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Gene Review

atp6ap1.2  -  ATPase, H+ transporting, lysosomal...

Xenopus laevis

Synonyms: ac45, atp6ip1, atp6s1, vatps1, x1311, ...
 
 
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Disease relevance of X1311

  • Either the 11-amino acid span of the vesicular stomatitis virus (VSV) G glycoprotein (P5D4 epitope) or a 6-amino acid epitope of the bovine papilloma virus capsid protein (AU1) was genetically engineered on the extreme N terminus of CCD-IRK3 [1].
  • The gene responsible for the lethal disorder cystic fibrosis encodes a 1480-amino acid glycoprotein, CFTR [2].
  • Mutations of the glycoprotein rBAT cause cystinuria type I, an autosomal recessive failure of dibasic amino acid transport (b(0,+) type) across luminal membranes of intestine and kidney cells [3].
  • An epitope from the coronavirus E1 glycoprotein was inserted into CHIP and localized to the outer or inner leaflet of the membrane by alpha-chymotrypsin digestion of intact oocytes or inside-out membrane vesicles [4].
  • 14-3-3 binds ligands such as Raf-1 kinase and Bad by recognizing the phosphorylated consensus motif, RSXpSXP, but must bind unphosphorylated ligands, such as glycoprotein Ib and Pseudomonas aeruginosa exoenzyme S, via a different motif [5].
 

High impact information on X1311

  • This in vivo pathway is rich in fibronectin, a glycoprotein that promotes cell adhesion and migration in vitro [6].
  • This glycoprotein is found in activated lymphocytes, together with an uncharacterized, disulphide-linked lipophilic light chain with an apparent relative molecular mass of 40,000 (M(r) 40K) [7].
  • The homologous protein from Schistosoma mansoni, SPRM1, also associates covalently with coexpressed h4F2hc glycoprotein, although it induces amino-acid transport of different substrate specificity [7].
  • Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts [8].
  • These oocytes specifically bound the gp70 envelope glycoprotein from an ecotropic murine leukaemia virus [9].
 

Biological context of X1311

 

Anatomical context of X1311

 

Associations of X1311 with chemical compounds

  • Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2 [20].
  • The nicotinic acetylcholine receptor (AcChoR) of Torpedo electroplax is a multisubunit transmembrane glycoprotein complex with a subunit stoichiometry of alpha 2 beta gamma delta [21].
  • Castanospermine (Cas), an inhibitor of alpha-glucosidase I, blocks "trimming" of the N-linked oligosaccharide Glc3Man9GlcNAc2, thus preventing normal glycoprotein maturation [22].
  • Both approaches indicated that estrogen did not have a preferential stimulatory effect on the general expression of glycoprotein mRNA [14].
  • Prostatic binding protein (PBP), a hormonally controlled oligomeric glycoprotein secreted by the rat ventral prostate, is composed of three different polypeptide chains, C1, C2, and C3 [23].
 

Other interactions of X1311

  • Additionally, processing at two pairs of basic residues is suggested to liberate two polypeptides ("spasmolysins") and "spasmolysin-glycoprotein."[24]
  • Noelin-1 is a secreted glycoprotein that likely forms large multiunit complexes [25].
  • Envelope conversion involves the pars recta protease oviductin, which selectively hydrolyzes envelope glycoprotein gp43 to gp41 [26].
  • From a dendrogram of known egg envelope glycoproteins, the new glycoprotein was shown to be unique among egg envelope components and was designated ZPD [27].
  • In vitro [3H]fucose incorporation studies combined with in vivo light and electron microscopic autoradiographic analysis, showed that the IRBP-like glycoprotein is synthesized by the neural retina and secreted into the interphotoreceptor matrix [28].
 

