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. 1986 Apr;83(8):2363–2367. doi: 10.1073/pnas.83.8.2363

Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family.

N Ishioka, N Takahashi, F W Putnam
PMCID: PMC323297  PMID: 3458201

Abstract

The complete amino acid sequence has been determined for alpha 1B-glycoprotein (alpha 1B), a protein of unknown function present in human plasma. This protein (Mr approximately equal to 63,000) consists of a single polypeptide chain N-linked to four glucosamine oligosaccharides. The polypeptide has five intrachain disulfide bonds and contains 474 amino acid residues. Analysis of the amino acid sequence by several computer programs shows that alpha 1B exhibits internal duplication and consists of five repeating structural domains, each containing about 95 amino acids and one disulfide bond. alpha 1B has a unique amino acid sequence. However, several domains of alpha 1B, especially the third, show statistically significant homology to variable regions of certain immunoglobulin light and heavy chains. alpha 1B also exhibits sequence similarity to other members of the immunoglobulin supergene family such as the receptor for transepithelial transport of IgA and IgM and the secretory component of human IgA. Because of its internal duplication and its sequence homology to immunoglobulin-like proteins, alpha 1B appears to have evolved from an ancestral gene similar to that of the immunoglobulin supergene family.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chung L. P., Bentley D. R., Reid K. B. Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system. Biochem J. 1985 Aug 15;230(1):133–141. doi: 10.1042/bj2300133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Church W. R., Jernigan R. L., Toole J., Hewick R. M., Knopf J., Knutson G. J., Nesheim M. E., Mann K. G., Fass D. N. Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins. Proc Natl Acad Sci U S A. 1984 Nov;81(22):6934–6937. doi: 10.1073/pnas.81.22.6934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M., Klingmüller D., Weber M. H., Hilschmann N. Die Primärstruktur der menschlichen freien Sekretkomponente und die Anordnung der Disulfidbrücken. Hoppe Seylers Z Physiol Chem. 1984 Dec;365(12):1489–1495. [PubMed] [Google Scholar]
  4. Hood L., Kronenberg M., Hunkapiller T. T cell antigen receptors and the immunoglobulin supergene family. Cell. 1985 Feb;40(2):225–229. doi: 10.1016/0092-8674(85)90133-3. [DOI] [PubMed] [Google Scholar]
  5. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  6. Leonard W. J., Depper J. M., Kanehisa M., Krönke M., Peffer N. J., Svetlik P. B., Sullivan M., Greene W. C. Structure of the human interleukin-2 receptor gene. Science. 1985 Nov 8;230(4726):633–639. doi: 10.1126/science.2996141. [DOI] [PubMed] [Google Scholar]
  7. Lozier J., Takahashi N., Putnam F. W. Complete amino acid sequence of human plasma beta 2-glycoprotein I. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3640–3644. doi: 10.1073/pnas.81.12.3640. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Mostov K. E., Friedlander M., Blobel G. The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains. Nature. 1984 Mar 1;308(5954):37–43. doi: 10.1038/308037a0. [DOI] [PubMed] [Google Scholar]
  10. SCHULTZE H. E., HEIDE K., HAUPT H. ISOLATION OF AN EASILY PRECIPITABLE ALPHA1-GLYCOPROTEIN OF HUMAN SERUM. Nature. 1963 Dec 14;200:1103–1103. doi: 10.1038/2001103a0. [DOI] [PubMed] [Google Scholar]
  11. Takahashi N., Ishioka N., Takahashi Y., Putnam F. W. Automated tandem high-performance liquid chromatographic system for separation of extremely complex peptide mixtures. J Chromatogr. 1985 Jun 19;326:407–418. doi: 10.1016/s0021-9673(01)87466-5. [DOI] [PubMed] [Google Scholar]
  12. Takahashi N., Ortel T. L., Putnam F. W. Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule. Proc Natl Acad Sci U S A. 1984 Jan;81(2):390–394. doi: 10.1073/pnas.81.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Takahashi N., Takahashi Y., Ortel T. L., Lozier J. N., Ishioka N., Putnam F. W. Purification of glycopeptides of human plasma proteins by high-performance liquid chromatography. J Chromatogr. 1984 Dec 28;317:11–26. doi: 10.1016/s0021-9673(01)91643-7. [DOI] [PubMed] [Google Scholar]
  14. Takahashi N., Takahashi Y., Putnam F. W. Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. Proc Natl Acad Sci U S A. 1985 Jan;82(1):73–77. doi: 10.1073/pnas.82.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Takahashi N., Takahashi Y., Putnam F. W. Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich alpha 2-glycoprotein of human serum. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1906–1910. doi: 10.1073/pnas.82.7.1906. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Vehar G. A., Keyt B., Eaton D., Rodriguez H., O'Brien D. P., Rotblat F., Oppermann H., Keck R., Wood W. I., Harkins R. N. Structure of human factor VIII. Nature. 1984 Nov 22;312(5992):337–342. doi: 10.1038/312337a0. [DOI] [PubMed] [Google Scholar]
  17. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  18. Williams A. F., Gagnon J. Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin. Science. 1982 May 14;216(4547):696–703. doi: 10.1126/science.6177036. [DOI] [PubMed] [Google Scholar]

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