Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g014399m |
Family | GH79 |
Protein Properties | Length: 426 Molecular Weight: 47549 Isoelectric Point: 8.7551 |
Chromosome | Chromosome/Scaffold: 00122 Start: 127482 End: 133450 |
Description | glucuronidase 2 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 40 | 413 | 0 |
DEHFICATVDWWPHDKCNYNHCPWGNSSVINLDLSHPLLANAIQAFQSLRIRIGGSLQDQVLYDVGDLKAPCHPFRKMKDGLFGFSKGCLHMQRWDELNQ LFNRTRAIVSFGLNALHGRHNIRHNAWGGAWDSNNARDFLKYTISMGYQIDSWEYGNELSGRTSIGASVDAELYGKDLINLKNIINELYKNSSSKPTILA PGGFFDQEWYAKFLQVSGSNVVNGVTHHIYNLGPGVDPNLVSKILNPQRLSRVSETFGNLKQTIEKHGPWASAWVGESGGAYNSGGRHVSNTFVNSFWYL DQLGMSSKYNTKVYCRQTLVGGNYGLLNATTFIPNPDYYSALLWHRLMGKGVLSVATDGSSSLRSYAHCSKERV |
Full Sequence |
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Protein Sequence Length: 426 Download |
MGIFLSLFIY LISYLPVILA RDVTRVTIFV DATKTVATND EHFICATVDW WPHDKCNYNH 60 CPWGNSSVIN LDLSHPLLAN AIQAFQSLRI RIGGSLQDQV LYDVGDLKAP CHPFRKMKDG 120 LFGFSKGCLH MQRWDELNQL FNRTRAIVSF GLNALHGRHN IRHNAWGGAW DSNNARDFLK 180 YTISMGYQID SWEYGNELSG RTSIGASVDA ELYGKDLINL KNIINELYKN SSSKPTILAP 240 GGFFDQEWYA KFLQVSGSNV VNGVTHHIYN LGPGVDPNLV SKILNPQRLS RVSETFGNLK 300 QTIEKHGPWA SAWVGESGGA YNSGGRHVSN TFVNSFWYLD QLGMSSKYNT KVYCRQTLVG 360 GNYGLLNATT FIPNPDYYSA LLWHRLMGKG VLSVATDGSS SLRSYAHCSK ERVSVVFISI 420 SLLII* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 0 | 25 | 343 | 319 | + 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 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. |
Gene Ontology | |
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GO Term | Description |
GO:0016020 | membrane |
GO:0016798 | hydrolase activity, acting on glycosyl bonds |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAB62595.1 | 0 | 19 | 422 | 1 | 404 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 15 | 422 | 14 | 420 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 422 | 1 | 426 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 15 | 422 | 14 | 420 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 16 | 422 | 15 | 420 | Heparanase-2, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.006 | 168 | 406 | 142 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vnz_A | 0.006 | 168 | 406 | 142 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vny_A | 0.006 | 168 | 406 | 142 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |