{PDOC51236}
{PS51236; TSP_CTER}
{BEGIN}
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* Thrombospondin C-terminal domain profile *
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Thrombospondins are multimeric multidomain glycoproteins that function at cell
surfaces  and  in  the  extracellular matrix milieu. They act as regulators of
cell interactions in vertebrates. They are divided into two subfamilies, A and
B,  according to their overall molecular organization. The subgroup A proteins
TSP-1  and  -2  contain an N-terminal domain, a VWFC domain (see <PDOC00928>),
three TSP1 repeats (see<PDOC50092>), three EGF-like domains (see <PDOC00021>),
TSP3  repeats (see <PDOC51234>) and a C-terminal domain. They are assembled as
trimer. The subgroup B thrombospondins designated TSP-3 -4 and COMP (cartilage
oligomeric  matrix  protein,  also designated TSP-5) are distinct in that they
contain  unique  N-terminal  regions,  lack  the VWFC domain and TSP1 repeats,
contain  four  copies of EGF-like domains, and are assembled as pentamers [1].
EGF,  TSP3  repeats  and  the  C-terminal  domain  are  thus the hallmark of a
thrombospondin.

The  globular  C-terminal domain is a beta sandwich of two curved antiparallel
beta-sheets (see <PDB:1UX6>) [2]. The fold is an elaboration of the jelly role
topology,  with strand B3-B7, B11 and B14-B15 forming the eight-stranded jelly
roll motif. The function of the C-terminal domain is not yet known.

The profile we developed covers the entire thrombospondin C-terminal domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: March 2007 / First entry.

[ 1] Adams J.C.
     "Thrombospondins: multifunctional regulators of cell interactions."
     Annu. Rev. Cell Dev. Biol. 17:25-51(2001).
     PubMed=11687483; DOI=10.1146/annurev.cellbio.17.1.25
[ 2] Kvansakul M., Adams J.C., Hohenester E.
     "Structure of a thrombospondin C-terminal fragment reveals a novel
     calcium core in the type 3 repeats."
     EMBO J. 23:1223-1233(2004).
     PubMed=15014436; DOI=10.1038/sj.emboj.7600166

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