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Conserved domains on  [gi|75127280|sp|Q6PQG3|]
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RecName: Full=Extracellular protease inhibitor 10; AltName: Full=Secreted effector EPI10; Flags: Precursor

Protein Classification

Kazal-type serine protease inhibitor family protein( domain architecture ID 10645127)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor; similar to follistatin-related protein 3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 25-70 3.35e-11

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.53  E-value: 3.35e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 75127280     25 NCSFGCLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:smart00280   1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 167-208 7.12e-10

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.


:

Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 52.66  E-value: 7.12e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 75127280 167 CPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRS-GRSITVAHNGPC 41
KAZAL_FS super family cl00097
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 96-127 1.02e-03

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.


The actual alignment was detected with superfamily member smart00280:

Pssm-ID: 412159  Cd Length: 46  Bit Score: 36.12  E-value: 1.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 75127280     96 CPDMCLDVYDPVSDENGKEYSNQCYMEMAKCK 127
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACE 33
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 25-70 3.35e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.53  E-value: 3.35e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 75127280     25 NCSFGCLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:smart00280   1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 30-70 3.88e-10

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.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 53.43  E-value: 3.88e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 75127280  30 CLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 167-208 7.12e-10

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.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 52.66  E-value: 7.12e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 75127280 167 CPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRS-GRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 164-208 3.76e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 48.06  E-value: 3.76e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 75127280    164 DMLCPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:smart00280   3 PEACPREYDPVCGSDGVTYSNECHLCKAACES-GKSIEVKHDGPC 46
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 25-70 7.83e-06

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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 7.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 75127280    25 NCSFGC-LDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAG---DGEC 70
Cdd:pfam07648   1 NCNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKvkyDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 164-186 2.41e-04

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.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 37.65  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|...
gi 75127280   164 DMLCPDNYAPVCGSDGETYPNEC 186
Cdd:pfam00050   6 SGACPRIYDPVCGTDGKTYSNEC 28
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 96-127 1.02e-03

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 36.12  E-value: 1.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 75127280     96 CPDMCLDVYDPVSDENGKEYSNQCYMEMAKCK 127
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACE 33
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 25-70 3.35e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.53  E-value: 3.35e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 75127280     25 NCSFGCLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:smart00280   1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 30-70 3.88e-10

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.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 53.43  E-value: 3.88e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 75127280  30 CLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 167-208 7.12e-10

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.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 52.66  E-value: 7.12e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 75127280 167 CPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:cd00104   1 CPKEYDPVCGSDGKTYSNECHLGCAACRS-GRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 164-208 3.76e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 48.06  E-value: 3.76e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 75127280    164 DMLCPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:smart00280   3 PEACPREYDPVCGSDGVTYSNECHLCKAACES-GKSIEVKHDGPC 46
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 163-208 3.07e-06

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.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 43.04  E-value: 3.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 75127280 163 GDMLCPDNYAPVCGSDGETYPNECDLGITSCNHpEQNITMVGEGPC 208
Cdd:cd01327   1 EVFGCPKDYDPVCGTDGVTYSNECLLCAENLKR-QTNIRIKHDGEC 45
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 28-70 6.26e-06

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.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 41.89  E-value: 6.26e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 75127280  28 FGCLDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:cd01327   3 FGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 25-70 7.83e-06

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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 7.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 75127280    25 NCSFGC-LDVYKPVCGSNGETYSNSCYLRLASCKSNNGITEAG---DGEC 70
Cdd:pfam07648   1 NCNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKvkyDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 164-186 2.41e-04

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.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 37.65  E-value: 2.41e-04
                          10        20
                  ....*....|....*....|...
gi 75127280   164 DMLCPDNYAPVCGSDGETYPNEC 186
Cdd:pfam00050   6 SGACPRIYDPVCGTDGKTYSNEC 28
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 34-70 3.15e-04

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.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 37.26  E-value: 3.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 75127280    34 YKPVCGSNGETYSNSCYLRLASCKSNNGITEAGDGEC 70
Cdd:pfam00050  13 YDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
MFS_SLCO5_OATP5 cd17404
Solute carrier organic anion transporter 5 family of the Major Facilitator Superfamily of ...
 26-100 4.27e-04

