., Liu Z., Klip A.
    Proc. Natl. Acad. Sci. U.S.A. 107:19909-19914(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EXOCYTOSIS, ENZYME REGULATION.
  5. "Rab13 is upregulated during osteoclast differentiation and associates with small vesicles revealing polarized distribution in resorbing cells."
    Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L., Vaeaenaenen H.K.
    J. Histochem. Cytochem. 60:537-549(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. Cited for: INTERACTION WITH LEPROT AND LEPROTL1.
  7. "RAB13 regulates Sertoli cell permeability barrier dynamics through protein kinase A."
    Su W., Liu X.
    J. Mol. Endocrinol. 50:305-318(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKACA.

Entry informationi

Entry nameiRAB13_RAT
AccessioniPrimary (citable) accession number: P35286
Secondary accession number(s): Q8K3X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: April 25, 2004
Last modified: March 31, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.