| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000199066 |
| Family | GH79 |
| Protein Properties | Length: 503 Molecular Weight: 54399.1 Isoelectric Point: 4.9998 |
| Chromosome | Chromosome/Scaffold: 013289478 Start: 33559 End: 37235 |
| Description | glucuronidase 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 52 | 496 | 0 |
| DDDFICATIDWWPPQKCDYGTCSWGSASLLNLDLDNAIFLNAIKAFAPLKIRLGGTLQDKVTYLADGSQPPSTSFVKDGSQLFGFSQGRNIDSNGAATGA WNSTNAETLIRYTVDKGYTIHGWELGNELSGNGVGTKVSADQYAADTHTLHEILQKIYADYGSKPLVLAPGGFFDADWFTEFVHKTPPSLKVITHHIYNL GPGSAGDLVDKILDPDVLDGISQTFSSLQNLVETSDTSAVAWVGEAGGAYNSGHDLVTNAFVFSFWYLDQLGLAASYDTKTYCRQTLIGGNYGLLDTNTF QPNPDYYSALLWHRLMGNKALSTSFSGTKKIRAYAHCSKKTKGITVLLINLDGNTTVQVRVSTDSTGRPVSSESLQSSKDSDDVREEYHLTAQDGDLQSK VMLLNGKALIVDSSGDIPPLEPITVRLSDPTTVAPFSIVFVHVPN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 503 Download |
| MCEGMRSLMI LSLLCYGLYW ATHSHKSSIS VASLSTEETL FVNKTAAIGA TDDDFICATI 60 DWWPPQKCDY GTCSWGSASL LNLDLDNAIF LNAIKAFAPL KIRLGGTLQD KVTYLADGSQ 120 PPSTSFVKDG SQLFGFSQGR NIDSNGAATG AWNSTNAETL IRYTVDKGYT IHGWELGNEL 180 SGNGVGTKVS ADQYAADTHT LHEILQKIYA DYGSKPLVLA PGGFFDADWF TEFVHKTPPS 240 LKVITHHIYN LGPGSAGDLV DKILDPDVLD GISQTFSSLQ NLVETSDTSA VAWVGEAGGA 300 YNSGHDLVTN AFVFSFWYLD QLGLAASYDT KTYCRQTLIG GNYGLLDTNT FQPNPDYYSA 360 LLWHRLMGNK ALSTSFSGTK KIRAYAHCSK KTKGITVLLI NLDGNTTVQV RVSTDSTGRP 420 VSSESLQSSK DSDDVREEYH LTAQDGDLQS KVMLLNGKAL IVDSSGDIPP LEPITVRLSD 480 PTTVAPFSIV FVHVPNTTVP ACA 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 3.0e-154 | 37 | 323 | 318 | + 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 |
| EMBL | CBI25561.1 | 0 | 35 | 502 | 27 | 532 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002283254.1 | 0 | 10 | 503 | 4 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002283260.1 | 0 | 20 | 502 | 13 | 545 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324878.1 | 0 | 39 | 502 | 2 | 504 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515478.1 | 0 | 26 | 502 | 3 | 522 | heparanase, putative [Ricinus communis] |
