| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000248683 |
| Family | GH79 |
| Protein Properties | Length: 486 Molecular Weight: 53993.4 Isoelectric Point: 10.532 |
| Chromosome | Chromosome/Scaffold: 007993313 Start: 13286 End: 15383 |
| Description | glucuronidase 2 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 263 | 418 | 2.8026e-45 |
| VWVGNWDYSNAYDFIKYTVSKRYQIDSWEFGNELSGSGVEASVGAGQYGRDLIKLKSIINHLYNKSVAKPALMAPGGFFDQSWFARLLQVSGSGTVDIIS QHLYNLGAGVDPMLNGHWASIWVGESGGAYNSGGRNVSDTYVNSFWYLDQLGMSAN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 486 Download |
| MIVSKPILTR PSPLSAKQIH LDQALHLTSL ARSPNPGLPC PLQARVQFFI IVISHRLFPM 60 VHLRLSQPQE PVQQLRMWIQ RRRRRLQEVR RLGERSPPRA TVRKPTLGGP TGSRATVRKP 120 TLAVISSPPM RSSTPGDLFL PLLRSKAIPN RRATEAAQVH VKSDVELSDL LLHPQQNTRL 180 FCNGPISIVS FFAANNLIQF HVFCTSPSDS EPLFVHLRTK PMNRNPISSK LPSRRSSQMT 240 TVWKKHQDPE QQHHQNHHKG GGVWVGNWDY SNAYDFIKYT VSKRYQIDSW EFGNELSGSG 300 VEASVGAGQY GRDLIKLKSI INHLYNKSVA KPALMAPGGF FDQSWFARLL QVSGSGTVDI 360 ISQHLYNLGA GVDPMLNGHW ASIWVGESGG AYNSGGRNVS DTYVNSFWYL DQLGMSANFR 420 NGHTSSPSQV KLVELQPKEA PEVDSTSLSA PISNLLQEPV TSSSYSPHSA SAPTPTSIDP 480 PQIREP 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 2.0e-68 | 264 | 414 | 177 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0016020 | membrane |
| GO:0016798 | hydrolase activity, acting on glycosyl bonds |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACJ85515.1 | 0 | 252 | 419 | 159 | 348 | unknown [Medicago truncatula] |
| EMBL | CBI15157.1 | 0 | 262 | 419 | 163 | 346 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002284470.1 | 0 | 262 | 419 | 163 | 346 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002321464.1 | 0 | 257 | 419 | 158 | 346 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514696.1 | 0 | 254 | 419 | 155 | 346 | Heparanase-2, putative [Ricinus communis] |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GO505680 | 156 | 263 | 392 | 0 |
| FQ451832 | 183 | 264 | 420 | 0 |
| FQ415973 | 183 | 264 | 420 | 0 |
| FQ450088 | 183 | 264 | 420 | 0 |
| FQ430098 | 183 | 264 | 420 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
