| Literature References | 1. SHIN, D.H., HWANG, K.Y., KIM, K.K., LIM, S., SWEET, R.S. AND SUH, S.W.
Crystallisation and preliminary X-ray crystallographic analysis of
phospholipid transfer protein from maize seedlings.
PROTEINS 19 80-83 (1994).
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| Documentation | Phospholipid transfer proteins (PLTPs) transfer phospholipids, glycolipids,
fatty acids and sterols from liposomes or microsomes to mitochondria [1].
PLTPs exist in animal and plant tissues, including rat liver cytosol,
potato tuber, castor bean, maize seedlings, spinach, barley and wheat.
While there is no sequence similarity between animal and plant PTLPs,
similarity between the plant proteins is high. The sequences contain 8
cysteines, which form 4 disulphide bridges. Plant PTLPs are also similar
to alpha-amylase inhibitor I2 from the seeds of ragi, Indian finger millet
and amylase/protease inhibitors from rice and barley.
LIPIDTRNSFER is a 5-element fingerprint that provides a signature for
plant phospholipid transfer proteins. The fingerprint was derived from
an initial alignment of 7 sequences: the motifs were drawn from short
conserved regions along the full alignment length, motifs 4 and 5
spanning the region encoded by PROSITE pattern PLANT_LTP (PS00597),
which contains 2 C-terminal Cys residues involved in disulphide bond
formation. Two iterations on OWL26.0 were required to reach convergence,
at which point a true set comprising 32 sequences was identified. Several
partial matches were also found, most of which are N-terminal fragments,
or sequences failing to make significant matches with motif 4.
An update on SPTR37_9f identified a true set of 65 sequences, and 11
partial matches.
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