EzCatDB: M00348
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DB codeM00348
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 1-.-.-.-
Domain 23.30.70.960 : Alpha-Beta Plaits
Domain 32.60.120.290 : Jelly Rolls
Domain 42.60.120.290 : Jelly Rolls
Domain 54.10.100.10
Domain 64.10.100.10
Domain 74.10.100.10
Domain 84.10.100.10
Domain 92.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 102.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.109

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00349,T00074,T00410,T00411
2.60.120.290 : Jelly RollsM00139,M00227,M00315,M00316,M00317
3.30.70.960 : Alpha-Beta PlaitsM00227

Enzyme Name
UniProtKBKEGG

Q9Y5Y6
Protein nameSuppressor of tumorigenicity 14 proteinMatriptase
Serine protease 14
Membrane-type serine protease 1
MT-SP1
Prostamin
Serine protease TADG-15
Tumor-associated differentially-expressed gene 15 protein
ST14
Breast cancer 80 kDa protease
Epithin
Serine endopeptidase SNC19
SynonymsEC 3.4.21.109
Matriptase
Membrane-type serine protease 1
MT-SP1
Prostamin
Serine protease 14
Serine protease TADG-15
Tumor-associated differentially-expressed gene 15 protein
RefSeqNP_068813.1 (Protein)
NM_021978.3 (DNA/RNA sequence)
MEROPSS01.302 (Serine)
PfamPF00431 (CUB)
PF00057 (Ldl_recept_a)
PF01390 (SEA)
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberQ9Y5Y6
Entry nameST14_HUMAN
ActivityCleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.
SubunitInteracts with CDCP1. May interact with TMEFF1.
Subcellular locationMembrane, Single-pass type II membrane protein (Probable).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00001C00017I00087I00085I00086
CompoundProteinH2OProteinPeptidyl-Ser-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Ser-acyl group)Peptidyl-Ser-tetrahedral-intermediate
Typepeptide/proteinH2Opeptide/protein


ChEBI
15377




PubChem
962
22247451




              
1eawA01Bound:LYS 15-ALA 16(chain B) UnboundUnboundUnboundUnbound
1eawC01Bound:LYS 15-ALA 16(chain D) UnboundUnboundUnboundUnbound
1eaxA01Unbound UnboundUnboundUnboundUnbound
2gv6A01Unbound UnboundUnboundUnboundUnbound
2gv7A01Unbound UnboundUnboundUnboundUnbound
3bn9A01Unbound UnboundUnboundUnboundUnbound
3bn9B01Unbound UnboundUnboundUnboundUnbound
3nclA01Unbound UnboundTransition-state-analogue:CCZUnboundUnbound
3npsA01Unbound UnboundUnboundUnboundUnbound
3p8fA01Bound:LYS 5-SER 6(chain I) UnboundUnboundUnboundUnbound
3p8gA01Unbound UnboundUnboundUnboundUnbound
3so3A01Unbound UnboundUnboundUnboundUnbound
1eawA02Unbound UnboundUnboundUnboundUnbound
1eawC02Unbound UnboundUnboundUnboundUnbound
1eaxA02Unbound UnboundUnboundUnboundUnbound
2gv6A02Unbound UnboundUnboundUnboundUnbound
2gv7A02Unbound UnboundUnboundUnboundUnbound
3bn9A02Unbound UnboundUnboundUnboundUnbound
3bn9B02Unbound UnboundUnboundUnboundUnbound
3nclA02Unbound UnboundUnboundUnboundUnbound
3npsA02Unbound UnboundUnboundUnboundUnbound
3p8fA02Unbound UnboundUnboundUnboundUnbound
3p8gA02Unbound UnboundUnboundUnboundUnbound
3so3A02Unbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [4] & Swiss-prot;Q9Y5Y6
pdbCatalytic residuesMain-chain involved in catalysis
          
1eawA01SER 195
GLY 193;SER 195
1eawC01SER 195
GLY 193;SER 195
1eaxA01SER 195
GLY 193;SER 195
2gv6A01SER 195
GLY 193;SER 195
2gv7A01SER 195
GLY 193;SER 195
3bn9A01SER 195
GLY 193;SER 195
3bn9B01SER 195
GLY 193;SER 195
3nclA01SER 208
GLY 206;SER 208
3npsA01SER 195
GLY 193;SER 195
3p8fA01SER 195
GLY 193;SER 195
3p8gA01SER 195
GLY 193;SER 195
3so3A01SER 195
GLY 193;SER 195
1eawA02HIS 57;ASP 102
 
1eawC02HIS 57;ASP 102
 
1eaxA02HIS 57;ASP 102
 
2gv6A02HIS 57;ASP 102
 
2gv7A02HIS 57;ASP 102
 
3bn9A02HIS 57;ASP 102
 
3bn9B02HIS 57;ASP 102
 
3nclA02HIS 52;ASP 107
 
3npsA02HIS 57;ASP 102
 
3p8fA02HIS 57;ASP 102
 
3p8gA02HIS 57;ASP 102
 
3so3A02HIS 57;ASP 102
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Figure 5

references
[1]
PubMed ID9374470
JournalJ Biol Chem
Year1997
Volume272
Pages29987-90
AuthorsPerona JJ, Craik CS
TitleEvolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold.
[2]
PubMed ID10831593
JournalJ Biol Chem
Year2000
Volume275
Pages26333-42
AuthorsTakeuchi T, Harris JL, Huang W, Yan KW, Coughlin SR, Craik CS
TitleCellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates.
[3]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[4]
PubMed ID11696548
JournalJ Biol Chem
Year2002
Volume277
Pages2160-8
AuthorsFriedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL
TitleCatalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase.
Related PDB1eaw,1eax
Related UniProtKBQ9Y5Y6
[5]
PubMed ID12696750
JournalCurr Top Dev Biol
Year2003
Volume54
Pages167-206
AuthorsWu Q
TitleType II transmembrane serine proteases.
[6]
PubMed ID12738778
JournalJ Biol Chem
Year2003
Volume278
Pages26773-9
AuthorsOberst MD, Williams CA, Dickson RB, Johnson MD, Lin CY
TitleThe activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor.
[7]
PubMed ID16821772
JournalJ Med Chem
Year2006
Volume49
Pages4116-26
AuthorsSteinmetzer T, Schweinitz A, Sturzebecher A, Donnecke D, Uhland K, Schuster O, Steinmetzer P, Muller F, Friedrich R, Than ME, Bode W, Sturzebecher J
TitleSecondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase.
Related PDB2gv6,2gv7
Related UniProtKBQ9Y5Y6
[8]
PubMed ID17981566
JournalFront Biosci
Year2008
Volume13
Pages528-39
AuthorsDarragh MR, Bhatt AS, Craik CS
TitleMT-SP1 proteolysis and regulation of cell-microenvironment interactions.
[9]
PubMed ID18514224
JournalJ Mol Biol
Year2008
Volume380
Pages351-60
AuthorsFarady CJ, Egea PF, Schneider EL, Darragh MR, Craik CS
TitleStructure of an Fab-protease complex reveals a highly specific non-canonical mechanism of inhibition.
Related PDB3bn9
Related UniProtKBQ9Y5Y6
[10]
PubMed ID20507279
JournalBiochem J
Year2010
Volume428
Pages325-46
AuthorsAntalis TM, Buzza MS, Hodge KM, Hooper JD, Netzel-Arnett S
TitleThe cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.
[11]
PubMed ID21276938
JournalChem Biol
Year2011
Volume18
Pages48-57
AuthorsBrown CM, Ray M, Eroy-Reveles AA, Egea P, Tajon C, Craik CS
TitlePeptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors.
Related PDB3ncl
[12]
PubMed ID21693064
JournalBMC Struct Biol
Year2011
Volume11
Pages30
AuthorsYuan C, Chen L, Meehan EJ, Daly N, Craik DJ, Huang M, Ngo JC
TitleStructure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1.
Related PDB3p8f,3p8g
[13]
PubMed ID22154938
JournalJ Mol Biol
Year2012
Volume415
Pages699-715
AuthorsSchneider EL, Lee MS, Baharuddin A, Goetz DH, Farady CJ, Ward M, Wang CI, Craik CS
TitleA reverse binding motif that contributes to specific protease inhibition by antibodies.
Related PDB3nps,3so3

comments
This enzyme belongs to peptidase family-S1.
This enzyme is composed of several non-catalytic domains in the N-terminal region and C-terminal trypsin-like catalytic domain. Although the structures of the non-catalytic domains have not been solved yet, their homologous domains have been elucidated.
Since this enzyme has got the same catalytic site as trypsin, it must catalyze the trypsin-like reaction.

createdupdated
2011-03-092012-08-02


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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