scholarly journals The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange

1983 ◽  
Vol 213 (3) ◽  
pp. 577-586 ◽  
Author(s):  
C J Brock ◽  
M J A Tanner ◽  
C Kempf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mechanism ◽  
Anion Exchange ◽  
Human Erythrocyte ◽  
Exchange Process ◽  
Anion Transport ◽  
Transport Protein ◽  
British Library ◽  
Alpha Helices

The N-terminal 72 residues of an integral membrane fragment, P5, of the human erythrocyte anion-transport protein, which is known to be directly involved in the anion-exchange process, was shown to have the following amino acid sequence: Met-Val-Pro-Lys-Pro-Gln-Gly-Pro-Leu-Pro-Asn-Thr-Ala-Leu-Leu-Ser-Leu-Val-Leu-Met -Ala-Gly-Thr-Phe-Phe-Phe-Ala-Met-Met-Leu-Arg-Lys-Phe-Lys-Asn-Ser-Ser-Tyr-Phe-Pro-Gly-Lys-Leu-Arg-Arg-Val-Ile-Gly-Asp-Phe-Gly-Val-Pro-Ile-Ser-Ile-Leu-Ile-Met-Val-Leu-Val-Asp-Phe-Phe-Ile-Gln-Asp-Thr-Tyr-Thr-Gln- The structure of this fragment was analysed, with account being taken of the constraints that apply to the folding of integral membrane proteins and the topographical locations of various sites in the sequence. It was concluded that this sequence forms two transmembrane alpha-helices. These are probably part of a cluster of amphipathic transmembrane alpha-helices, which could comprise that part of the protein responsible for transport activity. The presently available evidence relating to the anion-exchange process was considered with the structural features noted in this study and a possible molecular mechanism is proposed. In this model the rearrangement of a network of intramembranous charged pairs mediates the translocation of an anion between anion-binding regions at each surface of the membrane, which are composed of clusters of positively charged amino acids. This model imposes a sequential exchange mechanism on the system. Supplementary material, including Tables and Figures describing the compositions of peptides determined by amino acid analysis and sequence studies, quantitative and qualitative data that provide a residue-by-residue justification for the sequence assignment and a description of modifications to and use of the solid-phase sequencer has been deposited as Supplementary Publication SUP 50123 (12 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained as indicated in Biochem. J. (1983) 209, 5.

scholarly journals The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence

1988 ◽  
Vol 256 (3) ◽  
pp. 703-712 ◽  
Author(s):  
M J A Tanner ◽  
P G Martin ◽  
S High
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Band ◽  
Anion Transport ◽  
Transport Protein ◽  
Cdna Clones ◽  
Red Cell ◽  
Coding Region ◽  
Red Cell Membrane ◽  
Anion Transporter

1. We have isolated cDNA clones corresponding to the red cell membrane anion-transport protein (Band 3). 2. The cDNA clones cover 3475 bases of the mRNA and contain the entire protein-coding region, 150 bases of the 5′ untranslated region and part of the 3′ non-coding region, but do not extend to the 3′ end of the mRNA. 3. The translated protein sequence predicts that the human red cell anion transporter contains 911 amino acids. 4. The availability of the amino acid sequence allows the interpretation of some of the many studies on the chemical and proteolytic modification of the human protein aimed at examining the structure and mechanism of this membrane transport protein.

scholarly journals The membrane domain of the human erythrocyte anion transport protein. Epitope mapping of a monoclonal antibody defines the location of a cytoplasmic loop near the C-terminus of the protein

1990 ◽  
Vol 272 (1) ◽  
pp. 265-268 ◽  
Author(s):  
S D Wainwright ◽  
W J Mawby ◽  
M J A Tanner
Keyword(s):  
Amino Acid ◽  
Human Erythrocyte ◽  
Protein Band ◽  
Anion Transport ◽  
Transport Protein ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
C Terminus ◽  
Murine Monoclonal Antibodies ◽  
Cytoplasmic Side

