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P55258 (RAB8A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-8A
Alternative name(s):
Oncogene c-mel
Gene names
Name:Rab8a
Synonyms:Mel, Rab8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis. Ref.9

Enzyme regulation

Activated in response to insulin By similarity.

Subunit structure

Interacts (GTP-bound form) with MICALL1; regulates RAB8A association with recycling endosomes. Interacts with MICALL2; competes with RAB13 and is involved in E-cadherin endocytic recycling. Interacts with MICAL1. Interacts with EHD1. Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and SGSM3. Interacts with RABIF, RIMS2, RPH3A and RPH3A. Interacts with OPTN. Interacts with RAB3IP. Interacts with MYO5B. Interacts with PIFO. Interacts with BIRC6/bruce. Interacts with OCRL. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus By similarity. Recycling endosome membrane. Cell projectioncilium By similarity. Cytoplasmic vesiclephagosome By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or Mycobacterium By similarity. Ref.9

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasmic vesicle
Endosome
Golgi apparatus
Membrane
   DiseaseProto-oncogene
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi vesicle fusion to target membrane

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of protein transport

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle docking involved in exocytosis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

ciliary basal body

Inferred from direct assay PubMed 19625297. Source: MGI

dendrite

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nonmotile primary cilium

Inferred from direct assay PubMed 19625297PubMed 20592197. Source: MGI

phagocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

recycling endosome

Inferred from direct assay Ref.9. Source: UniProtKB

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activity

Inferred from electronic annotation. Source: Ensembl

Rab GTPase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11773082Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rph3aP477082EBI-398411,EBI-398376

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Ras-related protein Rab-8A
PRO_0000121132
Propeptide205 – 2073Removed in mature form Potential
PRO_0000370795

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding121 – 1244GTP By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue1811Phosphoserine By similarity
Modified residue1851Phosphoserine By similarity
Modified residue2041Cysteine methyl ester Potential
Lipidation2041S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict176 – 1838KLEGNSPQ → NWKATAA in AAB19682. Ref.1

Secondary structure

....................... 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55258 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: AC89DC85588FB8F8

FASTA20723,668
        10         20         30         40         50         60 
MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ 

        70         80         90        100        110        120 
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG 

       130        140        150        160        170        180 
NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN 

       190        200 
SPQGSSHGVK ITVEQQKRTS FFRCSLL 

« Hide

References

« Hide 'large scale' references
[1]"The MEL gene: a new member of the RAB/YPT class of RAS-related genes."
Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R., Johnson K.J.
Oncogene 6:1347-1351(1991) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
Tissue: Cerebellum and Retina.
[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: FVB/N.
Tissue: Liver.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-21; 59-69 AND 139-153, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase."
Ren M., Zeng J., De Lemos-Chiarandini C., Rosenfeld M., Adesnik M., Sabatini D.D.
Proc. Natl. Acad. Sci. U.S.A. 93:5151-5155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP4K2.
Strain: BALB/c.
Tissue: Melanoma.
[6]"Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2."
Fukuda M.
J. Biol. Chem. 278:15373-15380(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIMS2; RPH3A AND RPH3AL.
[7]"Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells."
Fukuda M.
J. Biol. Chem. 278:15390-15396(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYTL4.
[8]"Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway."
Yang H., Sasaki T., Minoshima S., Shimizu N.
Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGSM1 AND SGSM3.
[9]"The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions."
Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.
Mol. Biol. Cell 19:971-983(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTIC RECYCLING, SUBCELLULAR LOCATION, INTERACTION WITH MICAL1; MICALL1 AND MICALL2.
[10]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[12]"Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4."
Itzen A., Pylypenko O., Goody R.S., Alexandrov K., Rak A.
EMBO J. 25:1445-1455(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-175 IN COMPLEX WITH RABIF, INTERACTION WITH RABIF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S53270 mRNA. Translation: AAB19682.1.
AK076048 mRNA. Translation: BAC36146.1.
AK079306 mRNA. Translation: BAC37603.1.
AK080740 mRNA. Translation: BAC38003.1.
BC019990 mRNA. Translation: AAH19990.1.
CCDSCCDS22409.1.
RefSeqNP_075615.2. NM_023126.2.
UniGeneMm.162811.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FU5X-ray2.00C/D1-175[»]
ProteinModelPortalP55258.
SMRP55258. Positions 6-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201387. 5 interactions.
IntActP55258. 11 interactions.
MINTMINT-1862635.

PTM databases

PhosphoSiteP55258.

Proteomic databases

MaxQBP55258.
PaxDbP55258.
PRIDEP55258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003121; ENSMUSP00000003121; ENSMUSG00000003037.
GeneID17274.
KEGGmmu:17274.
UCSCuc009mfj.1. mouse.

Organism-specific databases

CTD4218.
MGIMGI:96960. Rab8a.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
KOK07901.
OMAIDKAFYS.
OrthoDBEOG7VB2H4.
TreeFamTF314097.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

ArrayExpressP55258.
BgeeP55258.
CleanExMM_RAB8A.
GenevestigatorP55258.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP55258.
NextBio291770.
PROP55258.
SOURCESearch...

Entry information

Entry nameRAB8A_MOUSE
AccessionPrimary (citable) accession number: P55258
Secondary accession number(s): Q8VCF6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot