Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4. 2

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ;  [1];  [2];  [3]
  1. St. Elizabeth's Hospital, Boston, MA (USA) Tufts Univ. School of Medicine, Boston, MA (USA)
  2. Brigham and Women's Hospital and Harvard Medical School, Boston, MA (USA)
  3. Wistar Institute, Philadelphia, PA (USA)

The complete amino acid sequence for human erythrocyte band 4.2 has been derived from the nucleotide sequence of a full-length 2.35-kilobase (kb) cDNA. The 2.35-kb cDNA was isolated from a human reticulocyte cDNA library made in the expression vector {lambda}gt11. Of the 2348 base pairs (bp), 2073 bp encode 691 amino acids representing 76.9 kDa. RNA blot analysis of human reticulocyte total RNA gives a message size for band 4.2 of 2.4 kb. The amino acid sequence of band 4.2 has homology with two closely related Ca{sup 2+}-dependent crosslinking proteins, guinea pig liver transglutaminase and the a subunit of human coagulation factor XIII, transglutaminase that forms intermolecular {gamma}-glutamyl-{epsilon}-lysine bonds between fibrin molecules. The region of greatest identity includes a 49-amino acid stretch of band 4.2, which is 69% and 51% identical with guinea pig liver transglutaminase and the a subunit of factor XIII, respectively, within the regions that contain the active sites of these enzymes. Significantly, within the five contiguous consensus residues of the transglutaminase active site, Gly-Gln-Cys-Trp-Val, band 4.2 has an alanine substituted for cysteine. Consistent with this active site substitution, erythrocyte membranes or inside-out vesicles, which contain band 4.2, show no evidence of transglutaminase activity by two types of in vitro assay.

OSTI ID:
6700166
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:2; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English

Similar Records

Molecular cloning of human protein 4. 2: A major component of the erythrocyte membrane
Journal Article · Wed Jan 31 23:00:00 EST 1990 · Proceedings of the National Academy of Sciences of the United States of America; (USA) · OSTI ID:6719299

Primary structure of keratinocyte transglutaminase
Journal Article · Fri Nov 30 23:00:00 EST 1990 · Proceedings of the National Academy of Sciences of the United States of America; (United States) · OSTI ID:5044523

Organization of the gene for human erythrocyte membrane protein 4. 2: Structural similarities with the gene for the a subunit of factor XIII
Journal Article · Sat Jun 01 00:00:00 EDT 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States) · OSTI ID:5933793