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 530360311    31 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTG 110
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 530360311   111 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 146
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360311  1400 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1479
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530360311  1480 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1531
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 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 530360311   1130 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 530360311   1210 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 1254
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    489 ECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 534
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 530360311    704 VCDFSCQSVPgSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 750
Cdd:smart00280    1 DCPEACPREY-DPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    619 VCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 664
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530360311   847 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 883
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    272 CPATCRGAPEgTVCGSDGADYPGECQLLRRACARQENVFKKFDGPC 317
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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 530360311 1825 ASGHPCLNGASCVPREAAYVCLCPGGFSGPHCE 1857
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        30
                  ....*....|....*....|....*....|.
gi 530360311 1555 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1585
Cdd:cd00054     8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37

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 530360311    31 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTG 110
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 530360311   111 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 146
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360311  1400 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1479
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530360311  1480 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1531
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360311  1668 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1747
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530360311  1748 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1803
Cdd:pfam00054   79 GESPLGAT---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 530360311 1870 TLAFDGRTFVEYLNavteSEKALQSNHFELSLRTEATQGLVLWSGKATeRADYVALAIVDGHLQLSYNLGSQPVVLRSTV 1949
Cdd:cd00110     1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360311 1950 PVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVV 2026
Cdd:cd00110    76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150

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 530360311 1640 FNGFSHLELRGLHTFARDlgekMALEVVFLARGPSGLLLYNGQKTdgKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPV 1719
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530360311 1720 TLGAWTRVSLERNGRKGALRVgDGPRVLgESPKSRKVPHtvLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSL 1797
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGGSAL--LNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150

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 530360311   1130 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 530360311   1210 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 1254
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120

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        40
                  ....*....|....*....|....*....|....*....|..
gi 530360311  792 ACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 833
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    489 ECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 534
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    554 VCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPC 599
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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 530360311  494 CSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 534
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        40
                  ....*....|....*....|....*....|....*....|.
gi 530360311  202 CPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPC 242
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        40
                  ....*....|....*....|....*....|....*....|....*
gi 530360311  555 CPSECvalaQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPC 599
Cdd:cd00104     1 CPKEY----DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 530360311    922 VCPMlTCPEANAtKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 969
Cdd:smart00280    1 DCPE-ACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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
                  ....*....|....*....|....*....|....*.
gi 530360311  715 SPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 750
Cdd:cd00104     6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

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        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530360311  846 PCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG---RALGPAGCE 892
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530360311    416 CDRVtCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPC 461
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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
                   ....*....|....*....|....*....|....*...
gi 530360311   705 CDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGL 742
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39

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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 530360311   349 CPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQC 389
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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 530360311   489 ECLQACS-SLYDPVCGSDGVTYGSACELEATACTLGREIQ---VARKGPC 534
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        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 530360311   618 CVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARA---GPC 664
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 530360311   202 CPSVV-APVCGSDASTYSNECELQRAQCSQQRRIR---LLSRGPC 242
Cdd:pfam07648    6 CPKTEyEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

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 530360311  284 VCGSDGADYPGECQLLRRACARQENVFKKFDGPC 317
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 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
                   ....*....|....*....|....*....|....*....|....*.
gi 530360311   927 TCPEANATKVCGSDGVTYGNECQLKTIACRQGLQIS---IQSLGPC 969
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

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 530360311 1555 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1585
Cdd:cd00054     8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37

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 530360311   272 CPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFK---KFDGPC 317
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                           10        20        30
                   ....*....|....*....|....*....|..
gi 530360311  1553 CLPNPCHGGAPCQNLEaGRFHCQCPPGRVGPT 1584
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31

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 530360311    31 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTG 110
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 530360311   111 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 146
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360311  1400 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1479
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530360311  1480 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1531
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360311  1668 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1747
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78