Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGlycosyl hydrolase domain-like 8051979 3001528 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyGlycosyl hydrolase domain-like 8051979 3001528 SCOP2B (2022-06-29)
ASCOP2B Superfamily(Trans)glycosidases 8051977 3000313 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAlpha-L-AF_Ce7psiA1 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: Alpha-L-AF_CECOD (1.6)
AGlyco_hydro_3e7psiA2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: Glyco_hydro_3ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF16862Glycosyl hydrolase family 79 C-terminal beta domain (Glyco_hydro_79C)Glycosyl hydrolase family 79 C-terminal beta domainThis domain is found at the C-terminus of glycosyl hydrolase family 79 proteins. It's function is not yet known [1].Domain
PF03662Glycosyl hydrolase family 79, N-terminal domain (Glyco_hydro_79n)Glycosyl hydrolase family 79, N-terminal domainFamily of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate ...Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesised as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Beta-glucuronidase -