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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth L]SCOP2B SuperfamilySRCR-like 8035378 3001377 SCOP2B (2022-06-29)
B [auth H]SCOP2B SuperfamilyTrypsin-like serine proteases 8035375 3000114 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth L]Hepsin-SRCRe1o5eL1 A: a+b complex topologyX: SRCR-likeH: SRCR-like (From Topology)T: SRCR-likeF: Hepsin-SRCRECOD (1.6)
B [auth H]Trypsin_1e1o5eH1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: FMN-binding split barrel 2F: Trypsin_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A [auth L]3.10.250.10 Alpha Beta Roll Mac-2 Binding Protein SRCR-like domainCATH (4.3.0)
B [auth H]2.40.10.10 Mainly Beta Beta Barrel Thrombin, subunit H Trypsin-like serine proteasesCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth L]PF09272Hepsin, SRCR domain (Hepsin-SRCR)Hepsin, SRCR domainMembers of this family form an extracellular domain of the serine protease hepsin. They are formed primarily by three elements of regular secondary structure: a 12-residue alpha helix, a twisted five-stranded antiparallel beta sheet, and a second, tw ...Members of this family form an extracellular domain of the serine protease hepsin. They are formed primarily by three elements of regular secondary structure: a 12-residue alpha helix, a twisted five-stranded antiparallel beta sheet, and a second, two-stranded, antiparallel sheet. The two beta-sheets lie at roughly right angles to each other, with the helix nestled between the two, adopting an SRCR fold. The exact function of this domain has not been identified, though it probably may serve to orient the protease domain or place it in the vicinity of its substrate [1].
Domain
B [auth H]PF00089Trypsin (Trypsin)Trypsin- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth L]Serine protease hepsin
B [auth H]Serine protease hepsin

Pharos: Disease Associations Pharos Homepage Annotation