Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras-related protein Rab-7a

Gene

Rab7a

Organism
Rattus norvegicus (Rat)
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 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.2 Publications

Regions

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

GO - Molecular functioni

  1. GDP binding Source: RGD
  2. GTPase activity Source: RGD
  3. GTP binding Source: RGD
  4. Rac GTPase binding Source: RGD

GO - Biological processi

  1. bone resorption Source: RGD
  2. early endosome to late endosome transport Source: UniProtKB
  3. endosome to lysosome transport Source: GO_Central
  4. epidermal growth factor catabolic process Source: Ensembl
  5. intracellular protein transport Source: GO_Central
  6. phagosome acidification Source: UniProtKB
  7. phagosome-lysosome fusion Source: UniProtKB
  8. protein targeting to lysosome Source: Ensembl
  9. Rab protein signal transduction Source: GO_Central
  10. regulation of autophagic vacuole assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_296088. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-7a
Alternative name(s):
Ras-related protein BRL-RAS
Ras-related protein p23
Gene namesi
Name:Rab7a
Synonyms:Rab7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi61908. Rab7a.

Subcellular locationi

Late endosome 1 Publication. Lysosome 1 Publication. Cytoplasmic vesiclephagosome By similarity. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; 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.By similarity

GO - Cellular componenti

  1. alveolar lamellar body Source: RGD
  2. cytoplasmic vesicle Source: RGD
  3. extracellular vesicular exosome Source: Ensembl
  4. Golgi apparatus Source: Ensembl
  5. late endosome Source: RGD
  6. lysosome Source: GO_Central
  7. melanosome Source: UniProtKB-SubCell
  8. phagocytic vesicle Source: UniProtKB
  9. phagocytic vesicle membrane Source: UniProtKB-SubCell
  10. pre-autophagosomal structure membrane Source: Ensembl
  11. terminal bouton Source: ParkinsonsUK-UCL
  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_0000121124Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP09527.
PRIDEiP09527.

PTM databases

PhosphoSiteiP09527.

Expressioni

Tissue specificityi

Expressed in osteoclasts and in neurons.2 Publications

Gene expression databases

GenevestigatoriP09527.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ChmP377272EBI-916225,EBI-1039231

Protein-protein interaction databases

BioGridi248093. 1 interaction.
IntActiP09527. 5 interactions.
MINTiMINT-1775656.
STRINGi10116.ENSRNOP00000016432.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Helixi21 – 3010Combined sources
Beta strandi42 – 5413Combined sources
Beta strandi56 – 649Combined sources
Helixi68 – 703Combined sources
Helixi76 – 783Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 975Combined sources
Helixi99 – 11012Combined sources
Helixi115 – 1173Combined sources
Beta strandi120 – 1256Combined sources
Beta strandi129 – 1313Combined sources
Helixi136 – 14510Combined sources
Beta strandi151 – 1533Combined sources
Turni156 – 1594Combined sources
Helixi162 – 18524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09527.
SMRiP09527. Positions 7-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09527.

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.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP09527.
KOiK07897.
OMAiDYPDPIK.
OrthoDBiEOG7G4QG8.
PhylomeDBiP09527.
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.

P09527-1 [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 KLDKNERAKA

SAESCSC
Length:207
Mass (Da):23,504
Last modified:September 30, 1996 - v2
Checksum:iA2AF33B02F672971
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01934.
RefSeqiNP_076440.1. NM_023950.3.
XP_006236911.1. XM_006236849.2.
UniGeneiRn.1425.

Genome annotation databases

EnsembliENSRNOT00000016432; ENSRNOP00000016432; ENSRNOG00000012247.
GeneIDi29448.
KEGGirno:29448.
UCSCiRGD:61908. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01934.
RefSeqiNP_076440.1. NM_023950.3.
XP_006236911.1. XM_006236849.2.
UniGeneiRn.1425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09527.
SMRiP09527. Positions 7-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248093. 1 interaction.
IntActiP09527. 5 interactions.
MINTiMINT-1775656.
STRINGi10116.ENSRNOP00000016432.

PTM databases

PhosphoSiteiP09527.

Proteomic databases

PaxDbiP09527.
PRIDEiP09527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016432; ENSRNOP00000016432; ENSRNOG00000012247.
GeneIDi29448.
KEGGirno:29448.
UCSCiRGD:61908. rat.

Organism-specific databases

CTDi7879.
RGDi61908. Rab7a.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119125.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP09527.
KOiK07897.
OMAiDYPDPIK.
OrthoDBiEOG7G4QG8.
PhylomeDBiP09527.
TreeFamiTF105605.

Enzyme and pathway databases

ReactomeiREACT_296088. MHC class II antigen presentation.

Miscellaneous databases

EvolutionaryTraceiP09527.
NextBioi609213.
PROiP09527.

Gene expression databases

GenevestigatoriP09527.

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. "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(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Buffalo.
    Tissue: Liver.
  2. Bruni C.B.
    Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. Zhao H., Gao L., Vaananen K.H.
    Submitted (JUN-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(2004) [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(2003) [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(2004) [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(2004) [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(2007) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-185 IN COMPLEX WITH GTP ANALOG AND CHM.

Entry informationi

Entry nameiRAB7A_RAT
AccessioniPrimary (citable) accession number: P09527
Secondary accession number(s): Q4AEF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1989
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 139 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.