Ras-related protein Rab-7a

Details

Name
Ras-related protein Rab-7a
Synonyms
  • RAB7
Gene Name
RAB7A
Organism
Humans
Amino acid sequence
>lcl|BSEQ0009406|Ras-related protein Rab-7a
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQ
IWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPF
VVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEV
ELYNEFPEPIKLDKNDRAKASAESCSC
Number of residues
207
Molecular Weight
23489.55
Theoretical pI
Not Available
GO Classification
Functions
GDP binding / GTP binding / GTPase activity
Processes
antigen processing and presentation of exogenous peptide antigen via MHC class II / bone resorption / early endosome to late endosome transport / endocytosis / endosome to lysosome transport / epidermal growth factor catabolic process / lipophagy / phagosome acidification / phagosome maturation / phagosome-lysosome fusion / positive regulation of exosomal secretion / positive regulation of protein catabolic process / positive regulation of viral process / protein targeting to lysosome / protein to membrane docking / protein transport / Rab protein signal transduction / regulation of autophagosome assembly / retrograde transport, endosome to Golgi / viral release from host cell
Components
alveolar lamellar body / autophagosome membrane / extracellular exosome / extrinsic component of lysosome membrane / Golgi apparatus / intracellular membrane-bounded organelle / late endosome / late endosome membrane / lipid particle / lysosomal membrane / lysosome / melanosome membrane / phagocytic vesicle / phagocytic vesicle membrane / pre-autophagosomal structure membrane / terminal bouton / vacuolar membrane
General Function
Gtpase activity
Specific 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 M.tuberculosis. 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 (PubMed:11179213, PubMed:12944476, PubMed:14617358, PubMed:20028791, PubMed:21255211). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic vesicle
Gene sequence
>lcl|BSEQ0017451|Ras-related protein Rab-7a (RAB7A)
ATGACCTCTAGGAAGAAAGTGTTGCTGAAGGTTATCATCCTGGGAGATTCTGGAGTCGGG
AAGACATCACTCATGAACCAGTATGTGAATAAGAAATTCAGCAATCAGTACAAAGCCACA
ATAGGAGCTGACTTTCTGACCAAGGAGGTGATGGTGGATGACAGGCTAGTCACAATGCAG
ATATGGGACACAGCAGGACAGGAACGGTTCCAGTCTCTCGGTGTGGCCTTCTACAGAGGT
GCAGACTGCTGCGTTCTGGTATTTGATGTGACTGCCCCCAACACATTCAAAACCCTAGAT
AGCTGGAGAGATGAGTTTCTCATCCAGGCCAGTCCCCGAGATCCTGAAAACTTCCCATTT
GTTGTGTTGGGAAACAAGATTGACCTCGAAAACAGACAAGTGGCCACAAAGCGGGCACAG
GCCTGGTGCTACAGCAAAAACAACATTCCCTACTTTGAGACCAGTGCCAAGGAGGCCATC
AACGTGGAGCAGGCGTTCCAGACGATTGCACGGAATGCACTTAAGCAGGAAACGGAGGTG
GAGCTGTACAACGAATTTCCTGAACCTATCAAACTGGACAAGAATGACCGGGCCAAGGCC
TCGGCAGAAAGCTGCAGTTGCTGA
Chromosome Location
3
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP51149
UniProtKB Entry NameRAB7A_HUMAN
HGNC IDHGNC:9788
General References
  1. Vitelli R, Chiariello M, Lattero D, Bruni CB, Bucci C: Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid. Biochem Biophys Res Commun. 1996 Dec 24;229(3):887-90. [PubMed:8954989]
  2. Davies JP, Cotter PD, Ioannou YA: Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene. Genomics. 1997 Apr 1;41(1):131-4. [PubMed:9126495]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  5. Cantalupo G, Alifano P, Roberti V, Bruni CB, Bucci C: Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J. 2001 Feb 15;20(4):683-93. [PubMed:11179213]
  6. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed:12643545]
  7. Harrison RE, Bucci C, Vieira OV, Schroer TA, Grinstein S: Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Mol Cell Biol. 2003 Sep;23(18):6494-506. [PubMed:12944476]
