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Gene Review

A1cf  -  APOBEC1 complementation factor

Mus musculus

Synonyms: 1810073H04Rik, ACF, ACF64, ACF65, APOBEC1-stimulating protein, ...
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Disease relevance of 1810073H04Rik

  • Mice bearing the Asp mutation in the serine 191 phosphorylation site are runted and anemic and display splenomegaly [1].
  • Mastocytosis is often associated with a somatic point mutation in the Kit protooncogene leading to an Asp/Val substitution at position 816 in the kinase domain of this receptor [2].
  • We have analyzed how the immune system generates antibodies that are specific for analogues of an epitope on the influenza virus hemagglutinin (HA) that differ solely by the presence of Asp or Gly at amino acid 225 [3].
  • In contrast, poly(Arg, Gly, Asp), in which three amino acids are randomly arranged, showed neither inhibition of lung metastases nor any adhesive ability to attach to tumor cells [4].
  • In longitudinal analyses, among subjects in the upper tertile of change in percent body fat, those with Asp/Asp had a larger increase in fasting and postprandial glycemia and basal EGP and a larger decrease in M and AIR than subjects with X/Gly, independent of change in obesity (all P < 0.05) [5].

Psychiatry related information on 1810073H04Rik

  • In a functional presenilin-1 variant (carrying a deletion in exon 9) that is associated with familial Alzheimer's disease and which does not require this cleavage, the Asp 385 --> Ala mutation still inhibited gamma-secretase activity [6].

High impact information on 1810073H04Rik

  • We have previously demonstrated that the pentapeptide Asp/Glu-Trp-Asp/Glu-Tyr-Ser/Gly is a molecular mimic of double-stranded DNA [7].
  • The molecular basis for the little (lit) mouse phenotype, characterized by a hypoplastic anterior pituitary gland, is the mutation of a single nucleotide that alters Asp 60 to Gly in the growth hormone releasing factor receptor [8].
  • The NOD mouse does not express I-E owing to a deletion in the promoter region of the I-E alpha-chain gene, and the sequence of NOD I-A beta-chain in the first external domain is unique with His 56 and Ser 57 replacing Pro and Asp, respectively, at these positions [9].
  • The major excitatory amino acids, glutamate (Glu) and aspartate (Asp), are thought to act at three receptor subtypes in the mammalian central nervous system (CNS) [10].
  • The active site "charge-relay" residues (His57, Asp102, and Ser195 of the chymotrypsin numbering system) are conserved, as well as the trypsin-specific Asp (position 189 in trypsin) [11].

Chemical compound and disease context of 1810073H04Rik


Biological context of 1810073H04Rik

  • Taken together, these data suggest that ACF plays a crucial role, which is independent of apobec-1 expression, in cell survival, particularly during early embryonic development [14].
  • Thr308 and/or Ser473 were mutated to Ala or Asp and activities of mutant PKBalpha molecules were analysed after transfection into 293 cells [15].
  • Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein [16].
  • Lunasin is a unique 43-amino acid soybean peptide that contains at its carboxyl end: (a) nine Asp (D) residues; (b) an Arg-Gly-Asp (RGD) cell adhesion motif; and (c) a predicted helix with structural homology to a conserved region of chromatin-binding proteins [17].
  • The transgenes (integrated copy number, 5-6) in the tumors developed in 55 of 56 affected transgenic mice (98%) contained at least 1 copy of the transgene that was activated by somatic point mutation at the 12th codon, from GGC (Gly) to GAC (Asp) [18].

Anatomical context of 1810073H04Rik

  • Mutant acf(-)(/)(-) embryos were detectable only until the blastocyst (embryonic day 3.5 [E3.5]) stage [14].
  • To examine T cell reactivity to Af antigens, T cell clones (TCC) specific to the Asp f 1 antigen, an 18-kD protein of Af, were established from the peripheral blood of three ABPA patients [19].
  • Furthermore, a mutated recombinant entactin, altered to contain a Glu in place of Asp at the RGD site, provided no trophoblast cell adhesive activity [20].
  • When various amino acid beta-naphthylamides were used as substrates, the preference of the secretory granule enzyme was Ala greater than Leu greater than Phe much greater than Arg much greater than Asp = Tyr [21].
  • In support of these results, COS cell transfection experiments show that phosphomimetic mutation Thr-35 --> Asp or induced cellular PKC caused increased CYP1A1 targeting to MT and correspondingly lower levels to the endoplasmic reticulum [22].

Associations of 1810073H04Rik with chemical compounds

  • Two independent lines of evidence demonstrate that at least two of these acidic residues are directly involved in coordinating a divalent metal ion: The substitution of Cys for Asp allows rescue of some catalytic function, whereas an alanine substitution is no longer subject to iron-induced hydroxyl radical cleavage [23].
  • The proprotein convertases are all dependent on calcium for activity and all possess highly conserved subtilisin-like domains with the characteristic catalytic triad of this serine protease (ordered Asp, His, and Ser along the polypeptide chain) [24].
  • The majority of TCC isolated from ABPA patients, and specific for the Asp f 1 allergen of Af, are IL-4 producing CD4+ cells of the Th2 phenotype [19].
  • A human phosphorylcholine-binding myeloma protien also had Phe, Tyr, and Met at positions 32, 33, and 34, but had Asp instead of Glu at position 35 and showed a lower binding constant [25].
  • One allele had a single nucleotide substitution of A to G in the NH2-terminal domain, which altered Asp to Ser at amino acid 363 [26].

