{PDOC00298} {PS00341; SURFACT_PALMITOYL} {BEGIN} *************************************************************** * Surfactant associated polypeptide SP-C palmitoylation sites * *************************************************************** Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines [1]. -Consensus pattern: I-P-C-C-P-V [The 2 C's are palmitoylated] -Sequences known to belong to this class detected by the pattern: ALL, except for dog SP-C, in which the second Cys is replaced by Phe [2]. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: May 2004 / Text revised. [ 1] Curstedt T., Johansson J., Persson P., Eklund A., Robertson B., Lowenadler B., Jornvall H. "Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups." Proc. Natl. Acad. Sci. U.S.A. 87:2985-2989(1990). PubMed=2326260 [ 2] Johansson J., Persson P., Lowenadler B., Robertson B., Jornvall H., Curstedt T. "Canine hydrophobic surfactant polypeptide SP-C. A lipopeptide with one thioester-linked palmitoyl group." FEBS Lett. 281:119-122(1991). PubMed=2015882 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}