Mj. Runswick et al., EXTENSION OF THE MITOCHONDRIAL TRANSPORTER SUPER-FAMILY - SEQUENCES OF 5 MEMBERS FROM THE NEMATODE WORM, CAENORHABDITIS-ELEGANS, DNA sequence, 4(5), 1994, pp. 281-291
The sequences are presented of cDNAs encoding five related proteins fr
om the nematode worm, Caenorhabditis elegans. Three of them can be rec
ognised as the homologues of the ADP/ATP, phosphate and oxoglutarate/m
alate carrier proteins that have been found in the inner membranes of
mitochondria in other species. These carrier proteins, and the uncoupl
ing protein from the mitochondria in mammalian brown adipose tissue, h
ave common features in their primary and secondary structures, and are
members of the same protein super-family. Members of this super-famil
y have polypeptide chains approximately 300 amino acid long that consi
st of three tandem related sequences of about 100 amino acids. The tan
dem repeats from the different proteins are inter-related, and each re
peat is probably folded into a common secondary structural motif consi
sting of two hydrophobic stretches of amino acids with the potential t
o form membrane spanning alpha-helices, linked by an extensive hydroph
ilic region. The common characteristic features of this family of prot
eins are also present in sequences of two further proteins, named C1 a
nd C2, encoded in nematode cDNAs, and in tour published protein sequen
ces from various sources. Neither the transport properties nor the sub
cellular locations of any of this latter group of six proteins are kno
wn. Therefore, currently the super-family of mitochondrial carrier pro
teins has at least ten different members.