Other interactions of 1810073H04Rik


Analytical, diagnostic and therapeutic context of 1810073H04Rik

  • Using site-directed mutagenesis, we constructed a mutant mouse lung carbonyl reductase in which Thr-38 was replaced by Asp (T38D), and we compared kinetic properties of the mutant and wild-type enzymes in both forward and reverse reactions [28].
  • Sequence analysis showed that Dub-1A encodes a 468-amino acid protein that has a molecular mass of approximately 51 kDa and that contains a putative catalytic domain (Cys, His, and Asp) conserved among DUB proteins [29].
  • One mutant, M1, at position 97 (Asp to Ala) in CDR3 of the heavy chain, resulted in an 8- to 10-fold improvement in Ag binding, as assessed by ELISA [30].
  • 6. In cross-sectional analyses, subjects homozygous for the Asp1057 allele (Asp/Asp) had a higher prevalence of type 2 diabetes than heterozygote individuals and subjects homozygous for the Gly1057 allele (X/Gly, P = 0.04) [5].
  • Five murine IgG MAbs and two IgM MAbs were raised against the 2M fraction, and immunoprecipitation with the IgG MAb demonstrated two distinct antigens within the 2M fraction, Asp f I, and a 16 kd antigen [31].


  1. A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region. Hua, Z.C., Sohn, S.J., Kang, C., Cado, D., Winoto, A. Immunity (2003) [Pubmed]
  2. Mastocytosis in mice expressing human Kit receptor with the activating Asp816Val mutation. Zappulla, J.P., Dubreuil, P., Desbois, S., Létard, S., Hamouda, N.B., Daëron, M., Delsol, G., Arock, M., Liblau, R.S. J. Exp. Med. (2005) [Pubmed]
  3. Antibodies that are specific for a single amino acid interchange in a protein epitope use structurally distinct variable regions. Stark, S.E., Caton, A.J. J. Exp. Med. (1991) [Pubmed]
  4. Inhibition of the metastasis of murine malignant melanoma by synthetic polymeric peptides containing core sequences of cell-adhesive molecules. Saiki, I., Iida, J., Murata, J., Ogawa, R., Nishi, N., Sugimura, K., Tokura, S., Azuma, I. Cancer Res. (1989) [Pubmed]
  5. Metabolic effects of the Gly1057Asp polymorphism in IRS-2 and interactions with obesity. Stefan, N., Kovacs, P., Stumvoll, M., Hanson, R.L., Lehn-Stefan, A., Permana, P.A., Baier, L.J., Tataranni, P.A., Silver, K., Bogardus, C. Diabetes (2003) [Pubmed]
  6. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Wolfe, M.S., Xia, W., Ostaszewski, B.L., Diehl, T.S., Kimberly, W.T., Selkoe, D.J. Nature (1999) [Pubmed]
  7. A subset of lupus anti-DNA antibodies cross-reacts with the NR2 glutamate receptor in systemic lupus erythematosus. DeGiorgio, L.A., Konstantinov, K.N., Lee, S.C., Hardin, J.A., Volpe, B.T., Diamond, B. Nat. Med. (2001) [Pubmed]
  8. Molecular basis of the little mouse phenotype and implications for cell type-specific growth. Lin, S.C., Lin, C.R., Gukovsky, I., Lusis, A.J., Sawchenko, P.E., Rosenfeld, M.G. Nature (1993) [Pubmed]
  9. Prevention of insulin-dependent diabetes mellitus in non-obese diabetic mice by transgenes encoding modified I-A beta-chain or normal I-E alpha-chain. Lund, T., O'Reilly, L., Hutchings, P., Kanagawa, O., Simpson, E., Gravely, R., Chandler, P., Dyson, J., Picard, J.K., Edwards, A. Nature (1990) [Pubmed]
  10. Glutamate stimulates inositol phosphate formation in striatal neurones. Sladeczek, F., Pin, J.P., Récasens, M., Bockaert, J., Weiss, S. Nature (1985) [Pubmed]
  11. Cloning of a cDNA for a T cell-specific serine protease from a cytotoxic T lymphocyte. Gershenfeld, H.K., Weissman, I.L. Science (1986) [Pubmed]
  12. Necessity of tyrosine 719 and phosphatidylinositol 3'-kinase-mediated signal pathway in constitutive activation and oncogenic potential of c-kit receptor tyrosine kinase with the Asp814Val mutation. Hashimoto, K., Matsumura, I., Tsujimura, T., Kim, D.K., Ogihara, H., Ikeda, H., Ueda, S., Mizuki, M., Sugahara, H., Shibayama, H., Kitamura, Y., Kanakura, Y. Blood (2003) [Pubmed]
  13. Design and chemical synthesis of a magnetic resonance contrast agent with enhanced in vitro binding, high blood-brain barrier permeability, and in vivo targeting to Alzheimer's disease amyloid plaques. Poduslo, J.F., Curran, G.L., Peterson, J.A., McCormick, D.J., Fauq, A.H., Khan, M.A., Wengenack, T.M. Biochemistry (2004) [Pubmed]
  14. Targeted deletion of the murine apobec-1 complementation factor (acf) gene results in embryonic lethality. Blanc, V., Henderson, J.O., Newberry, E.P., Kennedy, S., Luo, J., Davidson, N.O. Mol. Cell. Biol. (2005) [Pubmed]
  15. Mechanism of activation of protein kinase B by insulin and IGF-1. Alessi, D.R., Andjelkovic, M., Caudwell, B., Cron, P., Morrice, N., Cohen, P., Hemmings, B.A. EMBO J. (1996) [Pubmed]
  16. The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region. Hu, M.C., Sharp, S.B., Davidson, N. Mol. Cell. Biol. (1986) [Pubmed]
  17. Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation. Galvez, A.F., Chen, N., Macasieb, J., de Lumen, B.O. Cancer Res. (2001) [Pubmed]
  18. Chemically induced forestomach papillomas in transgenic mice carry mutant human c-Ha-ras transgenes. Ando, K., Saitoh, A., Hino, O., Takahashi, R., Kimura, M., Katsuki, M. Cancer Res. (1992) [Pubmed]
  19. T cell subsets, epitope mapping, and HLA-restriction in patients with allergic bronchopulmonary aspergillosis. Chauhan, B., Knutsen, A., Hutcheson, P.S., Slavin, R.G., Bellone, C.J. J. Clin. Invest. (1996) [Pubmed]
  20. Recombinant entactin promotes mouse primary trophoblast cell adhesion and migration through the Arg-Gly-Asp (RGD) recognition sequence. Yelian, F.D., Edgeworth, N.A., Dong, L.J., Chung, A.E., Armant, D.R. J. Cell Biol. (1993) [Pubmed]
  21. Identification of aminopeptidase activity in the secretory granules of mouse mast cells. Serafin, W.E., Guidry, U.A., Dayton, E.T., Kamada, M.M., Stevens, R.L., Austen, K.F. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  22. Role of Protein Kinase C-mediated Protein Phosphorylation in Mitochondrial Translocation of Mouse CYP1A1, Which Contains a Non-canonical Targeting Signal. Dasari, V.R., Anandatheerthavarada, H.K., Robin, M.A., Boopathi, E., Biswas, G., Fang, J.K., Nebert, D.W., Avadhani, N.G. J. Biol. Chem. (2006) [Pubmed]
  23. Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase. Kim, D.R., Dai, Y., Mundy, C.L., Yang, W., Oettinger, M.A. Genes Dev. (1999) [Pubmed]
  24. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Rouillé, Y., Duguay, S.J., Lund, K., Furuta, M., Gong, Q., Lipkind, G., Oliva, A.A., Chan, S.J., Steiner, D.F. Frontiers in neuroendocrinology. (1995) [Pubmed]
  25. Attempts to locate residues in complementarity-determining regions of antibody combining sites that make contact with antigen. Kabat, E.A., Wu, T.T., Bilofsky, H. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  26. Glucocorticoid receptor structure and function in glucocorticoid-resistant small cell lung carcinoma cells. Ray, D.W., Davis, J.R., White, A., Clark, A.J. Cancer Res. (1996) [Pubmed]
  27. The peroxisome proliferator-activated receptor alpha (PPARalpha) agonist ciprofibrate inhibits apolipoprotein B mRNA editing in low density lipoprotein receptor-deficient mice: effects on plasma lipoproteins and the development of atherosclerotic lesions. Fu, T., Mukhopadhyay, D., Davidson, N.O., Borensztajn, J. J. Biol. Chem. (2004) [Pubmed]
  28. Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid. Nakanishi, M., Matsuura, K., Kaibe, H., Tanaka, N., Nonaka, T., Mitsui, Y., Hara, A. J. Biol. Chem. (1997) [Pubmed]
  29. DUB-1A, a novel deubiquitinating enzyme subfamily member, is polyubiquitinated and cytokine-inducible in B-lymphocytes. Baek, K.H., Kim, M.S., Kim, Y.S., Shin, J.M., Choi, H.K. J. Biol. Chem. (2004) [Pubmed]
  30. Affinity maturation of the BR96 anti-carcinoma antibody by codon-based mutagenesis. Yelton, D.E., Rosok, M.J., Cruz, G., Cosand, W.L., Bajorath, J., Hellström, I., Hellström, K.E., Huse, W.D., Glaser, S.M. J. Immunol. (1995) [Pubmed]
  31. Aspergillus fumigatus: identification of 16, 18, and 45 kd antigens recognized by human IgG and IgE antibodies and murine monoclonal antibodies. Arruda, L.K., Platts-Mills, T.A., Longbottom, J.L., el-Dahr, J.M., Chapman, M.D. J. Allergy Clin. Immunol. (1992) [Pubmed]
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