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Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT5G34940.1 |
Family | GH79 |
Protein Properties | Length: 402 Molecular Weight: 44735.8 Isoelectric Point: 9.4695 |
Chromosome | Chromosome/Scaffold: 5 Start: 13235829 End: 13238457 |
Description | heparanase-like protein precursor, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 1 | 395 | 0 |
MRRWDELNAFFRKTGTKVIFGLNALSGRSIKSNGEAIGAWNYTNAESFIRFTAENNYTIDGWELGNELCGSGVGARVGANQYAIDTINLRNIVNRVYKNV SPMPLVIGPGGFFEVDWFTEYLNKAENSLNATTRHIYDLGPGVDEHLIEKILNPSYLDQEAKSFRSLKNIIKNSSTKAVAWVGESGGAYNSGRNLVSNAF VYSFWYLDQLGMASLYDTKTYCRQSLIGGNYGLLNTTNFTPNPDYYSALIWRQLMGRKALFTTFSGTKKIRSYTHCARQSKGITVLLMNLDNTTTVVAKV ELNNSFSLRHTKHMKSYKRASSQLFGGPNGVIQREEYHLTAKDGNLHSQTMLLNGNALQVNSMGDLPPIEPIHINSTEPITIAPYSIVFVHMRNV |
Full Sequence |
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Protein Sequence Length: 402 Download |
MRRWDELNAF FRKTGTKVIF GLNALSGRSI KSNGEAIGAW NYTNAESFIR FTAENNYTID 60 GWELGNELCG SGVGARVGAN QYAIDTINLR NIVNRVYKNV SPMPLVIGPG GFFEVDWFTE 120 YLNKAENSLN ATTRHIYDLG PGVDEHLIEK ILNPSYLDQE AKSFRSLKNI IKNSSTKAVA 180 WVGESGGAYN SGRNLVSNAF VYSFWYLDQL GMASLYDTKT YCRQSLIGGN YGLLNTTNFT 240 PNPDYYSALI WRQLMGRKAL FTTFSGTKKI RSYTHCARQS KGITVLLMNL DNTTTVVAKV 300 ELNNSFSLRH TKHMKSYKRA SSQLFGGPNG VIQREEYHLT AKDGNLHSQT MLLNGNALQV 360 NSMGDLPPIE PIHINSTEPI TIAPYSIVFV HMRNVVVPAC A* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 4.0e-134 | 1 | 211 | 212 | + 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:0004566 | beta-glucuronidase activity |
GO:0008150 | biological_process |
GO:0009505 | plant-type cell wall |
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 |
DDBJ | BAB10787.1 | 0 | 1 | 401 | 136 | 536 | unnamed protein product [Arabidopsis thaliana] |
RefSeq | NP_851092.1 | 0 | 1 | 401 | 1 | 401 | AtGUS3 (Arabidopsis thaliana glucuronidase 3); beta-glucuronidase |
RefSeq | NP_851093.1 | 0 | 1 | 401 | 136 | 536 | AtGUS3 (Arabidopsis thaliana glucuronidase 3); beta-glucuronidase |
RefSeq | XP_002324603.1 | 0 | 1 | 401 | 106 | 506 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 1 | 401 | 132 | 547 | predicted protein [Populus trichocarpa] |
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 | 0.00000009 | 7 | 258 | 124 | 369 | A Chain A, Ribonuclease From Escherichia Coli Complexed With Its Inhibitor Protein |
PDB | 3vnz_A | 0.00000009 | 7 | 258 | 124 | 369 | A Chain A, Ribonuclease From Escherichia Coli Complexed With Its Inhibitor Protein |
PDB | 3vny_A | 0.00000009 | 7 | 258 | 124 | 369 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FG565197 | 226 | 65 | 290 | 0 |
DR384073 | 207 | 196 | 402 | 0 |
CX636465 | 278 | 41 | 318 | 0 |
EE440979 | 218 | 102 | 319 | 0 |
FG564968 | 214 | 54 | 267 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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