Biology:LCCL domain

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LCCL
Protein COCH PDB 1jbi.png
LCCL domain in human Cochlin (PDB: 1jbi​)
Identifiers
SymbolLCCL
PfamPF03815
Pfam clanCL0513
InterProIPR004043
CATH1jbi
SCOP21jbi / SCOPe / SUPFAM

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]

References

  1. "The LCCL module". Eur. J. Biochem. 267 (18): 5751–7. September 2000. doi:10.1046/j.1432-1327.2000.01641.x. PMID 10971586. 
  2. "Mutations in a novel cochlear gene cause DFNA9, a human nonsyndromic deafness with vestibular dysfunction". Nat. Genet. 20 (3): 299–303. November 1998. doi:10.1038/3118. PMID 9806553. 
  3. Liepinsh, E; Trexler, M; Kaikkonen, A; Weigelt, J; Bányai, L; Patthy, L; Otting, G (1 October 2001). "NMR structure of the LCCL domain and implications for DFNA9 deafness disorder.". The EMBO Journal 20 (19): 5347–53. doi:10.1093/emboj/20.19.5347. PMID 11574466. 
  4. "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. doi:10.1152/ajplung.1999.276.6.L1027. PMID 10362728. 
This article incorporates text from the public domain Pfam and InterPro: IPR004043