Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    747 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 826
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    827 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 906
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6755781    907 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 944
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6755781  221 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 264
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6755781    694 EDSNNDGVGDICEADFDQDQVIDHIDVCPENAEIT 728
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6755781  381 DVDECQ-NGACVLNSICINTLGSYRCGpCKPGYTGD 415
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781   466 DVDIDSYPDEElpcSARNCKKDNCKYVPNSGQEDADRDGIGDAcDEDADGDGILNEQDNCVLTHNIDQ-RNSDKDIFGDA 544
Cdd:NF033609 631 ASDSDSASDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDS 706

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781   545 CDNCRMVLNNDQ-KDTDGDGRGDACDDDMDGDGIKNILDNCPRVPNRDQQDRDGDDVGDAcDSCPDVSNPNQSDVDNDLV 623
Cdd:NF033609 707 DSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD 785

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755781   624 GDScDTNQDSDGDGHQDSTDNCPTVINS---SQLDTDKDGIGDECDDDDDNDGIPDLVPPGPDNCRLVPNPAQEDSNND 699
Cdd:NF033609 786 SDS-DSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    747 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 826
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    827 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 906
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6755781    907 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 944
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6755781  221 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 264
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6755781    498 EDADRDGIGDACDEDADGDGILNEQDNCVLTHNIDQ 533
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 6755781    617 DVDNDLVGDSCDtnQDSDGDGHQDSTDNCPTVINSSQ 653
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6755781  328 DVDECK-YHPCYPGVRCVNLAPGFRCDaCPVGFTGP 362
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 6755781     328 DVDECK-YHPCYPGVRCVNLAPGFRCDaCPVGFT 360
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCE-CPPGYT 33

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781   466 DVDIDSYPDEElpcSARNCKKDNCKYVPNSGQEDADRDGIGDAcDEDADGDGILNEQDNCVLTHNIDQ-RNSDKDIFGDA 544
Cdd:NF033609 631 ASDSDSASDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDS 706

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781   545 CDNCRMVLNNDQ-KDTDGDGRGDACDDDMDGDGIKNILDNCPRVPNRDQQDRDGDDVGDAcDSCPDVSNPNQSDVDNDLV 623
Cdd:NF033609 707 DSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD 785

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755781   624 GDScDTNQDSDGDGHQDSTDNCPTVINS---SQLDTDKDGIGDECDDDDDNDGIPDLVPPGPDNCRLVPNPAQEDSNND 699
Cdd:NF033609 786 SDS-DSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    747 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 826
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755781    827 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 906
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6755781    907 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 944
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6755781  221 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 264
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

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 6755781  224 QFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQAC 263
Cdd:cd16076   1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6755781    498 EDADRDGIGDACDEDADGDGILNEQDNCVLTHNIDQ 533
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6755781    694 EDSNNDGVGDICEADFDQDQVIDHIDVCPENAEIT 728
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6755781  381 DVDECQ-NGACVLNSICINTLGSYRCGpCKPGYTGD 415
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 6755781     381 DVDECQ-NGACVLNSICINTLGSYRCGpCKPGYTGDQT 417
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCE-CPPGYTDGRN 37

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 6755781    381 DVDECQNGA--CVLNSICINTLGSYRCgPCKPG 411
Cdd:pfam07645   1 DVDECATGThnCPANTVCVNTIGSFEC-RCPDG 32

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6755781  379 CTDVDECQNGAcvlnsICINTLGSYRCGpCKPGYTGDQT 417
Cdd:cd00053   2 CAASNPCSNGG-----TCVNTPGSYRCV-CPPGYTGDRS 34