  8. Stein MP, Feng Y, Cooper KL, Welford AM, Wandinger-Ness A: Human VPS34 and p150 are Rab7 interacting partners. Traffic. 2003 Nov;4(11):754-71. [PubMed:14617358]
  9. Dong J, Chen W, Welford A, Wandinger-Ness A: The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes. J Biol Chem. 2004 May 14;279(20):21334-42. Epub 2004 Mar 2. [PubMed:14998988]
  10. Wang T, Wong KK, Hong W: A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34. Mol Biol Cell. 2004 Feb;15(2):815-26. Epub 2003 Dec 10. [PubMed:14668488]
  11. Johansson M, Lehto M, Tanhuanpaa K, Cover TL, Olkkonen VM: The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell. 2005 Dec;16(12):5480-92. Epub 2005 Sep 21. [PubMed:16176980]
  12. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed:17081065]
  13. Burger A, Amemiya Y, Kitching R, Seth AK: Novel RING E3 ubiquitin ligases in breast cancer. Neoplasia. 2006 Aug;8(8):689-95. [PubMed:16925951]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648]
  15. Zhang M, Chen L, Wang S, Wang T: Rab7: roles in membrane trafficking and disease. Biosci Rep. 2009 Jun;29(3):193-209. doi: 10.1042/BSR20090032. [PubMed:19392663]
  16. Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, Overvatn A, Bjorkoy G, Johansen T: FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol. 2010 Jan 25;188(2):253-69. doi: 10.1083/jcb.200907015. [PubMed:20100911]
  17. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231]
  18. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  19. Wang T, Ming Z, Xiaochun W, Hong W: Rab7: role of its protein interaction cascades in endo-lysosomal traffic. Cell Signal. 2011 Mar;23(3):516-21. doi: 10.1016/j.cellsig.2010.09.012. Epub 2010 Sep 21. [PubMed:20851765]
  20. Seto S, Tsujimura K, Koide Y: Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic. 2011 Apr;12(4):407-20. doi: 10.1111/j.1600-0854.2011.01165.x. Epub 2011 Feb 21. [PubMed:21255211]
  21. Uusi-Rauva K, Kyttala A, van der Kant R, Vesa J, Tanhuanpaa K, Neefjes J, Olkkonen VM, Jalanko A: Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments. Cell Mol Life Sci. 2012 Jun;69(12):2075-89. doi: 10.1007/s00018-011-0913-1. Epub 2012 Jan 20. [PubMed:22261744]
  22. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  23. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712]
  24. Wu M, Wang T, Loh E, Hong W, Song H: Structural basis for recruitment of RILP by small GTPase Rab7. EMBO J. 2005 Apr 20;24(8):1491-501. Epub 2005 Mar 31. [PubMed:15933719]
  25. McCray BA, Skordalakes E, Taylor JP: Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation. Hum Mol Genet. 2010 Mar 15;19(6):1033-47. doi: 10.1093/hmg/ddp567. Epub 2009 Dec 22. [PubMed:20028791]
  26. Verhoeven K, De Jonghe P, Coen K, Verpoorten N, Auer-Grumbach M, Kwon JM, FitzPatrick D, Schmedding E, De Vriendt E, Jacobs A, Van Gerwen V, Wagner K, Hartung HP, Timmerman V: Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy. Am J Hum Genet. 2003 Mar;72(3):722-7. Epub 2003 Jan 21. [PubMed:12545426]
  27. Houlden H, King RH, Muddle JR, Warner TT, Reilly MM, Orrell RW, Ginsberg L: A novel RAB7 mutation associated with ulcero-mutilating neuropathy. Ann Neurol. 2004 Oct;56(4):586-90. [PubMed:15455439]
  28. Meggouh F, Bienfait HM, Weterman MA, de Visser M, Baas F: Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene. Neurology. 2006 Oct 24;67(8):1476-8. [PubMed:17060578]
  29. BasuRay S, Mukherjee S, Romero E, Wilson MC, Wandinger-Ness A: Rab7 mutants associated with Charcot-Marie-Tooth disease exhibit enhanced NGF-stimulated signaling. PLoS One. 2010 Dec 9;5(12):e15351. doi: 10.1371/journal.pone.0015351. [PubMed:21151572]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04315Guanosine-5'-DiphosphateexperimentalunknownDetails