Coiled coil region of thrombospondin in protostomes; This family contains the N-terminal coiled coil region of thrombospondin (TSP) in some protostomes, which suggest ancient functions that include bridging activities in cell-cell and cell-ECM interactions. It appears that most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil. This region has heparin-binding activity and is a component of extracellular matrix (ECM), showing that the pentameric TSPs are of earlier origin and that the trimeric TSP subfamily A form is associated with higher chordates. The left-handed coiled coil pentamer forms a channel that is a unique carrier for lipophilic compounds, and is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. Several heparan sulphate (HS) proteoglycans are known in D. melanogaster, including both transmembrane and matrix forms, which could contribute to its retention in pericellular matrix.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 22945792 245 EDALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGC 286
Cdd:cd16081   1 DELLAKTLNELIEAIKKLREEVERNRQETRYLRELIENCAAC 42

Coiled coil region of thrombospondin in protostomes; This family contains the N-terminal coiled coil region of thrombospondin (TSP) in some protostomes, which suggest ancient functions that include bridging activities in cell-cell and cell-ECM interactions. It appears that most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil. This region has heparin-binding activity and is a component of extracellular matrix (ECM), showing that the pentameric TSPs are of earlier origin and that the trimeric TSP subfamily A form is associated with higher chordates. The left-handed coiled coil pentamer forms a channel that is a unique carrier for lipophilic compounds, and is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. Several heparan sulphate (HS) proteoglycans are known in D. melanogaster, including both transmembrane and matrix forms, which could contribute to its retention in pericellular matrix.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 22945792 245 EDALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGC 286
Cdd:cd16081   1 DELLAKTLNELIEAIKKLREEVERNRQETRYLRELIENCAAC 42

Giardia variant-specific surface protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22945792   281 ENCAGCKNPLTTDNQlriepDCRSANPCYPGVECLDSaagprCGHCPLGFIG----DGKSCKPgvtcahhmCYPGvQCHD 356
Cdd:pfam03302  26 ENCKACSNDKREVCE-----ECNSNNYLTPTSQCIDD-----CAKIGNYYYTtnanNKKICKE--------CTVA-NCKT 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22945792   357 TVNGAQCDSCPAGYEGDGRTCSlrnPClDTPCPSGN 392
Cdd:pfam03302  87 CEDQGQCQACNDGFYKSGDACS---PC-HESCKTCS 118

Coiled coil region of thrombospondin in protostomes; This family contains the N-terminal coiled coil region of thrombospondin (TSP) in some protostomes, which suggest ancient functions that include bridging activities in cell-cell and cell-ECM interactions. It appears that most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil. This region has heparin-binding activity and is a component of extracellular matrix (ECM), showing that the pentameric TSPs are of earlier origin and that the trimeric TSP subfamily A form is associated with higher chordates. The left-handed coiled coil pentamer forms a channel that is a unique carrier for lipophilic compounds, and is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. Several heparan sulphate (HS) proteoglycans are known in D. melanogaster, including both transmembrane and matrix forms, which could contribute to its retention in pericellular matrix.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 22945792 245 EDALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGC 286
Cdd:cd16081   1 DELLAKTLNELIEAIKKLREEVERNRQETRYLRELIENCAAC 42

Coiled coil region of thrombospondin; This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 22945792 247 ALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGC 286
Cdd:cd16076   1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40