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词条 LCCL domain
释义

  1. References

{{Infobox protein family
| Symbol = LCCL
| Name = LCCL
| image =
| width =
| caption =
| Pfam = PF03815
| Pfam_clan = CL0513
| InterPro = IPR004043
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1jbi
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}

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, Coch-5b2 (Cochlin) 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, 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] Secondary structure prediction suggests that the LCCL domain contains six beta strands and two alpha helices.[1]

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.[3]

References

1. ^{{cite journal |vauthors=Trexler M, Banyai L, Patthy L | title = The LCCL module | journal = Eur. J. Biochem. | volume = 267 | issue = 18 | pages = 5751–7 |date=September 2000 | pmid = 10971586 | doi = 10.1046/j.1432-1327.2000.01641.x| url = }}
2. ^{{cite journal |vauthors=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 | title = Mutations in a novel cochlear gene cause DFNA9, a human nonsyndromic deafness with vestibular dysfunction | journal = Nat. Genet. | volume = 20 | issue = 3 | pages = 299–303 |date=November 1998 | pmid = 9806553 | doi = 10.1038/3118 | url = }}
3. ^{{cite journal |vauthors=Kaplan F, Ledoux P, Kassamali FQ, Gagnon S, Post M, Koehler D, Deimling J, Sweezey NB | title = A novel developmentally regulated gene in lung mesenchyme: homology to a tumor-derived trypsin inhibitor | journal = Am. J. Physiol. | volume = 276 | issue = 6 Pt 1 | pages = L1027-36 |date=June 1999 | pmid = 10362728 | doi = | url = }}
{{InterPro content|IPR004043}}

1 : Protein domains

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