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J Biol Chem, Vol. 275, Issue 2, 1247-1260, January 14, 2000
From the Departments of Five members of a novel
Ca2+-binding protein subfamily (CaBP), with 46-58%
sequence similarity to calmodulin (CaM), were identified in the
vertebrate retina. Important differences between these Ca2+-binding proteins and CaM include alterations within
their second EF-hand loop that render these motifs inactive in
Ca2+ coordination and the fact that their central
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) short form of human CaBP1, AF169148; long form of human
CaBP1, AF169149; short form of bovine CaBP1, AF169150; long form of
bovine CaBP1, AF169151; short form of mouse CaBP1, AF169153; long form
of mouse CaBP1, AF1691152; human CaBP2, AF169154; bovine CaBP2,
AF169155; short form of mouse CaBP2, AF169156; long form of mouse
CaBP2, AF169157; human CaBP3, AF169158; human CaBP5, AF169159;
bovine CaBP5, AF169160; mouse CaBP5, AF169161; human CaBP2 genomic
sequence, AF170811; exons 1, 2-3-4, 5, and 6 of human CaBP5 genomic
sequence, AF170812, AF170813, AF170814, and AF170815, respectively; and
exons 1-2, 3-4, 5, and 6 of human CaBP3 genomic sequence, AF170816, AF170817, AF170818, and AF170815, respectively.
Five Members of a Novel Ca2+-binding Protein (CABP)
Subfamily with Similarity to Calmodulin*
,,
,,, and**§§
Ophthalmology, ** Chemistry,
and Pharmacology and the
§ Biological Structure and BioMolecular Structure Center,
University of Washington, Seattle, Washington 98195, the ¶ Program
of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York,
New York 10021, and the Departments of Microbiology and
Immunology, Kimmel Cancer Center, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107
-helixes are extended by one -helical turn. CaBP1 and CaBP2
contain a consensus sequence for N-terminal myristoylation, similar to
members of the recoverin subfamily and are fatty acid acylated in
vitro. The patterns of expression differ for each of the various
members. Expression of CaBP5, for example, is restricted to retinal rod
and cone bipolar cells. In contrast, CaBP1 has a more widespread
pattern of expression. In the brain, CaBP1 is found in the cerebral
cortex and hippocampus, and in the retina this protein is found in cone
bipolar and amacrine cells. CaBP1 and CaBP2 are expressed as multiple,
alternatively spliced variants, and in heterologous expression systems
these forms show different patterns of subcellular localization. In reconstitution assays, CaBPs are able to substitute functionally for
CaM. These data suggest that these novel CaBPs are an important component of Ca2+-mediated cellular signal transduction in
the central nervous system where they may augment or substitute for
CaM.
*
This research was supported by National Institutes of Health
Grants EY08061 (to K. P.) and EY06935-01 (to R. N. F.), an award from Research to Prevent Blindness, Inc. to the Department of Ophthalmology at the University of Washington, Grant-in aid Award GA99001 from Fight For Sight-Prevent Blindness America Research (to
F. H.), and by the E. K. Bishop Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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