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Protein

Ras-related protein Rab-7a

Gene

Rab7a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi34 – 407GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi125 – 1284GTPBy similarity
Nucleotide bindingi156 – 1572GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: MGI
  2. GTPase activity Source: MGI
  3. GTP binding Source: MGI

GO - Biological processi

  1. bone resorption Source: Ensembl
  2. early endosome to late endosome transport Source: UniProtKB
  3. endosome to lysosome transport Source: MGI
  4. epidermal growth factor catabolic process Source: MGI
  5. intracellular protein transport Source: MGI
  6. phagosome acidification Source: UniProtKB
  7. phagosome-lysosome fusion Source: UniProtKB
  8. positive regulation of exosomal secretion Source: MGI
  9. protein targeting to lysosome Source: MGI
  10. protein to membrane docking Source: MGI
  11. Rab protein signal transduction Source: GO_Central
  12. regulation of autophagic vacuole assembly Source: MGI
  13. retrograde transport, endosome to Golgi Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_316383. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-7a
Gene namesi
Name:Rab7a
Synonyms:Rab7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:105068. Rab7.

Subcellular locationi

  1. Late endosome By similarity
  2. Lysosome By similarity
  3. Cytoplasmic vesiclephagosome By similarity
  4. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  5. Melanosome By similarity

  6. 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).By similarity

GO - Cellular componenti

  1. alveolar lamellar body Source: Ensembl
  2. cytoplasm Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. Golgi apparatus Source: MGI
  5. intracellular membrane-bounded organelle Source: MGI
  6. late endosome Source: MGI
  7. lysosome Source: MGI
  8. melanosome Source: UniProtKB-SubCell
  9. phagocytic vesicle Source: UniProtKB
  10. phagocytic vesicle membrane Source: UniProtKB-SubCell
  11. pre-autophagosomal structure membrane Source: UniProtKB
  12. vacuolar membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Ras-related protein Rab-7aPRO_0000121122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Phosphoserine1 Publication
Lipidationi205 – 2051S-geranylgeranyl cysteineBy similarity
Modified residuei207 – 2071Cysteine methyl esterBy similarity
Lipidationi207 – 2071S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP51150.
PaxDbiP51150.
PRIDEiP51150.

PTM databases

PhosphoSiteiP51150.

Expressioni

Tissue specificityi

Widely expressed. High expression in liver, heart and kidney. Found in sensory and motor neurons.1 Publication

Gene expression databases

BgeeiP51150.
CleanExiMM_RAB7.
ExpressionAtlasiP51150. baseline and differential.
GenevestigatoriP51150.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi202553. 3 interactions.
DIPiDIP-60513N.
IntActiP51150. 2 interactions.
MINTiMINT-1864693.
STRINGi10090.ENSMUSP00000109230.

Structurei

3D structure databases

ProteinModelPortaliP51150.
SMRiP51150. Positions 7-190.
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.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP51150.
KOiK07897.
OMAiDYPDPIK.
OrthoDBiEOG7G4QG8.
PhylomeDBiP51150.
TreeFamiTF105605.

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.

P51150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV
60 70 80 90 100
MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD
110 120 130 140 150
SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP
160 170 180 190 200
YFETSAKEAI NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA

SAESCSC
Length:207
Mass (Da):23,490
Last modified:April 13, 2004 - v2
Checksum:iA2AF33B16A672971
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451S → R in CAA61797 (PubMed:8547311).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89650 mRNA. Translation: CAA61797.1.
AK005004 mRNA. Translation: BAB23738.1.
BC004597 mRNA. Translation: AAH04597.1.
BC086793 mRNA. Translation: AAH86793.1.
CCDSiCCDS39552.1.
PIRiS62733.
RefSeqiNP_001280581.1. NM_001293652.1.
NP_001280582.1. NM_001293653.1.
NP_001280583.1. NM_001293654.1.
NP_001280584.1. NM_001293655.1.
NP_033031.2. NM_009005.3.
UniGeneiMm.333233.
Mm.471618.
Mm.486309.

Genome annotation databases

EnsembliENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477.
ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477.
ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477.
ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477.
ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
GeneIDi19349.
KEGGimmu:19349.
UCSCiuc009cuv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89650 mRNA. Translation: CAA61797.1.
AK005004 mRNA. Translation: BAB23738.1.
BC004597 mRNA. Translation: AAH04597.1.
BC086793 mRNA. Translation: AAH86793.1.
CCDSiCCDS39552.1.
PIRiS62733.
RefSeqiNP_001280581.1. NM_001293652.1.
NP_001280582.1. NM_001293653.1.
NP_001280583.1. NM_001293654.1.
NP_001280584.1. NM_001293655.1.
NP_033031.2. NM_009005.3.
UniGeneiMm.333233.
Mm.471618.
Mm.486309.

3D structure databases

ProteinModelPortaliP51150.
SMRiP51150. Positions 7-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202553. 3 interactions.
DIPiDIP-60513N.
IntActiP51150. 2 interactions.
MINTiMINT-1864693.
STRINGi10090.ENSMUSP00000109230.

PTM databases

PhosphoSiteiP51150.

Proteomic databases

MaxQBiP51150.
PaxDbiP51150.
PRIDEiP51150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477.
ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477.
ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477.
ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477.
ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
GeneIDi19349.
KEGGimmu:19349.
UCSCiuc009cuv.1. mouse.

Organism-specific databases

CTDi19349.
MGIiMGI:105068. Rab7.

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP51150.
KOiK07897.
OMAiDYPDPIK.
OrthoDBiEOG7G4QG8.
PhylomeDBiP51150.
TreeFamiTF105605.

Enzyme and pathway databases

ReactomeiREACT_316383. MHC class II antigen presentation.

Miscellaneous databases

NextBioi296377.
PROiP51150.
SOURCEiSearch...

Gene expression databases

BgeeiP51150.
CleanExiMM_RAB7.
ExpressionAtlasiP51150. baseline and differential.
GenevestigatoriP51150.

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

« Hide 'large scale' publications
  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.
    , 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. 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. 23:3579-3595(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C9ORF72.

Entry informationi

Entry nameiRAB7A_MOUSE
AccessioniPrimary (citable) accession number: P51150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 13, 2004
Last modified: April 1, 2015
This is version 136 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.