Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250   33 CPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVATG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2043849250  113 DTRIFFVNPAPQalwpahrNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1941 IKTEATQGLLLWSGKGLQRsDYIALAIVDGHVQLSYDLGSKGVTLRSSVPVNTNQWVRIRASRVQREGSLQVGNEAPIAG 2020
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2043849250 2021 SSPLGATQ-LDTDGALWLGGLDKPSVPQRlPKAFSTGFVGCMRDVLVDRRELH 2072
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250  1153 ATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESALDELFRGSEVRRDFRSVRVRDLGQSSAVRVIVEAHFD 1232
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2043849250  1233 PATsyTAADIQGALLKQLRAARRkTILVKKpqQEHIKFMDFDW 1275
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAY-SLKITN--VNVVDVLDPDS 118

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2043849250   564 VCPTECVPSAQPVCGSDGNTYGSECELHVRACTQQENILVAAQGPC 609
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2043849250   713 VCDFTCAAAPRaPVCGSDGVTYANECQLKKTRCEKRQELFVTSQGAC 759
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2043849250   211 CAPVVAPVCGSDHSTYSNECELDRAQCNQQRRIKVVSKGPC 251
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2043849250   930 ECPSPlCPEgNATKVCGSDGVTYGDQCQLRTIACRQGQHITVKHVGQC 977
Cdd:smart00280    1 DCPEA-CPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2043849250   355 PEDCPPGSGPVCGDDGVTYESECAMGRAGAIRGIDIQKVRSGQC 398
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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 2043849250 1865 QEPNPCQPGGTCQPSMAGYQCSCHAGFAGARCE 1897
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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
                   ....*....|....*....|....*...
gi 2043849250 1381 CRHGGTCRDDGHGFTCSCPAGTAGTTCE 1408
Cdd:cd00054     11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250   33 CPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVATG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2043849250  113 DTRIFFVNPAPQalwpahrNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1941 IKTEATQGLLLWSGKGLQRsDYIALAIVDGHVQLSYDLGSKGVTLRSSVPVNTNQWVRIRASRVQREGSLQVGNEAPIAG 2020
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2043849250 2021 SSPLGATQ-LDTDGALWLGGLDKPSVPQRlPKAFSTGFVGCMRDVLVDRRELH 2072
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1711 ARRPRGLILYNGQRSDGggDFVSLALHGGHLEFRFDLGKGPALLRSREPVPLDTWVSVRLERSGRKGVLRVNGGPAVTGE 1790
Cdd:pfam00054    3 TTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2043849250 1791 SPKSRKvphMVLNLKEPLYLGGAPDFSRLARAAAVSSGFEGALQKVLVDGVPVL 1844
Cdd:pfam00054   81 SPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1910 AVAFDGRTYLEFhnavTRSEKALQSNHFELSIKTEATQGLLLWSGkGLQRSDYIALAIVDGHVQLSYDLGSKGVTLRSSV 1989
Cdd:cd00110      1 GVSFSGSSYVRL----PTLPAPRTRLSISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043849250 1990 PVNTNQWVRIRASRVQREGSLQVGNEAPIAGSSPLGATQLDTDGALWLGGLdkPSVPQRLPKAFSTGFVGCMRDVLVD 2067
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGL--PEDLKSPGLPVSPGFVGCIRDLKVN 151

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1681 FSGSSYLELPGLQSFvpglPDRMSLDLVLLARRPRGLILYNGqrSDGGGDFVSLALHGGHLEFRFDLGKGPALLRSREPV 1760
Cdd:cd00110      4 FSGSSYVRLPTLPAP----RTRLSISFSFRTTSPNGLLLYAG--SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043849250 1761 PLDTWVSVRLERSGRKGVLRVNGGPAVTGESPKSrkvpHMVLNLKEPLYLGGAPDFSRLaRAAAVSSGFEGALQKVLVD 1839
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGG----SALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKVN 151

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250  1153 ATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESALDELFRGSEVRRDFRSVRVRDLGQSSAVRVIVEAHFD 1232
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2043849250  1233 PATsyTAADIQGALLKQLRAARRkTILVKKpqQEHIKFMDFDW 1275
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAY-SLKITN--VNVVDVLDPDS 118

