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P51150

- RAB7A_MOUSE

UniProt

P51150 - RAB7A_MOUSE

Protein

Ras-related protein Rab-7a

Gene

Rab7a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      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 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: Ensembl
    2. GTPase activity Source: Ensembl
    3. GTP binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. bone resorption Source: Ensembl
    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. intracellular protein transport Source: MGI
    6. phagosome acidification Source: UniProtKB
    7. phagosome-lysosome fusion Source: UniProtKB
    8. protein targeting to lysosome Source: Ensembl
    9. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. 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: Chromosome 6

    Organism-specific databases

    MGIiMGI:105068. Rab7.

    Subcellular locationi

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

    GO - Cellular componenti

    1. alveolar lamellar body Source: Ensembl
    2. cytoplasm Source: MGI
    3. Golgi apparatus Source: MGI
    4. late endosome Source: MGI
    5. lysosome Source: MGI
    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_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

    ArrayExpressiP51150.
    BgeeiP51150.
    CleanExiMM_RAB7.
    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

    MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV    50
    MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD 100
    SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP 150
    YFETSAKEAI NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA 200
    SAESCSC 207
    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:
    EMBL
    GenBank
    DDBJ
    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_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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89650 mRNA. Translation: CAA61797.1 .
    AK005004 mRNA. Translation: BAB23738.1 .
    BC004597 mRNA. Translation: AAH04597.1 .
    BC086793 mRNA. Translation: AAH86793.1 .
    CCDSi CCDS39552.1.
    PIRi S62733.
    RefSeqi NP_033031.2. NM_009005.3.
    UniGenei Mm.333233.
    Mm.471618.
    Mm.486309.

    3D structure databases

    ProteinModelPortali P51150.
    SMRi P51150. Positions 7-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202553. 3 interactions.
    DIPi DIP-60513N.
    IntActi P51150. 2 interactions.
    MINTi MINT-1864693.
    STRINGi 10090.ENSMUSP00000109230.

    PTM databases

    PhosphoSitei P51150.

    Proteomic databases

    MaxQBi P51150.
    PaxDbi P51150.
    PRIDEi P51150.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000095048 ; ENSMUSP00000092658 ; ENSMUSG00000079477 .
    ENSMUST00000113596 ; ENSMUSP00000109226 ; ENSMUSG00000079477 .
    ENSMUST00000113597 ; ENSMUSP00000109227 ; ENSMUSG00000079477 .
    ENSMUST00000113598 ; ENSMUSP00000109228 ; ENSMUSG00000079477 .
    ENSMUST00000113600 ; ENSMUSP00000109230 ; ENSMUSG00000079477 .
    GeneIDi 19349.
    KEGGi mmu:19349.
    UCSCi uc009cuv.1. mouse.

    Organism-specific databases

    CTDi 19349.
    MGIi MGI:105068. Rab7.

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P51150.
    KOi K07897.
    OMAi DYPDPIK.
    OrthoDBi EOG7G4QG8.
    PhylomeDBi P51150.
    TreeFami TF105605.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.

    Miscellaneous databases

    NextBioi 296377.
    PROi P51150.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51150.
    Bgeei P51150.
    CleanExi MM_RAB7.
    Genevestigatori P51150.

    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. "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: October 1, 2014
    This is version 131 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