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P09527

- RAB7A_RAT

UniProt

P09527 - RAB7A_RAT

Protein

Ras-related protein Rab-7a

Gene

Rab7a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. 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: Ensembl
    4. epidermal growth factor catabolic process Source: Ensembl
    5. phagosome acidification Source: UniProtKB
    6. phagosome-lysosome fusion Source: UniProtKB
    7. protein targeting to lysosome Source: Ensembl
    8. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198830. 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: 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. Golgi apparatus Source: Ensembl
    4. late endosome Source: RGD
    5. lysosome Source: UniProtKB-SubCell
    6. melanosome Source: UniProtKB-SubCell
    7. phagocytic vesicle Source: UniProtKB
    8. phagocytic vesicle membrane Source: UniProtKB-SubCell

    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 – 147
    Helixi21 – 3010
    Beta strandi42 – 5413
    Beta strandi56 – 649
    Helixi68 – 703
    Helixi76 – 783
    Beta strandi82 – 898
    Helixi93 – 975
    Helixi99 – 11012
    Helixi115 – 1173
    Beta strandi120 – 1256
    Beta strandi129 – 1313
    Helixi136 – 14510
    Beta strandi151 – 1533
    Turni156 – 1594
    Helixi162 – 18524

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00700000104345.
    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

    MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV    50
    MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD 100
    SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP 150
    YFETSAKEAI NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNERAKA 200
    SAESCSC 207
    Length:207
    Mass (Da):23,504
    Last modified:October 1, 1996 - v2
    Checksum:iA2AF33B02F672971
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006236849.1.
    UniGeneiRn.1425.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S01934.
    RefSeqi NP_076440.1. NM_023950.3.
    XP_006236911.1. XM_006236849.1.
    UniGenei Rn.1425.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VG0 X-ray 2.20 B 1-207 [» ]
    1VG1 X-ray 1.90 A 1-185 [» ]
    1VG8 X-ray 1.70 A/B/C/D 1-207 [» ]
    1VG9 X-ray 2.50 B/D/F/H 1-185 [» ]
    ProteinModelPortali P09527.
    SMRi P09527. Positions 7-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248093. 1 interaction.
    IntActi P09527. 5 interactions.
    MINTi MINT-1775656.
    STRINGi 10116.ENSRNOP00000016432.

    PTM databases

    PhosphoSitei P09527.

    Proteomic databases

    PaxDbi P09527.
    PRIDEi P09527.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000016432 ; ENSRNOP00000016432 ; ENSRNOG00000012247 .
    GeneIDi 29448.
    KEGGi rno:29448.
    UCSCi RGD:61908. rat.

    Organism-specific databases

    CTDi 7879.
    RGDi 61908. Rab7a.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00700000104345.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P09527.
    KOi K07897.
    OMAi DYPDPIK.
    OrthoDBi EOG7G4QG8.
    PhylomeDBi P09527.
    TreeFami TF105605.

    Enzyme and pathway databases

    Reactomei REACT_198830. MHC class II antigen presentation.

    Miscellaneous databases

    EvolutionaryTracei P09527.
    NextBioi 609213.
    PROi P09527.

    Gene expression databases

    Genevestigatori P09527.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiRAB7A_RAT
    AccessioniPrimary (citable) accession number: P09527
    Secondary accession number(s): Q4AEF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 133 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