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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTrypsin-like serine proteases8037496 3000114 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyBPTI-like8038527 3000628 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATrypsin_1e1tawA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrel 2F: Trypsin_1ECOD (1.6)
BKunitz_BPTIe1tawB1 A: few secondary structure elementsX: BPTI-like (From Topology)H: BPTI-like (From Topology)T: BPTI-likeF: Kunitz_BPTIECOD (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)
B4.10.410.10 Few Secondary Structures Irregular Factor Xa Inhibitor Pancreatic trypsin inhibitor Kunitz domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00089Trypsin (Trypsin)Trypsin- Domain
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
TRYPSIN
PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR009003Peptidase S1, PA clanHomologous Superfamily
IPR001314Peptidase S1A, chymotrypsin familyFamily
IPR033116Serine proteases, trypsin family, serine active siteActive Site
IPR001254Serine proteases, trypsin domainDomain
IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
IPR018114Serine proteases, trypsin family, histidine active siteActive Site
IPR013803Amyloidogenic glycoprotein, amyloid-beta peptideDomain
IPR008154Amyloidogenic glycoprotein, extracellularDomain
IPR036176E2 domain superfamilyHomologous Superfamily
IPR024329Amyloidogenic glycoprotein, E2 domainDomain
IPR036669Amyloidogenic glycoprotein, copper-binding domain superfamilyHomologous Superfamily
IPR019745Amyloidogenic glycoprotein, intracellular domain, conserved siteConserved Site
IPR011178Amyloidogenic glycoprotein, copper-bindingDomain
IPR037071Amyloidogenic glycoprotein, amyloid-beta peptide superfamilyHomologous Superfamily
IPR020901Proteinase inhibitor I2, Kunitz, conserved siteConserved Site
IPR019744Amyloidogenic glycoprotein, copper-binding domain conserved siteConserved Site
IPR002223Pancreatic trypsin inhibitor Kunitz domainDomain
IPR015849Amyloidogenic glycoprotein, heparin-bindingDomain
IPR036454Amyloidogenic glycoprotein, heparin-binding domain superfamilyHomologous Superfamily
IPR011993PH-like domain superfamilyHomologous Superfamily
IPR019543Beta-amyloid precursor protein C-terminalDomain
IPR036880Pancreatic trypsin inhibitor Kunitz domain superfamilyHomologous Superfamily
IPR008155Amyloidogenic glycoproteinFamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP05067