We have used synthetic peptides to study the location of the amino acid sequences in the human erythrocyte anion transport protein (band 3) which are recognized by four murine monoclonal antibodies, BRIC 130, 132, 154 and 155. These antibodies are known to react with epitopes in the protein which are on the cytoplasmic side of the membrane. The results suggest that the amino acid residues important for the reaction of BRIC 130 and BRIC 154/155 are located within amino acids 899-908 and 895-901 respectively in the cytoplasmic tail of the protein. The BRIC 132 epitope is located within amino acid residues 813-824. This is part of a surface loop in the protein which probably extends from residue 814 to residue 832 and is located on the cytoplasmic side of the membrane. These results provide direct evidence for the topographical location of a sequence in a poorly understood region of the protein.

scholarly journals The human erythrocyte anion-transport protein. Further amino acid sequence from the integral membrane domain homologous with the murine protein

1986 ◽  
Vol 235 (3) ◽  
pp. 899-901 ◽  
Author(s):  
C J Brock ◽  
M J A Tanner
Keyword(s):  
Amino Acid ◽  
Human Erythrocyte ◽  
Proteolytic Enzymes ◽  
Transmembrane Helix ◽  
Anion Transport ◽  
Transport Protein ◽  
Membrane Domain ◽  
C Terminus ◽  
N Terminus ◽  
Almost All

Sequences from the human erythrocyte anion-transport protein homologous with residues 417-449 and 794-813 of the murine erythrocyte anion-transport protein have been determined. The former sequence includes the putative transmembrane helix closest to the N-terminus of the protein. The latter sequence traverses almost all of the lipid bilayer and is located towards the C-terminus of the protein. Sites have been identified by alignment with the murine sequence in the integral membrane domain that are accessible to proteolytic enzymes. Sequences from the integral membrane domain of the erythrocyte anion-transport protein are highly conserved.

Conformation and stability of the anion transport protein of human erythrocyte membranes

Biochemistry ◽  
1985 ◽  
Vol 24 (12) ◽  
pp. 2843-2848 ◽  
Author(s):  
Kimio Oikawa ◽  
Debra M. Lieberman ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Human Erythrocyte ◽  
Anion Transport ◽  
Transport Protein ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

scholarly journals The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster

1980 ◽  
Vol 187 (3) ◽  
pp. 875-883 ◽  
Author(s):  
D R Thatcher
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alcohol Dehydrogenase ◽  
Aspartic Acid ◽  
Structure Prediction ◽  
Secondary Structure Prediction ◽  
British Library ◽  
Horse Liver ◽  
And Staphylococcus Aureus

The sequence of three alcohol dehydrogenase alleloenzymes from the fruitfly Drosophila melanogaster has been determined by the sequencing of peptides produced by trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus-V8-proteinase digestion. The amino acid sequence shows no obvious homology with the published sequences of the horse liver and yeast enzymes, and secondary structure prediction suggests that the nucleotide-binding domain is located in the N-terminal half of the molecule. The amino acid substitutions between AdhN-11 (a point mutation of AdhF), AdhS and AdhUF alleloenzymes were identified. AdhN-11 alcohol dehydrogenase differed from the other two by a glycine-14-(AdhS and AdhUF)-to-aspartic acid substitution, the AdhS enzyme from AdhN-11 and AdhUF enzymes by a threonine-192-(AdhN-11 and AdhUF)-to-lysine (AdhS) substitution and the AdhUF enzyme was found to differ by an alanine-45-(AdhS and AdhN-11)-to-aspartic acid (AdhUF) charge substitution and a ‘silent’ asparagine-8-(AdhS and AdhN-11)-to-alanine (AdhUF) substitution. Detailed sequence evidence has been deposited as Supplementary Publication SUP 50107 (36 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals The amino acid sequence of cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015

1973 ◽  
Vol 135 (4) ◽  
pp. 751-758 ◽  
Author(s):  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Attachment Site ◽  
Photosynthetic Bacterium ◽  
Chromatium Vinosum ◽  
British Library ◽  
Pseudomonas Denitrificans ◽  
Single Polypeptide Chain ◽  
C Terminus

The amino acid sequence of the cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015 (Iwasaki's ‘Pseudomonas denitrificans’) has been determined. This organism is the only non-photosynthetic bacterium in which the protein has been found. The protein consists of a single polypeptide chain of 127 residues, with a single haem covalently attached to two cysteines. Unlike normal cytochromes c, the haem attachment site is very close to the C-terminus. The amino acid sequence around the haem attachment site is very similar to that of Chromatium vinosum D cytochrome c′. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50022 at the British Library (Lending Division), (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

Sign in / Sign up

Export Citation Format

Share Document