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P51150 (RAB7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-7a
Gene names
Name:Rab7a
Synonyms:Rab7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 a role in the fusion of phagosomes with lysosomes. 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 By similarity.

Subunit structure

Interacts with NTRK1/TRKA, 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 CLN3. Interacts with CHM, the substrate-binding subunit of the Rab geranylgeranyltransferase complex By similarity. Interacts with C9orf72. Ref.6 Ref.8

Subcellular location

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

Tissue specificity

Widely expressed. High expression in liver, heart and kidney. Found in sensory and motor neurons. Ref.5

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 termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from electronic annotation. Source: Ensembl

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

intracellular protein transport

Traceable author statement PubMed 11042173. Source: MGI

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 direct assay PubMed 11042173. Source: MGI

alveolar lamellar body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 18656450. Source: MGI

late endosome

Inferred from direct assay PubMed 11172003PubMed 15588329PubMed 19509052PubMed 20943658PubMed 23028046PubMed 24035762. Source: MGI

lysosome

Inferred from sequence orthology PubMed 15078902. Source: MGI

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 electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.6Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Ras-related protein Rab-7a
PRO_0000121122

Regions

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

Amino acid modifications

Modified residue721Phosphoserine Ref.7
Modified residue2071Cysteine methyl ester By similarity
Lipidation2051S-geranylgeranyl cysteine By similarity
Lipidation2071S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict1451S → R in CAA61797. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51150 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: A2AF33B16A672971

FASTA20723,490
        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 KLDKNDRAKA SAESCSC 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression analysis of the murine Rab7 cDNA."
Vitelli R., Chiariello M., Bruni C.B., Bucci C.
Biochim. Biophys. Acta 1264:268-270(1995) [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: Liver.
[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/6 and FVB/N.
Tissue: Brain and Mammary tumor.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-31; 70-79; 114-126 AND 147-157, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy."
Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M., Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A., Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V.
Am. J. Hum. Genet. 72:722-727(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Rabring7, a novel Rab7 target protein with a RING finger motif."
Mizuno K., Kitamura A., Sasaki T.
Mol. Biol. Cell 14:3741-3752(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF115.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking."
Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.
Hum. Mol. Genet. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C9ORF72.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89650 mRNA. Translation: CAA61797.1.
AK005004 mRNA. Translation: BAB23738.1.
BC004597 mRNA. Translation: AAH04597.1.
BC086793 mRNA. Translation: AAH86793.1.
CCDSCCDS39552.1.
PIRS62733.
RefSeqNP_033031.2. NM_009005.2.
XP_006505824.1. XM_006505761.1.
XP_006505825.1. XM_006505762.1.
UniGeneMm.333233.
Mm.471618.
Mm.486309.

3D structure databases

ProteinModelPortalP51150.
SMRP51150. Positions 7-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202553. 3 interactions.
DIPDIP-60513N.
IntActP51150. 1 interaction.
MINTMINT-1864693.
STRING10090.ENSMUSP00000109230.

PTM databases

PhosphoSiteP51150.

Proteomic databases

MaxQBP51150.
PaxDbP51150.
PRIDEP51150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477.
ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477.
ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477.
ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477.
ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
GeneID19349.
KEGGmmu:19349.
UCSCuc009cuv.1. mouse.

Organism-specific databases

CTD19349.
MGIMGI:105068. Rab7.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP51150.
KOK07897.
OMADYPDPIK.
OrthoDBEOG7G4QG8.
PhylomeDBP51150.
TreeFamTF105605.

Gene expression databases

ArrayExpressP51150.
BgeeP51150.
CleanExMM_RAB7.
GenevestigatorP51150.

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

NextBio296377.
PROP51150.
SOURCESearch...

Entry information

Entry nameRAB7A_MOUSE
AccessionPrimary (citable) accession number: P51150
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 129 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

MGD cross-references

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