P09527 (RAB7A_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ras-related protein Rab-7a Alternative name(s): Ras-related protein BRL-RAS Ras-related protein p23 | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. Ref.6 Ref.7 |
| Subcellular location | Late endosome. Lysosome. Cytoplasmic vesicle › phagosome By similarity. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Melanosome By similarity. Note: Co-localizes 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 | |
| Sequence similarities | Belongs to the small GTPase superfamily. Rab family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Chm | P37727 | 2 | EBI-916225,EBI-1039231 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 207 | 207 | Ras-related protein Rab-7a | PRO_0000121124 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 15 – 22 | 8 | GTP By similarity | ||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 63 – 67 | 5 | GTP By similarity | ||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 125 – 128 | 4 | GTP By similarity | ||||||||||||||||||||||||||||||||||||||
| Motif | 37 – 45 | 9 | Effector region By similarity | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Modified residue | 72 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||||||||
| Modified residue | 207 | 1 | Cysteine methyl ester By similarity | ||||||||||||||||||||||||||||||||||||||
| Lipidation | 205 | 1 | S-geranylgeranyl cysteine By similarity | ||||||||||||||||||||||||||||||||||||||
| Lipidation | 207 | 1 | S-geranylgeranyl cysteine By similarity | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 8 – 14 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 21 – 30 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 42 – 54 | 13 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 56 – 64 | 9 | |||||||||||||||||||||||||||||||||||||||
| Helix | 68 – 70 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 76 – 78 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 82 – 89 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 97 | 5 | |||||||||||||||||||||||||||||||||||||||
| Helix | 99 – 110 | 12 | |||||||||||||||||||||||||||||||||||||||
| Helix | 115 – 117 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 125 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 129 – 131 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 136 – 145 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 153 | 3 | |||||||||||||||||||||||||||||||||||||||
| Turn | 156 – 159 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 162 – 185 | 24 | |||||||||||||||||||||||||||||||||||||||
Sequences
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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. |
| + | 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. | ||||||||||||||||||||||||||||||
| IPI | IPI00215564. | ||||||||||||||||||||||||||||||
| PIR | S01934. | ||||||||||||||||||||||||||||||
| RefSeq | NP_076440.1. NM_023950.3. | ||||||||||||||||||||||||||||||
| UniGene | Rn.1425. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P09527. | ||||||||||||||||||||||||||||||
| SMR | P09527. Positions 7-190. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| IntAct | P09527. 2 interactions. | ||||||||||||||||||||||||||||||
| MINT | MINT-1775656. | ||||||||||||||||||||||||||||||
| STRING | 10116.ENSRNOP00000016432. | ||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||
| PhosphoSite | P09527. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PaxDb | P09527. | ||||||||||||||||||||||||||||||
| PRIDE | P09527. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENSRNOT00000016432; ENSRNOP00000016432; ENSRNOG00000012247. | ||||||||||||||||||||||||||||||
| GeneID | 29448. | ||||||||||||||||||||||||||||||
| KEGG | rno:29448. | ||||||||||||||||||||||||||||||
| UCSC | RGD:61908. rat. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 7879. | ||||||||||||||||||||||||||||||
| RGD | 61908. Rab7a. | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | COG1100. | ||||||||||||||||||||||||||||||
| GeneTree | ENSGT00700000104345. | ||||||||||||||||||||||||||||||
| HOGENOM | HOG000233968. | ||||||||||||||||||||||||||||||
| HOVERGEN | HBG009351. | ||||||||||||||||||||||||||||||
| InParanoid | P09527. | ||||||||||||||||||||||||||||||
| KO | K07897. | ||||||||||||||||||||||||||||||
| OMA | SPRDPEH. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG4QFWF4. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| Genevestigator | P09527. | ||||||||||||||||||||||||||||||
| GermOnline | ENSRNOG00000012247. Rattus norvegicus. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF00071. Ras. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PRINTS | PR00449. RASTRNSFRMNG. | ||||||||||||||||||||||||||||||
| SMART | SM00175. RAB. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR00231. small_GTP. 1 hit. | ||||||||||||||||||||||||||||||
| PROSITE | PS51419. RAB. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||
| EvolutionaryTrace | P09527. | ||||||||||||||||||||||||||||||
| NextBio | 609213. | ||||||||||||||||||||||||||||||
Entry information
| Entry name | RAB7A_RAT | ||||||||
| Accession | Primary (citable) accession number: P09527 Secondary accession number(s): Q4AEF6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