Analytical, diagnostic and therapeutic context of X1311

References

  1. Basolateral membrane targeting of a renal-epithelial inwardly rectifying potassium channel from the cortical collecting duct, CCD-IRK3, in MDCK cells. Le Maout, S., Brejon, M., Olsen, O., Merot, J., Welling, P.A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. CFTR protein expression in primary and cultured epithelia. Zeitlin, P.L., Crawford, I., Lu, L., Woel, S., Cohen, M.E., Donowitz, M., Montrose, M.H., Hamosh, A., Cutting, G.R., Gruenert, D. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  3. Luminal heterodimeric amino acid transporter defective in cystinuria. Pfeiffer, R., Loffing, J., Rossier, G., Bauch, C., Meier, C., Eggermann, T., Loffing-Cueni, D., Kühn, L.C., Verrey, F. Mol. Biol. Cell (1999) [Pubmed]
  4. Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. Preston, G.M., Jung, J.S., Guggino, W.B., Agre, P. J. Biol. Chem. (1994) [Pubmed]
  5. 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. Petosa, C., Masters, S.C., Bankston, L.A., Pohl, J., Wang, B., Fu, H., Liddington, R.C. J. Biol. Chem. (1998) [Pubmed]
  6. Primordial germ cells of Xenopus embryos: the role of fibronectin in their adhesion during migration. Heasman, J., Hynes, R.O., Swan, A.P., Thomas, V., Wylie, C.C. Cell (1981) [Pubmed]
  7. Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family. Mastroberardino, L., Spindler, B., Pfeiffer, R., Skelly, P.J., Loffing, J., Shoemaker, C.B., Verrey, F. Nature (1998) [Pubmed]
  8. Cloning and characterization of the vasopressin-regulated urea transporter. You, G., Smith, C.P., Kanai, Y., Lee, W.S., Stelzner, M., Hediger, M.A. Nature (1993) [Pubmed]
  9. Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter. Wang, H., Kavanaugh, M.P., North, R.A., Kabat, D. Nature (1991) [Pubmed]
  10. Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein. Yost, C.S., Lopez, C.D., Prusiner, S.B., Myers, R.M., Lingappa, V.R. Nature (1990) [Pubmed]
  11. Cloning, functional analysis and cell localization of a kidney proximal tubule water transporter homologous to CHIP28. Zhang, R., Skach, W., Hasegawa, H., van Hoek, A.N., Verkman, A.S. J. Cell Biol. (1993) [Pubmed]
  12. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. Finlay, D.R., Newmeyer, D.D., Price, T.M., Forbes, D.J. J. Cell Biol. (1987) [Pubmed]
  13. Targeted disruption of mouse fibroblast activation protein. Niedermeyer, J., Kriz, M., Hilberg, F., Garin-Chesa, P., Bamberger, U., Lenter, M.C., Park, J., Viertel, B., Püschner, H., Mauz, M., Rettig, W.J., Schnapp, A. Mol. Cell. Biol. (2000) [Pubmed]
  14. Selective activation of the N-glycosylation apparatus in uteri by estrogen. Carson, D.D., Farrar, J.D., Laidlaw, J., Wright, D.A. J. Biol. Chem. (1990) [Pubmed]
  15. XTRPC1-dependent chemotropic guidance of neuronal growth cones. Shim, S., Goh, E.L., Ge, S., Sailor, K., Yuan, J.P., Roderick, H.L., Bootman, M.D., Worley, P.F., Song, H., Ming, G.L. Nat. Neurosci. (2005) [Pubmed]
  16. Noelin-1 is a secreted glycoprotein involved in generation of the neural crest. Barembaum, M., Moreno, T.A., LaBonne, C., Sechrist, J., Bronner-Fraser, M. Nat. Cell Biol. (2000) [Pubmed]
  17. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. Powers, M.A., Forbes, D.J., Dahlberg, J.E., Lund, E. J. Cell Biol. (1997) [Pubmed]
  18. B cell growth modulating and differentiating activity of recombinant human 26-kd protein (BSF-2, HuIFN-beta 2, HPGF). Poupart, P., Vandenabeele, P., Cayphas, S., Van Snick, J., Haegeman, G., Kruys, V., Fiers, W., Content, J. EMBO J. (1987) [Pubmed]
  19. Characterization of the gene encoding the human Kidd blood group/urea transporter protein. Evidence for splice site mutations in Jknull individuals. Lucien, N., Sidoux-Walter, F., Olivès, B., Moulds, J., Le Pennec, P.Y., Cartron, J.P., Bailly, P. J. Biol. Chem. (1998) [Pubmed]
  20. Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2. Tian, J., Gong, H., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  21. Control of Torpedo acetylcholine receptor biosynthesis in Xenopus oocytes. Buller, A.L., White, M.M. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  22. Inhibition of oligosaccharide processing and membrane morphogenesis in retinal rod photoreceptor cells. Fliesler, S.J., Rayborn, M.E., Hollyfield, J.G. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  23. Assembly, glycosylation, and secretion of the oligomeric rat prostatic binding protein in Xenopus oocytes. Mous, J.M., Peeters, B.L., Heyns, W.J., Rombauts, W.A. J. Biol. Chem. (1982) [Pubmed]
  24. A new repetitive protein from Xenopus laevis skin highly homologous to pancreatic spasmolytic polypeptide. Hoffmann, W. J. Biol. Chem. (1988) [Pubmed]
  25. The secreted glycoprotein Noelin-1 promotes neurogenesis in Xenopus. Moreno, T.A., Bronner-Fraser, M. Dev. Biol. (2001) [Pubmed]
  26. Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several CUB domains. Lindsay, L.L., Wieduwilt, M.J., Hedrick, J.L. Biol. Reprod. (1999) [Pubmed]
  27. Identification and characterization of a unique Xenopus laevis egg envelope component, ZPD. Lindsay, L.L., Yang, J.C., Hedrick, J.L. Dev. Growth Differ. (2002) [Pubmed]
  28. Interphotoreceptor retinoid-binding protein (IRBP), a major 124 kDa glycoprotein in the interphotoreceptor matrix of Xenopus laevis. Characterization, molecular cloning and biosynthesis. Gonzalez-Fernandez, F., Kittredge, K.L., Rayborn, M.E., Hollyfield, J.G., Landers, R.A., Saha, M., Grainger, R.M. J. Cell. Sci. (1993) [Pubmed]
  29. Monoclonal antibodies prepared against the major Drosophila nuclear Matrix-pore complex-lamina glycoprotein bind specifically to the nuclear envelope in situ. Filson, A.J., Lewis, A., Blobel, G., Fisher, P.A. J. Biol. Chem. (1985) [Pubmed]
  30. The vitelline envelope to fertilization envelope conversion in eggs of Xenopus laevis. Gerton, G.L., Hedrick, J.L. Dev. Biol. (1986) [Pubmed]
  31. Expression of the Lewis group carbohydrate antigens during Xenopus development. Yoshida-Noro, C., Heasman, J., Goldstone, K., Vickers, L., Wylie, C. Glycobiology (1999) [Pubmed]
 
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