J. Bellingham et al., Sequence and tissue expression of a novel human carbonic anhydrase-relatedprotein, CARP-2, mapping to chromosome 19q13.3, BIOC BIOP R, 253(2), 1998, pp. 364-367
Citations number
15
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
In this study, we report the identification and characterisation of a novel
carbonic anhydrase related-protein. We have determined that the full lengt
h coding sequence of an anonymous expressed sequenced tag, D19S799E, encode
s a novel carbonic anhydrase related-protein (CARPS) that is 328 amino acid
s in length. This peptide exhibits between 23.1-28.8% amino acid identity w
ith the seven active human carbonic anhydrase (CA) isozymes. Four substitut
ions of key amino acids in the catalytic domain of CAs (equivalent to His94
Arg, His96Leu, His119Gln, and Thr199Ser) are likely to render CARP-2 inacti
ve as a carbonic anhydrase. Northern blot analysis of 23 human tissues indi
cates that CARP2 is expressed abundantly in the brain with moderate express
ion also present in spinal cord and thyroid. D19S799E (and thus CARP2) has
previously been localised close to the polymorphic marker D19S412 and the g
enes DBP and FUT1/FUT2 on 19q13.3. (C) 1998 Academic Press.