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J. Biol. Chem., Vol. 275, Issue 28, 21385-21395, July 14, 2000
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From the Department of Pathology and the Department of Molecular,
Cellular, and Developmental Biology, Yale University,
New Haven, Connecticut 06510
Four mammalian The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF233523.
Identification and Characterization of
V Spectrin, a Mammalian
Ortholog of Drosophila H
Spectrin*,
-spectrin genes are
currently recognized, all encode proteins of 
240-280,000
Mr and display 17 triple helical homologous
106-residue repeat units. In Drosophila and
Caenorhabditis elegans, a variant spectrin with unusual
properties has been recognized. Termed heavy (H),
this spectrin contains 30 spectrin repeats, has a molecular weight in
excess of 400,000, and associates with the apical domain of polarized
epithelia. We have cloned and characterized from a human retina
cDNA library a mammalian ortholog of Drosophila
H spectrin, and in accord with standard spectrin naming
conventions we term this new mammalian spectrin 5 (V). The gene
for human V spectrin (HUBSPECV) is on chromosome 15q21.
The 11,722-nucleotide cDNA of V spectrin is generated from 68 exons and is predicted to encode a protein with a molecular weight of
416,960. Like its fly counterpart, the derived amino acid sequence of
this unusual mammalian spectrin displays 30 spectrin repeats, a
modestly conserved actin-binding domain, a conserved membrane
association domain 1, a conserved self-association domain, and a
pleckstrin homology domain near its COOH terminus. Its putative ankyrin-binding domain is poorly conserved and may be inactive. These
structural features suggest that V spectrin is likely to form
heterodimers and oligomers with 
spectrin and to interact directly
with cellular membranes. Unlike its Drosophila ortholog, V spectrin does not contain an SH3 domain but displays in repeat 5 a 45-residue insertion that displays 42% identity to amino
acids 85-115 of the E4 protein of type 75 human papilloma virus. Human V spectrin is expressed at low levels in many tissues. By indirect immunofluorescence, it is detected prominently in the outer segments of
photoreceptor rods and cones and in the basolateral membrane and
cytosol of gastric epithelial cells. Unlike its Drosophila ortholog, a distinct apical distribution of V spectrin is
inapparent in the epithelial cell populations examined, although it is
confined to the outer segments of photoreceptor cells. The complete
cDNA sequence of human V spectrin is available from
GenBankTM as accession number AF233523.
*
This work was supported by grants from the National
Institutes of Health (to J. S. M.).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.
The on-line version of this article (available at
http://www.jbc.com) contains a supplementary figure.
To whom correspondence should be addressed: Dept. of Pathology,
Yale University, 310 Cedar St., New Haven, CT 06510. Tel.: 203-785-3624; Fax: 203-785-7037; E-mail: jon.morrow@yale.edu.
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