LCCL domain explained

Symbol:LCCL
LCCL
Pfam:PF03815
Pfam Clan:CL0513
Interpro:IPR004043
Scop:1jbi
Cath:1jbi

In molecular biology, the LCCL domain is a protein domain which has been named after several well-characterised proteins that were found to contain it, namely Limulus clotting factor C, Cochlin (Coch-5b2) and Lgl1 (CRISPLD2). 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, von Willebrand type A domains, CUB domains, discoidin lectin domains or CAP domains. It has been proposed that the LCCL domain could be involved in lipopolysaccharide (LPS) binding.[1] [2] LCCL exhibits a novel fold.[3]

Some proteins known to contain a LCCL domain include Limulus factor C, an 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); and mammalian late gestation lung protein Lgl1, contains two tandem copies of the LCCL domain.[4]

Notes and References

  1. Trexler M, Banyai L, Patthy L . The LCCL module . Eur. J. Biochem. . 267 . 18 . 5751–7 . September 2000 . 10971586 . 10.1046/j.1432-1327.2000.01641.x. free .
  2. Robertson NG, Lu L, Heller S, Merchant SN, Eavey RD, McKenna M, Nadol JB, Miyamoto RT, Linthicum FH, Lubianca Neto JF, Hudspeth AJ, Seidman CE, Morton CC, Seidman JG . Mutations in a novel cochlear gene cause DFNA9, a human nonsyndromic deafness with vestibular dysfunction . Nat. Genet. . 20 . 3 . 299–303 . November 1998 . 9806553 . 10.1038/3118 . 16350815 .
  3. Liepinsh . E . Trexler . M . Kaikkonen . A . Weigelt . J . Bányai . L . Patthy . L . Otting . G . NMR structure of the LCCL domain and implications for DFNA9 deafness disorder. . The EMBO Journal . 1 October 2001 . 20 . 19 . 5347–53 . 10.1093/emboj/20.19.5347 . 11574466. 125649 .
  4. Kaplan F, Ledoux P, Kassamali FQ, Gagnon S, Post M, Koehler D, Deimling J, Sweezey NB . A novel developmentally regulated gene in lung mesenchyme: homology to a tumor-derived trypsin inhibitor . Am. J. Physiol. . 276 . 6 Pt 1 . L1027-36 . June 1999 . 10362728 . 10.1152/ajplung.1999.276.6.L1027.