Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767937510   79 GDFICPDYYEAVCGTDGKTYDNRCALCAENAKTGSQIGVKSEGEC 123
Cdd:cd01327     1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 767937510    210 FCTRESDPVRGPDGRMHGNKCALCAEIFKQRFSEE 244
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIE 39

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

                            10        20
                    ....*....|....*....|....*....
gi 767937510    693 CTRESDPVRDADGKSYNNQCTMCKAKLER 721
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAACES 34

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 767937510    282 FCTRENDPIRGPDGKMHGNLCSMCQAYFQAENEEKKKAE 320
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHD 43

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 767937510    834 ICTRENNPVRGPYGKMHINKCAMCQSIFDREANERKKKDEE 874
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGP 45

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767937510   79 GDFICPDYYEAVCGTDGKTYDNRCALCAENAKTGSQIGVKSEGEC 123
Cdd:cd01327     1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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 767937510  1008 CPKDLKPVCGDDGQTYNNPCMLCHENLIRQTNTHIRSTGKC 1048
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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767937510    82 ICPDYYEAVCGTDGKTYDNRCALCAENAKTGSQIGVKSEGEC 123
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 767937510    210 FCTRESDPVRGPDGRMHGNKCALCAEIFKQRFSEE 244
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIE 39

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

                            10        20
                    ....*....|....*....|....*....
gi 767937510    693 CTRESDPVRDADGKSYNNQCTMCKAKLER 721
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAACES 34

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

                            10        20
                    ....*....|....*....|....*
gi 767937510    147 CTRENDPVLGPDGKTHGNKCAMCAE 171
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKA 30

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

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 767937510    282 FCTRENDPIRGPDGKMHGNLCSMCQAYFQAENEEKKKAE 320
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHD 43

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 767937510   679 CAEYREQmkngrlSCTRESDPVRDADGKSYNNQCTMCKAKLER 721
Cdd:pfam00050    1 CSDYPSG------ACPRIYDPVCGTDGKTYSNECLFCAENGKR 37

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767937510  756 GKLICTRESDPVRGPDGKTHGNKCTMCKEKLEREAAEKKKKEDE 799
Cdd:cd01327     1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGE 44

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 767937510    834 ICTRENNPVRGPYGKMHINKCAMCQSIFDREANERKKKDEE 874
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGP 45

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767937510   79 GDFICPDYYEAVCGTDGKTYDNRCALCAENAKTGSQIGVKSEGEC 123
Cdd:cd01327     1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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 767937510  1008 CPKDLKPVCGDDGQTYNNPCMLCHENLIRQTNTHIRSTGKC 1048
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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767937510    82 ICPDYYEAVCGTDGKTYDNRCALCAENAKTGSQIGVKSEGEC 123
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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 767937510 1008 CPKDLKPVCGDDGQTYNNPCMLCHENLIRQTNTHIRSTGKC 1048
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 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 767937510    80 DFICP-DYYEAVCGTDGKTYDNRCALCAENAKTGSQIG---VKSEGEC 123
Cdd:pfam07648    3 NCQCPkTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

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

                            10        20
                    ....*....|....*....|....*....
gi 767937510    617 FCTRENDPVRGPDGKTHGNKCAMCKAVFQ 645
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACE 33

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
                   ....*....|....*....|....*....|
gi 767937510   759 ICTRESDPVRGPDGKTHGNKCTMCKEKLER 788
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLFCAENGKR 37

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767937510  145 LGCTRENDPVLGPDGKTHGNKCAMCaelflkeAENAKREGETRIRRNAE 193
Cdd:cd01327     3 FGCPKDYDPVCGTDGVTYSNECLLC-------AENLKRQTNIRIKHDGE 44

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 767937510  1008 CPKD-LKPVCGDDGQTYNNPCMLCHENLIRQTNTH 1041
Cdd:pfam07648    6 CPKTeYEPVCGSDGVTYPSPCALCAAGCKLGKEVK 40

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 767937510   679 CAEYREQmkngrlSCTRESDPVRDADGKSYNNQCTMCKAKLER 721
Cdd:pfam00050    1 CSDYPSG------ACPRIYDPVCGTDGKTYSNECLFCAENGKR 37

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767937510  756 GKLICTRESDPVRGPDGKTHGNKCTMCKEKLEREAAEKKKKEDE 799
Cdd:cd01327     1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGE 44

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 767937510    834 ICTRENNPVRGPYGKMHINKCAMCQSIFDREANERKKKDEE 874
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGP 45