Solute carrier organic anion transporter 5 family of the Major Facilitator Superfamily of transporters; The Solute carrier organic anion transporter 5 (SLCO5) or Organic anion transporting polypeptide 5 (OATP5) family contains only one subfamily, OATP5A, which contains only one mammalian member OATP5A1 (encoded by SLCO5A1). Deletion of the SLCO5A1 gene has been implicated in the pathogenesis of Mesomelia-synostoses syndrome (MSS), a rare autosomal-dominant disorder characterized by mesomelic limb shortening, acral synostoses, and multiple congenital malformations. OATP5A1 may be a non-classical OATP which is involved in biological processes that require the reorganization of the cell shape, such as differentiation and migration. It seems to affect intracellular transport of drugs and may participate in chemoresistance of small cell lung cancer (SCLC by sequestration), rather than mediating cellular uptake. The SLCO5/OATP5 family belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340962 [Multi-domain]  Cd Length: 425  Bit Score: 40.80  E-value: 4.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75127280  26 CSFGC---LDVYKPVCGSNGETYSNSCYlrlASCKS-NNGITEAGD-GECASTPaSSATPSPVTSSTGSTSGTVGCPDMC 100
Cdd:cd17404 320 CNVNCgcsINEYEPVCGSDGITYFSPCL---AGCTSvGNTSTGIRNyTNCACLQ-SRSSISPPTVGQGSQLQAGPCSRTC 395
MFS_SLCO_OATP cd17336
Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; ...
 25-82 5.63e-04

Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; Solute carrier organic anion transporters (SLCOs) are also called organic anion transporting polypeptides (OATPs) or SLC21 (Solute carrier family 21) proteins. They are sodium-independent transporters that mediate the transport of a broad range of endo- as well as xenobiotics. Their substrates are mainly amphipathic organic anions with a molecular weight of more than 300Da, although there are a few known neutral or positively charged substrates. These include drugs including statins, angiotensin-converting enzyme inhibitors, angiotensin receptor blockers, antibiotics, antihistaminics, antihypertensives, and anticancer drugs. SLCOs/OATPs can be classified into 6 families (SLCO1-6 or OATP1-6) and each family may have subfamilies (e.g. OATP1A, OATP1B, OATP1C). Within the subfamilies, individual members are numbered according to the chronology of their identification and if there is already an ortholog known, they are given the same number. For example, the first SLCO identified, is rat OATP1A1 (encoded by the Slco1a1 gene). The second SLCO identified is the first human SLCO from the same subfamily and is called OATP1A2 (encoded by the SLCO1A2 gene). There are 11 human SLCOs/OATPs. SLCOs belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340894 [Multi-domain]  Cd Length: 411  Bit Score: 40.30  E-value: 5.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75127280  25 NCSFGCL---DVYKPVCGSNGETYSNSCYlrlASCKS---NNGITEAGDGECASTPASSATPSP 82
Cdd:cd17336 311 SCNSDCNcsdSSFSPVCGSDGITYFSPCH---AGCTSsdaGNGTKTYSNCSCINSGTATSSGCP 371
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 96-127 1.02e-03

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 36.12  E-value: 1.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 75127280     96 CPDMCLDVYDPVSDENGKEYSNQCYMEMAKCK 127
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACE 33
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 167-195 4.57e-03

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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 34.39  E-value: 4.57e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 75127280   167 CP-DNYAPVCGSDGETYPNECDLGITSCNH 195
Cdd:pfam07648   6 CPkTEYEPVCGSDGVTYPSPCALCAAGCKL 35
MFS_SLCO1A_OATP1A cd17458
Solute carrier organic anion transporter 1A subfamily of the Major Facilitator Superfamily of ...
 15-99 9.50e-03

Solute carrier organic anion transporter 1A subfamily of the Major Facilitator Superfamily of transporters; The Solute carrier organic anion transporter 1A (SLCO1A), also called Organic anion-transporting polypeptide 1A (OATP1A), subfamily is composed of one human member OATP1A2 (encoded by SLCO1A2) and several rodent proteins encoded by the Slco1a1, Slco1a3, Slco1a4, Slco1a5, and Slco1a6 genes. OATP1A2, also known as human OATP-A or OATP1, shows a broad spectrum of substrates including endogenous compounds (such as bile acids, steroid hormones and their conjugates, thyroid hormones) and various drugs (such as fexofenadine, ouabain and the cyanobacterial toxin microcystin). It is expressed in the brain, kidney, intestine, liver, lung, testes, and the eye (ciliary body). The SLCO1A/OATP1A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341016 [Multi-domain]  Cd Length: 527  Bit Score: 36.76  E-value: 9.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75127280  15 TATISAAADDNCSfgcLDVYKPVCGSNGETYSNSCylrLASCKSNNGITEAGDGECASTPASSATPSPVTSSTGSTSGTV 94
Cdd:cd17458 420 TLLADCNRDCDCP---LKVWDPVCGNNGLTYVSAC---LAGCKASVGTGKNMVFQNCSCVAASGFPSQNSSAVGQCDKGE 493


                ....*
gi 75127280  95 GCPDM 99
Cdd:cd17458 494 TCDKM 498
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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