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- ************************************
- * Clathrin light chains signatures *
- ************************************
-
- Clathrin [1,2] is the major coat-forming protein that encloses vesicles such
- as coated pits and forms cell surface patches involved in membrane traffic
- within eukaryotic cells. The clathrin coats (called triskelions) are composed
- of three heavy chains (180 Kd) and three light chains (23 to 27 Kd).
-
- The clathrin light chains [3], which may help to properly orient the assembly
- and disassembly of the clathrin coats, bind non-covalently to the heavy chain,
- they also bind calcium and interact with the hsc70 uncoating ATPase.
-
- - In higher eukaryotes two genes code for distinct but related light chains:
- LC(a) and LC(b). Each of the two genes can yield, by tissue-specific
- alternative splicing, two separate forms which differ by the insertion of a
- sequence of respectively thirty or eighteen residues. There is, in the N-
- terminal part of the clathrin light chains a domain of twenty one amino
- acid residues which is perfectly conserved in LC(a) and LC(b).
- - In yeast there is a single light chain (gene CLC1) whose sequence is only
- distantly related to that of higher eukaryotes.
-
- We developed two signature patterns for clathrin light chains. The first
- pattern is a heptapeptide from the center of the conserved N-terminal region
- of eukaryotic light chains; the second pattern is derived from a positively
- charged region located in the C-terminal extremity of all known clathrin light
- chains.
-
- -Consensus pattern: F-L-A-Q-Q-E-S
- -Sequences known to belong to this class detected by the pattern: ALL higher
- eukaryotes light chains.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [KR]-D-x-S-[KR]-[LIVM]-[KR]-x-[LIVM](3)-x-L-K
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: December 1991 / Patterns and text revised.
-
- [ 1] Keen J.H.
- Annu. Rev. Biochem. 59:415-438(1990).
- [ 2] Brodsky F.M.
- Science 242:1396-1402(1988).
- [ 3] Brodsky F.M., Hill B.L., Acton S.L., Naethke I., Wong D.H.,
- Ponnambalam S., Parham P.
- Trends Biochem. Sci. 16:208-213(1991).
-