CLONING OF 5 HUMAN CADHERINS CLARIFIES CHARACTERISTIC FEATURES OF CADHERIN EXTRACELLULAR DOMAIN AND PROVIDES FURTHER EVIDENCE FOR 2 STRUCTURALLY DIFFERENT TYPES OF CADHERIN
H. Tanihara et al., CLONING OF 5 HUMAN CADHERINS CLARIFIES CHARACTERISTIC FEATURES OF CADHERIN EXTRACELLULAR DOMAIN AND PROVIDES FURTHER EVIDENCE FOR 2 STRUCTURALLY DIFFERENT TYPES OF CADHERIN, Cell adhesion and communication, 2(1), 1994, pp. 15-26
The entire coding sequences for five possible human cadherins, named c
adherin-4, -8, -11, -12 and -13, were determined. The deduced amino ac
id sequences of cadherin-4 and cadherin-13 showed high homology with t
hose of chicken R-cadherin or chicken T-cadherin, suggesting that cadh
erin-4 and cadherin-13 are mammalian homologues of the chicken R-cadhe
rin or T-cadherin. Comparison of the extracellular domain of these pro
teins with those of other cadherins and cadherin-related proteins clar
ifies characteristic structural features of this domain. The domain is
subdivided into five subdomains, each of which contains a cadherin-sp
ecific motif characterized by well-conserved amino acid residues and s
hort amino acid sequences. Moreover, each subdomain has unique feature
s of its own. The comparison also provides additional evidence for two
structurally different types of cadherins: the first type includes B-
, E-, EP-, M, N-, P- and R-cadherins and cadherin-4; the second type i
ncludes cadherin-5 through cadherin-12. Cadherin-13 lacks the sequence
corresponding to the cytoplasmic domain of typical cadherins, but the
extracellular domain shares most of the features common to the extrac
ellular domain of cadherins, especially those of the first type of cad
herins, suggesting that cadherin-13 is a special type of cadherin. The
se results, and those of other recent cloning studies, indicate that m
any cadherins with different properties are expressed in various tissu
es of different organisms.