Article: Molecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator

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TitleMolecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator
AuthorsYorifuji, T1
Lemna, WK1
Ballard, CF1
Rosenbloom, CL1
Rozmahel, R1
Plavsic, N1
Tsui, LC1
Beaudet, AL1
Issue Date1991
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygeno
CitationGenomics, 1991, v. 10 n. 3, p. 547-550 [How to Cite?]
DOI: http://dx.doi.org/10.1016/0888-7543(91)90434-G
AbstractWe have cloned the mouse homolog of the human cystic fibrosis transmembrane conductance regulator (CFTR) using clones isolated from a mouse lung cDNA library and using amplification of cDNA to isolate specific regions. The cDNA was 6304 bp in length and encoded a polypeptide of 1476 amino acids. Comparison of the deduced amino acid sequence showed that the mouse protein has high homology to the human protein; overall identity was 78.3%. The amino acid identity was high for both transmembrane domains (first transmembrane domain, 86.7%; second transmembrane domain, 81.1%) and for both ATP-binding folds (first ATP-binding fold, 80.5%; second ATP-binding fold, 83.9%), suggesting the functional importance of these regions. On the other hand, the R domain was less well conserved (68.9% identity). All of the published missense mutation sites and the site of the common ΔF508 mutation were conserved between human and mouse.
ISSN0888-7543
2011 Impact Factor: 3.019
2011 SCImago Journal Rankings: 0.452
DOIhttp://dx.doi.org/10.1016/0888-7543(91)90434-G
ISI Accession Number IDWOS:A1991FQ64000005
DC Field
Value
dc.contributor.authorYorifuji, T
dc.contributor.authorLemna, WK
dc.contributor.authorBallard, CF
dc.contributor.authorRosenbloom, CL
dc.contributor.authorRozmahel, R
dc.contributor.authorPlavsic, N
dc.contributor.authorTsui, LC
dc.contributor.authorBeaudet, AL
dc.date.accessioned2007-09-12T03:49:47Z
dc.date.available2007-09-12T03:49:47Z
dc.date.issued1991
dc.description.abstractWe have cloned the mouse homolog of the human cystic fibrosis transmembrane conductance regulator (CFTR) using clones isolated from a mouse lung cDNA library and using amplification of cDNA to isolate specific regions. The cDNA was 6304 bp in length and encoded a polypeptide of 1476 amino acids. Comparison of the deduced amino acid sequence showed that the mouse protein has high homology to the human protein; overall identity was 78.3%. The amino acid identity was high for both transmembrane domains (first transmembrane domain, 86.7%; second transmembrane domain, 81.1%) and for both ATP-binding folds (first ATP-binding fold, 80.5%; second ATP-binding fold, 83.9%), suggesting the functional importance of these regions. On the other hand, the R domain was less well conserved (68.9% identity). All of the published missense mutation sites and the site of the common ΔF508 mutation were conserved between human and mouse.
dc.description.natureabstract
dc.identifier.citationGenomics, 1991, v. 10 n. 3, p. 547-550 [How to Cite?]
DOI: http://dx.doi.org/10.1016/0888-7543(91)90434-G
dc.identifier.doihttp://dx.doi.org/10.1016/0888-7543(91)90434-G
dc.identifier.epage550
dc.identifier.isiWOS:A1991FQ64000005
dc.identifier.issn0888-7543
2011 Impact Factor: 3.019
2011 SCImago Journal Rankings: 0.452
dc.identifier.issue3
dc.identifier.pmid1716243
dc.identifier.scopuseid_2-s2.0-0025789705
dc.identifier.spage547
dc.identifier.urihttp://hdl.handle.net/10722/44245
dc.identifier.volume10
dc.languageeng
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygeno
dc.publisher.placeUnited States
dc.relation.ispartofGenomics
dc.subject.meshCystic fibrosis transmembrane conductance regulator
dc.subject.meshAmino acid sequence
dc.subject.meshDna - genetics
dc.subject.meshMembrane proteins - genetics
dc.subject.meshMice - genetics
dc.titleMolecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator
dc.typeArticle
Author Affiliations
  1. Baylor College of Medicine