y
Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01007918001 |
Family | GH79 |
Protein Properties | Length: 514 Molecular Weight: 57304.3 Isoelectric Point: 7.5752 |
Chromosome | Chromosome/Scaffold: 17 Start: 7531886 End: 7537040 |
Description | glucuronidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 39 | 507 | 0 |
DANFICATLDWWPHDKCNYNHCPWGYSSVINMDLSHPLFAKAIEAFKHLRIRIGGSLQDQVLYDIGSLRSPCHPFRKMNDGLFGFSKGCLRMSRWDELNR LFSQTGVILTFGLNALYGRYQIRKGAWAGVWDSSNTQNFIKYTISKGYQIDSWEFGNELSGSGVGASVNAEQYGKDLINLKAIINKLYNNSNVKPLLVAP GGFYEQDWYAKLLQVSGSSTVNVVTHHIYNLGAGVDPNLVSKILNPHYLSRVEETFKSLDKTLQTWGPWASAWVGESGGAYNSGGHLVSNTFVNSFWYLD QLGMASKYHTKVYCRQTLIGGNYGLLNTTTLVPNPDYYSALLWHRLMGKGVLAVDSTASPFLRSYAHCSKGKAGITLLLINLSNQTTFQINVENSMNLNF KADEQLFREEYHLTPKDGYLRSQTMVLNGMPLELTDDGNIPSLNPVRLNLNAPIFINPLSIAFIAFPNF |
Full Sequence |
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Protein Sequence Length: 514 Download |
MGFRFFLFLF LATLPAFLAQ EFEDAIIKVD GATTVAETDA NFICATLDWW PHDKCNYNHC 60 PWGYSSVINM DLSHPLFAKA IEAFKHLRIR IGGSLQDQVL YDIGSLRSPC HPFRKMNDGL 120 FGFSKGCLRM SRWDELNRLF SQTGVILTFG LNALYGRYQI RKGAWAGVWD SSNTQNFIKY 180 TISKGYQIDS WEFGNELSGS GVGASVNAEQ YGKDLINLKA IINKLYNNSN VKPLLVAPGG 240 FYEQDWYAKL LQVSGSSTVN VVTHHIYNLG AGVDPNLVSK ILNPHYLSRV EETFKSLDKT 300 LQTWGPWASA WVGESGGAYN SGGHLVSNTF VNSFWYLDQL GMASKYHTKV YCRQTLIGGN 360 YGLLNTTTLV PNPDYYSALL WHRLMGKGVL AVDSTASPFL RSYAHCSKGK AGITLLLINL 420 SNQTTFQINV ENSMNLNFKA DEQLFREEYH LTPKDGYLRS QTMVLNGMPL ELTDDGNIPS 480 LNPVRLNLNA PIFINPLSIA FIAFPNFDAP ACA* 540 |
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 | 23 | 341 | 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 | CBI15157.1 | 0 | 1 | 513 | 1 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 513 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 1 | 513 | 1 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321464.1 | 0 | 1 | 513 | 1 | 541 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514696.1 | 0 | 15 | 513 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |