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Gene Review

PROC  -  protein C (inactivator of coagulation...

Gallus gallus

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Disease relevance of PROC

  • Muscle cells infected at the permissive temperature with temperature-sensitive mutants of Rous sarcoma virus and shifted to the non-permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269) [1].
  • We previously reported our characterizations of the B-lymphoma tumors induced in a highly susceptible line of chickens (15I5 X 7(2)) by the avian leukosis virus RAV-1 (Proc. Natl. Acad. Sci. 78:3418-3422, 1981) [2].
  • A reverse genetics system for birnavirus, based on synthetic transcripts of the infectious bursal disease virus (IBDV) genome, was recently developed (E. Mundt and V. N. Vakharia, Proc. Natl. Acad. Sci. USA 93:11131-11136, 1996) [3].
  • The avian myeloblastosis virus provirus inserted in a lambda bacteriophage, recombinant clone 11A1-1 (Souza et al., Proc. Natl. Acad. Sci. U.S.A. 77:3004-3008, 1980), was transfected into chicken embryo fibroblasts which had been preinfected with either Rous-associated virus type 61 or the transformation-defective avian sarcoma virus tdB77 [4].
  • To identify the protein encoded by v-rel, the oncogene of reticuloendotheliosis virus (REV-T), antisera have been raised to three synthetic peptides derived from the translation of our previously published v-rel DNA sequence [R.M. Stephens, N.R. Rice, R.R. Hiebsch, H.R. Bose, Jr., and R.V. Gilden, Proc. Natl. Acad. Sci. USA 80, 6229-6233 (1983)] [5].

Psychiatry related information on PROC

  • A recent report has suggested that the interaction between the head and the rod region of smooth muscle myosin at S2 is important for the phosphorylation-mediated regulation of myosin motor activity [Trybus, K. M., Freyzon, Y., Faust, L. Z., and Sweeney, H. L. (1997) Proc. Natl. Acad. Sci. U.S.A. 74, 48-52] [6].

High impact information on PROC

  • This common element, which also comprises several previously proposed skeletal muscle specific motifs [Buskin, J. N. and Hauschka, S. D. (1989) Mol. Cell Biol., 9, 2627-2640; Mar, J. H. and Ordahl, C. P. (1988) Proc. Natl. Acad. Sci. USA, 85, 6404-6408], may account for the coordinate expression of the two subunits [7].
  • The lamin B receptor is a previously identified integral membrane protein in the nuclear envelope of turkey erythrocytes that associates with the nuclear intermediate filament protein lamin B (Worman, H. J., J. Yuan, G. Blobel, and S. D. Georgatos. 1988. Proc. Natl. Acad. Sci. USA. 85:8531-8534) [8].
  • The structure of the intact type IX collagen molecule with the location of both collagenous and noncollagenous domains was as predicted after converting the nucleotide sequence of a cDNA clone encoding for one of the chains of type IX collagen to an amino acid sequence (Ninomiya, Y., and B. R. Olsen, 1984, Proc. Natl. Acad. Sci. USA, 81:3014-3018) [9].
  • The results with both tissues, along with those in previous papers (Geiger, 1979, Cell. 18:193-205.; Geiger et al., 1980, Proc. Natl. Acad. Sci. U. S. A. 77:4127-4131), suggest that vinculin may play an important and widespread role in the linkage of actin-containing microfilament bundles to membranes [10].
  • To approach this problem, we have investigated an alternative method of gene transfer, "transferrinfection," in which DNA complexed to transferrin-polycation conjugates is introduced into cells by receptor-mediated endocytosis [Wagner, E., Zenke, M., Cotten, M., Beug, H. & Birnstiel, M. L. (1990) Proc. Natl. Acad. Sci. USA 87, 3410-3414] [11].

Biological context of PROC

  • A chicken calmodulin pseudogene with no introns was previously shown to hybridize under stringent conditions with an mRNA species present in skeletal and cardiac muscles, yet it would not hybridize to calmodulin mRNA (J. P. Stein, R. P. Munjaal, L. Lagace', E. C. Lai, B. W. O'Malley, and A. R. Means, Proc. Natl. Acad. Sci. USA 80:6485-6489, 1983) [12].
  • This analysis and a comparison with the nucleotide sequence of the cDNApYN1738 (Ninomiya, Y., and Olsen, B.R. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 3014-3018) shows that HMW and LMW are pepsin-resistant fragments of a unique collagen composed of molecules with three different polypeptide chains (alpha-chains) [13].
  • On the basis of x-ray crystallographic studies of the complex of apoenzyme with N-(5'-phosphopyridoxyl)-aspartate (minus pyridoxal form of the enzyme), Arg 292 has been proposed as the binding site of the distal carboxylate group (Ford, G. C., Eichele, G., and Jansonius, J. N. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 2559-2563) [14].
  • The basic residue, Arg-16, was found to have a strong influence on the kinetics of phosphorylation similar to that reported previously for the three adjacent residues, Lys-11, Lys-12, and Lys-13 (Kemp, B. E., Pearson, R. B., and House, C. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 7471-7475) [15].
  • A segment of chick elastin cDNA cloned in the plasmid pBR322 was sequenced by the method of Maxam and Gilbert ((1977) Proc. Natl. Acad. Sci. U. S. A. 74, 560-564) and the 192-base pair insert was found to be derived from the nontranslated region of the 3' end of the mRNA [16].

Anatomical context of PROC

  • Filamin is a major high-molecular-weight protein in smooth muscle which was recently identified and isolated [Wang, K., Ash, J. F. & Singer, S. J. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 4483-4486] [17].
  • A specific RNase protection assay revealed that, in contrast to a previous report (K. Strebhardt, J. I. Mullins, C. Bruck, and H. Rübsamen-Waigmann, Proc. Natl. Acad. Sci. USA 84:8778-8782, 1987), tkl expression is restricted to the lymphoid tissues thymus and spleen [18].
  • Filamin, a protein recently identified in chicken gizzard (Wang, K., Ash, F., and Singer, S. J. (1975) Proc. Natl. Acad. Sci. U. S. A. 72, 4483-4486), has been purified free of other components and its molecular properties have been examined [19].
  • We previously reported the characterization of a rabbit uterus cDNA clone (SMHC29) which encoded part of the light meromyosin of smooth muscle myosin heavy chain (Nagai, R., Larson, D.M., and Periasamy, M. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 1047-1051) [20].
  • (Proc. Natl. Acad. Sci. USA 88, 1510-1520, 1991) showed that treatment of atrioventricular canal endocardial and myocardial cocultures with TGFbeta3 antisense oligodeoxynucleotides blocked mesenchyme formation [21].

Associations of PROC with chemical compounds

  • Furthermore, the 3' end of the insert overlapped with 23 bases at the 5' end of the published sequence for the C-terminal globular domain (Sai, S., Tanaka, T., Kosher, R. A., and Tanzer, M. L. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 5081-5085), which oriented this clone, as well as the CS peptide, along the protein core [22].
  • This sequence bears a striking analogy to part of a highly conserved region of lactate dehydrogenase (residues 100 to 109) (Taylor, S. S., Oxley, S. S., Allison, W. S., and Kaplan, N. O. (1973) Proc. Natl. Acad. Sci. U. S. A. 70, 1970-1974) [23].
  • The bound creatine kinase is located at the M-band and contributes to the electron density of this sarcomeric structure (Wallimann, T., Pelloni, G.W., Turner, D.C., and Eppenberger, H. M. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 4296-4300) [24].
  • Together with our previous results (Palmiter, R.D., Gagnon, J., and Walsh, K.A. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 94-98), these data show that the only co-translational processing event at the NH2 terminus of the primary translation product is the replacement of the initiator methionine by an acetyl group [25].
  • The altered feather pattern obtained by disrupting proteoglycan structure is highly similar to that obtained when skins are cultured in the presence of antibodies to L-CAM (W.J. Gallin, C.-M., Chuong, L.H. Finkel, and G.M. Edelman (1986), Proc. Natl. Acad. Sci. USA 83, 8235-8239) [26].

Analytical, diagnostic and therapeutic context of PROC

  • Antibody probes of Western blots [Renart, J., Reiser, J., & Stark, G. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 3116] of chicken liver homogenates under various conditions revealed that glycinamide ribonucleotide transformylase can be rapidly proteolyzed in such homogenates [27].
  • This structure is similar to the structure of the globular domain of histone H5 (GH5) obtained both by NMR spectroscopy [Zarbock et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7628-7632; Clore et al. (1987) EMBO J. 6, 1833-1842] and by X-ray crystallography [Ramakrishnan et al. (1993) Nature 362, 219-223] [28].


  1. A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors. Anthony, D.T., Jacobs-Cohen, R.J., Marazzi, G., Rubin, L.L. J. Cell Biol. (1988) [Pubmed]
  2. Orientation and position of avian leukosis virus DNA relative to the cellular oncogene c-myc in B-lymphoma tumors of highly susceptible 15I5 X 7(2) chickens. Fung, Y.K., Crittenden, L.B., Kung, H.J. J. Virol. (1982) [Pubmed]
  3. Generation of a mutant infectious bursal disease virus that does not cause bursal lesions. Yao, K., Goodwin, M.A., Vakharia, V.N. J. Virol. (1998) [Pubmed]
  4. Avian myeloblastosis provirus cloned in a lambda bacteriophage is leukemogenic. Silva, R.F., Perbal, B., Bergmann, D.G., Baluda, M.A. J. Virol. (1982) [Pubmed]
  5. Detection and characterization of the protein encoded by the v-rel oncogene. Rice, N.R., Copeland, T.D., Simek, S., Oroszlan, S., Gilden, R.V. Virology (1986) [Pubmed]
  6. Registration of the rod is not critical for the phosphorylation-dependent regulation of smooth muscle myosin. Ikebe, M., Yamada, M., Mabuchi, K., Kambara, T., Ikebe, R. Biochemistry (1999) [Pubmed]
  7. Expression of the acetylcholine receptor delta-subunit gene in differentiating chick muscle cells is activated by an element that contains two 16 bp copies of a segment of the alpha-subunit enhancer. Wang, X.M., Tsay, H.J., Schmidt, J. EMBO J. (1990) [Pubmed]
  8. The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domains. Worman, H.J., Evans, C.D., Blobel, G. J. Cell Biol. (1990) [Pubmed]
  9. Monoclonal antibody against chicken type IX collagen: preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes. Irwin, M.H., Silvers, S.H., Mayne, R. J. Cell Biol. (1985) [Pubmed]
  10. Immunoelectron microscope studies of membrane-microfilament interactions: distributions of alpha-actinin, tropomyosin, and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells. Geiger, B., Dutton, A.H., Tokuyasu, K.T., Singer, S.J. J. Cell Biol. (1981) [Pubmed]
  11. Receptor-mediated endocytosis of transferrin-polycation conjugates: an efficient way to introduce DNA into hematopoietic cells. Zenke, M., Steinlein, P., Wagner, E., Cotten, M., Beug, H., Birnstiel, M.L. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  12. The nontranscribed chicken calmodulin pseudogene cross-hybridizes with mRNA from the slow-muscle troponin C gene. Putkey, J.A., Carroll, S.L., Means, A.R. Mol. Cell. Biol. (1987) [Pubmed]
  13. The structure of type IX collagen. van der Rest, M., Mayne, R., Ninomiya, Y., Seidah, N.G., Chretien, M., Olsen, B.R. J. Biol. Chem. (1985) [Pubmed]
  14. Chemical modification of a functional arginyl residue (Arg 292) of mitochondrial aspartate aminotransferase. Identification as the binding site for the distal carboxylate group of the substrate. Sandmeier, E., Christen, P. J. Biol. Chem. (1982) [Pubmed]
  15. Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase. Kemp, B.E., Pearson, R.B. J. Biol. Chem. (1985) [Pubmed]
  16. Analysis of elastin gene expression in the developing chick aorta using cloned elastin cDNA. Burnett, W., Finnigan-Bunick, A., Yoon, K., Rosenbloom, J. J. Biol. Chem. (1982) [Pubmed]
  17. Interaction of filamin with f-actin in solution. Wang, K., Singer, S.J. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  18. tkl is the avian homolog of the mammalian lck tyrosine protein kinase gene. Chow, L.M., Ratcliffe, M.J., Veillette, A. Mol. Cell. Biol. (1992) [Pubmed]
  19. Purification and properties of filamin, and actin binding protein from chicken gizzard. Shizuta, Y., Shizuta, H., Gallo, M., Davies, P., Pastan, I. J. Biol. Chem. (1976) [Pubmed]
  20. Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis. Nagai, R., Kuro-o, M., Babij, P., Periasamy, M. J. Biol. Chem. (1989) [Pubmed]
  21. An autocrine function for transforming growth factor (TGF)-beta3 in the transformation of atrioventricular canal endocardium into mesenchyme during chick heart development. Nakajima, Y., Yamagishi, T., Nakamura, H., Markwald, R.R., Krug, E.L. Dev. Biol. (1998) [Pubmed]
  22. Chick cartilage chondroitin sulfate proteoglycan core protein. II. Nucleotide sequence of cDNA clone and localization of the S103L epitope. Krueger, R.C., Fields, T.A., Mensch, J.R., Schwartz, N.B. J. Biol. Chem. (1990) [Pubmed]
  23. The sequence of a peptide containing the active site phosphohistidine residue of phosphoglycerate mutase from chicken breast muscle. Rose, Z.B., Hamasaki, N., Dube, S. J. Biol. Chem. (1975) [Pubmed]
  24. Function of M-line-bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphorylcreatine shuttle in muscle. Wallimann, T., Schlösser, T., Eppenberger, H.M. J. Biol. Chem. (1984) [Pubmed]
  25. Comparison of the NH2-terminal sequence of ovalbumin as synthesized in vitro and in vivo. Gagnon, J., Palmiter, R.D., Walsh, K.A. J. Biol. Chem. (1978) [Pubmed]
  26. Altered proteoglycan synthesis disrupts feather pattern formation in chick embryonic skin. Goetinck, P.F., Carlone, D.L. Dev. Biol. (1988) [Pubmed]
  27. An antibody probe to determine the native species of glycinamide ribonucleotide transformylase in chicken liver. Young, M., Sammons, R.D., Mueller, W.T., Benkovic, S.J. Biochemistry (1984) [Pubmed]
  28. Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure. Cerf, C., Lippens, G., Muyldermans, S., Segers, A., Ramakrishnan, V., Wodak, S.J., Hallenga, K., Wyns, L. Biochemistry (1993) [Pubmed]
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