Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad5jbta_ All beta proteins Trypsin-like serine proteases Trypsin-like serine proteases Eukaryotic proteases Trypsin(ogen) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTrypsin-like serine proteases8036274 3000114 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF00089e5jbtA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrel 2F: PF00089ECOD (1.6)
C [auth Y]PF00014e5jbtY1 A: few secondary structure elementsX: BPTI-like (From Topology)H: BPTI-like (From Topology)T: BPTI-likeF: PF00014ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.40.10.10 Mainly Beta Beta Barrel Thrombin, subunit H Trypsin-like serine proteasesCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00089Trypsin (Trypsin)Trypsin- Domain
B [auth X]PF00014Kunitz/Bovine pancreatic trypsin inhibitor domain (Kunitz_BPTI)Kunitz/Bovine pancreatic trypsin inhibitor domainIndicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the ...Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP, Swiss:P17726). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways [1]. TAP molecules are highly dipolar [2], and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix [1].
Domain
C [auth Y]PF00014Kunitz/Bovine pancreatic trypsin inhibitor domain (Kunitz_BPTI)Kunitz/Bovine pancreatic trypsin inhibitor domainIndicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the ...Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP, Swiss:P17726). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways [1]. TAP molecules are highly dipolar [2], and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
PRSS3 protein
B [auth X]Amyloid-like protein 2
C [auth Y]Amyloid-like protein 2

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR009003Peptidase S1, PA clanHomologous Superfamily
IPR001314Peptidase S1A, chymotrypsin familyFamily
IPR001254Serine proteases, trypsin domainDomain
IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
IPR018114Serine proteases, trypsin family, histidine active siteActive Site
B [auth X]IPR019744Amyloidogenic glycoprotein, copper-binding domain conserved siteConserved Site
B [auth X]IPR019745Amyloidogenic glycoprotein, intracellular domain, conserved siteConserved Site
B [auth X]IPR011178Amyloidogenic glycoprotein, copper-bindingDomain
B [auth X]IPR002223Pancreatic trypsin inhibitor Kunitz domainDomain
B [auth X]IPR008154Amyloidogenic glycoprotein, extracellularDomain
B [auth X]IPR015849Amyloidogenic glycoprotein, heparin-bindingDomain
B [auth X]IPR011993PH-like domain superfamilyHomologous Superfamily
B [auth X]IPR019543Beta-amyloid precursor protein C-terminalDomain
B [auth X]IPR036176E2 domain superfamilyHomologous Superfamily
B [auth X]IPR036454Amyloidogenic glycoprotein, heparin-binding domain superfamilyHomologous Superfamily
B [auth X]IPR020901Proteinase inhibitor I2, Kunitz, conserved siteConserved Site
B [auth X]IPR036880Pancreatic trypsin inhibitor Kunitz domain superfamilyHomologous Superfamily
B [auth X]IPR024329Amyloidogenic glycoprotein, E2 domainDomain
B [auth X]IPR036669Amyloidogenic glycoprotein, copper-binding domain superfamilyHomologous Superfamily
B [auth X]IPR008155Amyloidogenic glycoproteinFamily
C [auth Y]IPR019744Amyloidogenic glycoprotein, copper-binding domain conserved siteConserved Site
C [auth Y]IPR019745Amyloidogenic glycoprotein, intracellular domain, conserved siteConserved Site
C [auth Y]IPR011178Amyloidogenic glycoprotein, copper-bindingDomain
C [auth Y]IPR002223Pancreatic trypsin inhibitor Kunitz domainDomain
C [auth Y]IPR008154Amyloidogenic glycoprotein, extracellularDomain
C [auth Y]IPR015849Amyloidogenic glycoprotein, heparin-bindingDomain
C [auth Y]IPR011993PH-like domain superfamilyHomologous Superfamily
C [auth Y]IPR019543Beta-amyloid precursor protein C-terminalDomain
C [auth Y]IPR036176E2 domain superfamilyHomologous Superfamily
C [auth Y]IPR036454Amyloidogenic glycoprotein, heparin-binding domain superfamilyHomologous Superfamily
C [auth Y]IPR020901Proteinase inhibitor I2, Kunitz, conserved siteConserved Site
C [auth Y]IPR036880Pancreatic trypsin inhibitor Kunitz domain superfamilyHomologous Superfamily
C [auth Y]IPR024329Amyloidogenic glycoprotein, E2 domainDomain
C [auth Y]IPR036669Amyloidogenic glycoprotein, copper-binding domain superfamilyHomologous Superfamily
C [auth Y]IPR008155Amyloidogenic glycoproteinFamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP35030
B [auth X]PharosQ06481
C [auth Y]PharosQ06481