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P09527 (RAB7A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-7a
Alternative name(s):
Ras-related protein BRL-RAS
Ras-related protein p23
Gene names
Name:Rab7a
Synonyms:Rab7
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Ref.6 Ref.7

Subunit structure

Interacts with RILP, PSMA7, RNF115 and FYCO1. Interacts with the PIK3C3/VPS34-PIK3R4 complex. The GTP-bound form interacts with OSBPL1A and RAC1 By similarity. Interacts with NTRK1/TRKA. The GTP-bound form interacts with RAC1. Interacts with CLN3 By similarity. Interacts with C9orf72 By similarity. Interacts with CHM, the substrate-binding subunit of the Rab geranylgeranyltransferase complex. Ref.6 Ref.7 Ref.8

Subcellular location

Late endosome. Lysosome. Cytoplasmic vesiclephagosome By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Melanosome By similarity. Note: Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or Mycobacterium By similarity. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Ref.6

Tissue specificity

Expressed in osteoclasts and in neurons. Ref.6 Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasmic vesicle
Endosome
Lysosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from mutant phenotype PubMed 11514537. Source: RGD

early endosome to late endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

endosome to lysosome transport

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor catabolic process

Inferred from electronic annotation. Source: Ensembl

phagosome acidification

Inferred from sequence or structural similarity. Source: UniProtKB

phagosome-lysosome fusion

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to lysosome

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

alveolar lamellar body

Inferred from direct assay PubMed 7868367. Source: RGD

cytoplasmic vesicle

Inferred from direct assay Ref.6. Source: RGD

late endosome

Inferred from direct assay PubMed 19337031. Source: RGD

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay Ref.6. Source: RGD

GTP binding

Inferred from direct assay Ref.6. Source: RGD

GTPase activity

Traceable author statement PubMed 11514537. Source: RGD

Rac GTPase binding

Inferred from physical interaction Ref.6. Source: RGD

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ChmP377272EBI-916225,EBI-1039231

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Ras-related protein Rab-7a
PRO_0000121124

Regions

Nucleotide binding15 – 228GTP
Nucleotide binding34 – 407GTP
Nucleotide binding63 – 675GTP
Nucleotide binding125 – 1284GTP
Nucleotide binding156 – 1572GTP
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue721Phosphoserine By similarity
Modified residue2071Cysteine methyl ester By similarity
Lipidation2051S-geranylgeranyl cysteine By similarity
Lipidation2071S-geranylgeranyl cysteine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P09527 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: A2AF33B02F672971

FASTA20723,504
        10         20         30         40         50         60 
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ 

        70         80         90        100        110        120 
IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF 

       130        140        150        160        170        180 
VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV 

       190        200 
ELYNEFPEPI KLDKNERAKA SAESCSC 

« Hide

References

« Hide 'large scale' references
[1]"A new member of the ras gene superfamily identified in a rat liver cell line."
Bucci C., Franzio R., Chiariotti L., Brown A.L., Rechler M.M., Bruni C.B.
Nucleic Acids Res. 16:9979-9994(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Buffalo.
Tissue: Liver.
[2]Bruni C.B.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]Zhao H., Gao L., Vaananen K.H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Bone.
[4]"Fine mapping of radiation susceptibility and gene expression analysis of LEC congenic rat lines."
Tsuji A.B., Sugyo A., Ogiu T., Sagara M., Kimura T., Ishikawa A., Sudo H., Ohtsuki M., Aburatani H., Imai T., Harada Y.N.
Genomics 86:271-279(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344/DuCrj and LEC/Crj.
[5]"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].
Tissue: Lung.
[6]"Possible role of direct Rac1-Rab7 interaction in ruffled border formation of osteoclasts."
Sun Y., Bueki K.G., Ettala O., Vaeaeraeniemi J.P., Vaeaenaenen H.K.
J. Biol. Chem. 280:32356-32361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAC1.
[7]"The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor TrkA."
Saxena S., Bucci C., Weis J., Kruttgen A.
J. Neurosci. 25:10930-10940(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NTRK1/TRKA, TISSUE SPECIFICITY.
[8]"Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation."
Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.
EMBO J. 27:2444-2456(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH CHM.
[9]"Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease."
Rak A., Pylypenko O., Niculae A., Pyatkov K., Goody R.S., Alexandrov K.
Cell 117:749-760(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-185 IN COMPLEX WITH GTP ANALOG AND CHM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12535 mRNA. Translation: CAA31053.1.
AF286535 mRNA. Translation: AAG00543.1.
AB158427 mRNA. Translation: BAE16999.1.
AB158428 mRNA. Translation: BAE17000.1.
BC072470 mRNA. Translation: AAH72470.1.
PIRS01934.
RefSeqNP_076440.1. NM_023950.3.
XP_006236911.1. XM_006236849.1.
UniGeneRn.1425.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VG0X-ray2.20B1-207[»]
1VG1X-ray1.90A1-185[»]
1VG8X-ray1.70A/B/C/D1-207[»]
1VG9X-ray2.50B/D/F/H1-185[»]
ProteinModelPortalP09527.
SMRP09527. Positions 7-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248093. 1 interaction.
IntActP09527. 4 interactions.
MINTMINT-1775656.
STRING10116.ENSRNOP00000016432.

PTM databases

PhosphoSiteP09527.

Proteomic databases

PaxDbP09527.
PRIDEP09527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016432; ENSRNOP00000016432; ENSRNOG00000012247.
GeneID29448.
KEGGrno:29448.
UCSCRGD:61908. rat.

Organism-specific databases

CTD7879.
RGD61908. Rab7a.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00700000104345.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP09527.
KOK07897.
OMADYPDPIK.
OrthoDBEOG7G4QG8.
PhylomeDBP09527.
TreeFamTF105605.

Gene expression databases

GenevestigatorP09527.

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

EvolutionaryTraceP09527.
NextBio609213.
PROP09527.

Entry information

Entry nameRAB7A_RAT
AccessionPrimary (citable) accession number: P09527
Secondary accession number(s): Q4AEF6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 131 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