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InterPro: IPR018114 Peptidase S1/S6, chymotrypsin/Hap, active site

Protein matchesHelp
UniProtKB
Matches:
7885 proteins
AccessionHelp IPR018114 Peptidase_S1/S6_AS
TypeHelp Active_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001254 Peptidase S1/S6, chymotrypsin/Hap
IPR001314 Peptidase S1A, chymotrypsin
IPR001316 Peptidase S1A, streptogrisin
IPR003966 Peptidase S1A, prothrombin/thrombin
IPR008256 Peptidase S1B, glutamyl endopeptidase I
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR011163 Peptidase S1A, enteropeptidase
IPR011358 Peptidase S1A, plasmin
IPR011360 Complement B/C2
IPR012051 Peptidase S1A, prothrombin
IPR012224 Peptidase S1A, coagulation factor VII/IX/X/C/Z
IPR012267 Peptidase S1A, acrosin
IPR014394 Coagulation factor XII/hepatocyte growth factor activator
IPR017051 Suppressor of tumourigenicity 14
IPR017052 Atrial natriuteric peptide-converting enzyme
IPR017118 Matriptase-2
IPR017324 Transmembrane serine protease, TMPRSS9
IPR017326 Polyserase-2
IPR017327 Transmembrane serine protease, TMPRSS13
IPR017329 Serine protease, transmembrane, TMPRSS11A
GO Term annotationHelp
Process GO:0006508 proteolysis
Function GO:0004252 serine-type endopeptidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S))and to peptidase family S6 (Hap serine peptidases). The catalytic activity of the serine proteases from the chymotrypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site serine and histidine residues are well conserved in this family of proteases [1].

The chymotrypsin family is almost totally confined to animals, although trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora, and in the fungus Fusarium oxysporum [2]. The enzymes are inherently secreted, being synthesised with a signal peptide that targets them to the secretory pathway. Animal enzymes are either secreted directly, packaged into vesicles for regulated secretion, or are retained in leukocyte granules [2].

The Hap family, 'Haemophilus adhesion and penetration', are proteins that play a role in the interaction with human epithelial cells. The serine protease activity is localized at the N-terminal domain, whereas the binding domain is in the C-terminal region.

Structural linksHelp
PDB - click here
SCOP: b.47.1.1 , b.47.1.2
CATH: 2.40.10.10
Database linksHelp
Enzyme: EC:3.4.21

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR018114 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O00187 Mannan-binding lectin serine protease 2

P00743 Coagulation factor X

P00756 Kallikrein 1-related peptidase b3

P00775 Trypsin

P04814 Trypsin alpha

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000294 Gamma-carboxyglutamic acid-rich (GLA) domain
IPR001881 EGF-like calcium-binding
IPR001254 Peptidase S1/S6, chymotrypsin/Hap
IPR002383 Coagulation factor, Gla domain
IPR000859 CUB
IPR006210 EGF-like
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR016060 Complement control module
IPR000152 EGF-type aspartate/asparagine hydroxylation site
IPR000742 EGF-like, type 3
IPR018114 Peptidase S1/S6, chymotrypsin/Hap, active site
IPR013032 EGF-like region, conserved site
IPR000436 Sushi/SCR/CCP
IPR012224 Peptidase S1A, coagulation factor VII/IX/X/C/Z
IPR001314 Peptidase S1A, chymotrypsin
IPR006209 EGF
IPR018097 EGF-like calcium-binding, conserved site
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Brenner S.
The molecular evolution of genes and proteins: a tale of two serines.
Nature 334 528-30 1988 [PubMed: 3136396]
http://dx.doi.org/10.1038/334528a0
2. Rawlings ND, Barrett AJ.
Families of serine peptidases.
Meth. Enzymol. 244 19-61 1994 [PubMed: 7845208]
http://dx.doi.org/10.1016/0076-6879(94)44004-2

Additional ReadingHelp
Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G.
Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin.
J. Mol. Biol. 375 2008 812-23 [PubMed: 18054043]
http://dx.doi.org/10.1016/j.jmb.2007.10.084
Isaacs RC, Solinsky MG, Cutrona KJ, Newton CL, Naylor-Olsen AM, McMasters DR, Krueger JA, Lewis SD, Lucas BJ, Kuo LC, Yan Y, Lynch JJ, Lyle EA.
Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.
Bioorg. Med. Chem. Lett. 18 2008 2062-6 [PubMed: 18291642]
http://dx.doi.org/10.1016/j.bmcl.2008.01.098
Lima LM, Becker CF, Giesel GM, Marques AF, Cargnelutti MT, de Oliveira Neto M, Monteiro RQ, Verli H, Polikarpov I.
Structural and thermodynamic analysis of thrombin:suramin interaction in solution and crystal phases.
Biochim. Biophys. Acta 1794 2009 873-81 [PubMed: 19332154]
Nieman MT, Burke F, Warnock M, Zhou Y, Sweigart J, Chen A, Ricketts D, Lucchesi BR, Chen Z, Di Cera E, Hilfinger J, Kim JS, Mosberg HI, Schmaier AH.
Thrombostatin FM compounds: direct thrombin inhibitors - mechanism of action in vitro and in vivo.
J. Thromb. Haemost. 6 2008 837-45 [PubMed: 18315550]
http://dx.doi.org/10.1111/j.1538-7836.2008.02937.x
Fernandez IS, Standker L, Magert HJ, Forssmann WG, Gimenez-Gallego G, Romero A.
Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6).
J. Mol. Biol. 377 2008 1488-97 [PubMed: 18329042]
http://dx.doi.org/10.1016/j.jmb.2008.01.089
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InterPro 23.1