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1171 LFYTPEMADPKSELFGETARSIESALDELFRGSEVRRDFRSVRVRDLGQSS-AVRVIVEAHFDPATSYTAADIQGALLKQ 1249
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGgSVVVDVVLVFRFPSTEPALDREKLIEEI 91

                   ....*...
gi 2043849250 1250 LRAARRKT 1257
Cdd:pfam01390   92 LRQTLNNT 99

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2043849250   564 VCPTECVPSAQPVCGSDGNTYGSECELHVRACTQQENILVAAQGPC 609
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2043849250   499 ECQQQCQGRYDPVCGTDQRTYGSPCELHAMACLLQRDIGLRHRGPC 544
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 2043849250   630 CPRCERQPPAPVCGSDGVTYPSPCQLQVASCQLQKSIQVARTGPC 674
Cdd:smart00280    2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2043849250   211 CAPVVAPVCGSDHSTYSNECELDRAQCNQQRRIKVVSKGPC 251
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2043849250  630 CPRCERqppaPVCGSDGVTYPSPCQLQVASCQLQKSIQVARTGPC 674
Cdd:cd00104      1 CPKEYD----PVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2043849250   280 VCPSSCGGVaESPVCGSDGRDYRSLCHLQKHACDAQQDLAKQFDGPC 326
Cdd:smart00280    1 DCPEACPRE-YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2043849250  430 CDGAFRPLCGGDGRTYGSDCQRRRAECLRQAGIAVRHRGPC 470
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2043849250  725 PVCGSDGVTYANECQLKKTRCEKRQELFVTSQGAC 759
Cdd:cd00104      7 PVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2043849250  936 CPEgNATKVCGSDGVTYGDQCQLRTIACRQGQHITVKHVGQC 977
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2043849250  281 CPSSCggvaeSPVCGSDGRDYRSLCHLQKHACDAQQDLAKQFDGPC 326
Cdd:cd00104      1 CPKEY-----DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2043849250  628 CLCPRCErqpPAPVCGSDGVTYPSPCQLQVASCQLQKSIQVART---GPC 674
Cdd:pfam07648    4 CQCPKTE---YEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2043849250  854 PCGCDPVGSVRDDCEQMSGLCSCRPGISGMKCSRCPAG 891
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38

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 2043849250 1865 QEPNPCQPGGTCQPSMAGYQCSCHAGFAGARCE 1897
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2043849250  499 ECQQQCQG-RYDPVCGTDQRTYGSPCELHAMACLLQRDIG---LRHRGPC 544
Cdd:pfam07648    1 NCNCQCPKtEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2043849250  281 CPSSCGGVAESPVCGSDGRDYRSLCHLQKHACDAQQDLAKQF---DGPC 326
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKvkyDGSC 50

EBNA-3B; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2043849250 1292 AAPGSARRVPAATAALGQPVGSPGQPVGTAGTAGHPGHPVGTVGSPGEPVGTTGTARSPAGTAGSSRGAPP 1362
Cdd:PHA03378   709 APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPP 779

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2043849250  936 CPEGNATKVCGSDGVTYGDQCQLRTIACRQG---QHITVKHVGQC 977
Cdd:pfam07648    6 CPKTEYEPVCGSDGVTYPSPCALCAAGCKLGkevKEEKVKYDGSC 50

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2043849250  562 RCVCPTecvPSAQPVCGSDGNTYGSECELHVRACTQQENI 601
Cdd:pfam07648    3 NCQCPK---TEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39

Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250   33 CPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVATG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2043849250  113 DTRIFFVNPAPQalwpahrNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1941 IKTEATQGLLLWSGKGLQRsDYIALAIVDGHVQLSYDLGSKGVTLRSSVPVNTNQWVRIRASRVQREGSLQVGNEAPIAG 2020
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2043849250 2021 SSPLGATQ-LDTDGALWLGGLDKPSVPQRlPKAFSTGFVGCMRDVLVDRRELH 2072
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043849250 1711 ARRPRGLILYNGQRSDGggDFVSLALHGGHLEFRFDLGKGPALLRSREPVPLDTWVSVRLERSGRKGVLRVNGGPAVTGE 1790
Cdd:pfam00054    3 TTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2043849250 1791 SPKSRKvphMVLNLKEPLYLGGAPDFSRLARAAAVSSGFEGALQKVLVDGVPVL 1844
Cdd:pfam00054   81 SPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131