PROSITE documentation PDOC50820
LCCL domain profile


The LCCL domain has been named after the best characterized proteins that were found to contain it, namely Limulus factor C, Coch-5b2 and Lgl1. It is an about 100 amino acids domain whose C-terminal part contains a highly conserved histidine in a conserved motif YxxxSxxCxAAVHxGVI. The LCCL module is thought to be an autonomously folding domain that has been used for the construction of various modular proteins through exon-shuffling. It has been found in various metazoan proteins in association with complement B-type domains, C-type lectin domains (see <PDOC00537>), von Willebrand type A domains (see <PDOC50234>), CUB domains (see <PDOC00908>), discoidin lectin domains or CAP domains. It has been proposed that the LCCL domain could be involved in lipopolysaccharide (LPS) binding [1,2,E1].

Secondary structure prediction suggests that the LCCL domain contains six β strands and two α helices [1].

Some proteins known to contain a LCCL domain are listed below:

  • Limulus factor C, a LPS endotoxin-sensitive trypsin type serine protease, which serves to protect the organism from bacterial infection.
  • Vertebrate cochlear protein cochlin or coch-5b2. Cochlin is probably a secreted protein. Mutations affecting the LCCL domain of coch-5b2 cause the deafness disorder DFNA9 in humans.
  • Mammalian late gestation lung protein Lgl1, contains two tandem copies of the LCCL domain [3].

The profile we have developed covers the entire LCCL domain.

Last update:

December 2001 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LCCL, PS50820; LCCL domain profile  (MATRIX)


1AuthorsTrexler M. Banyai L. Patthy L.
TitleThe LCCL module.
SourceEur. J. Biochem. 267:5751-5757(2000).
PubMed ID10971586

2AuthorsRobertson N.G. Lu L. Heller S. Merchant S.N. Eavey R.D. McKenna M. Nadol J.B. Jr. Miyamoto R.T. Linthicum F.H. Jr. Lubianca Neto J.F. Hudspeth A.J. Seidman C.E. Morton C.C. Seidman J.G.
TitleMutations in a novel cochlear gene cause DFNA9, a human nonsyndromic deafness with vestibular dysfunction.
SourceNat. Genet. 20:299-303(1998).
PubMed ID9806553

3AuthorsKaplan F. Ledoux P. Kassamali F.Q. Gagnon S. Post M. Koehler D. Deimling J. Sweezey N.B.
TitleA novel developmentally regulated gene in lung mesenchyme: homology to a tumor-derived trypsin inhibitor.
SourceAm. J. Physiol. 276:L1027-L1036(1999).
PubMed ID10362728


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