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Conserved domains on  [gi|315360645|ref|NP_001186759|]
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heparanase isoform 3 preproprotein [Homo sapiens]

Protein Classification

glycosyl hydrolase family 79 N-terminal domain-containing protein( domain architecture ID 5168)

glycosyl hydrolase family 79 N-terminal domain-containing protein similar to Homo sapiens heparanase, which acts as an endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans

EC:  3.2.-.-
Gene Ontology:  GO:0016798
PubMed:  8535779|20552664|31731209|21639842|7624375
SCOP:  4004076|4003957

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_79n super family cl04201
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
 179-312 4.56e-11

Glycosyl hydrolase family 79, N-terminal domain; 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 synthesized 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.


The actual alignment was detected with superfamily member pfam03662:

Pssm-ID: 461010  Cd Length: 318  Bit Score: 63.79  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315360645  179 INGSQLGEDFIQLHKLLRKsTFKNA----KLYGP----DvgqprrktAKMLKSFL-KAGGEVIDSVTWHHYYLN--GRTA 247
Cdd:pfam03662 183 VDADQYAKDVIALKNIVDD-LYKNSepkpLVLAPggffD--------ADWFTELLqKSGPGVVDVVTHHIYNLGpgVDPH 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315360645  248 TKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLG 312
Cdd:pfam03662 254 LINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
Name Accession Description Interval E-value
Glyco_hydro_79n pfam03662
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
 179-312 4.56e-11

Glycosyl hydrolase family 79, N-terminal domain; 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 synthesized 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.


Pssm-ID: 461010  Cd Length: 318  Bit Score: 63.79  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315360645  179 INGSQLGEDFIQLHKLLRKsTFKNA----KLYGP----DvgqprrktAKMLKSFL-KAGGEVIDSVTWHHYYLN--GRTA 247
Cdd:pfam03662 183 VDADQYAKDVIALKNIVDD-LYKNSepkpLVLAPggffD--------ADWFTELLqKSGPGVVDVVTHHIYNLGpgVDPH 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315360645  248 TKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLG 312
Cdd:pfam03662 254 LINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
Name Accession Description Interval E-value
Glyco_hydro_79n pfam03662
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
 179-312 4.56e-11

Glycosyl hydrolase family 79, N-terminal domain; 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 synthesized 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.


Pssm-ID: 461010  Cd Length: 318  Bit Score: 63.79  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315360645  179 INGSQLGEDFIQLHKLLRKsTFKNA----KLYGP----DvgqprrktAKMLKSFL-KAGGEVIDSVTWHHYYLN--GRTA 247
Cdd:pfam03662 183 VDADQYAKDVIALKNIVDD-LYKNSepkpLVLAPggffD--------ADWFTELLqKSGPGVVDVVTHHIYNLGpgVDPH 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315360645  248 TKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLG 312
Cdd:pfam03662 254 LINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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