{PDOC50820}
{PS50820; LCCL}
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* LCCL domain profile *
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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 beta
strands and two alpha 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2001 / First entry.

[ 1] Trexler M., Banyai L., Patthy L.
     "The LCCL module."
     Eur. J. Biochem. 267:5751-5757(2000).
     PubMed=10971586
[ 2] Robertson 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.
     "Mutations in a novel cochlear gene cause DFNA9, a human nonsyndromic
     deafness with vestibular dysfunction."
     Nat. Genet. 20:299-303(1998).
     PubMed=9806553; DOI=10.1038/3118
[ 3] Kaplan F., Ledoux P., Kassamali F.Q., Gagnon S., Post M., Koehler D.,
     Deimling J., Sweezey N.B.
     "A novel developmentally regulated gene in lung mesenchyme: homology
     to a tumor-derived trypsin inhibitor."
     Am. J. Physiol. 276:L1027-L1036(1999).
     PubMed=10362728
[E1] https://web.expasy.org/spotlight/back_issues/004/

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