Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.018G121500.3 |
Family | GH79 |
Protein Properties | Length: 438 Molecular Weight: 48220.6 Isoelectric Point: 7.0783 |
Chromosome | Chromosome/Scaffold: 18 Start: 14530021 End: 14532987 |
Description | glucuronidase 3 |
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 | 57 | 427 | 0 |
ENSICATLDWWPPEKCDYGTCSWDHASLINLDLNNSILLNAIKAFSPLKIRIGGTLQDKVIYDTEDNKQPCVQFVKNTREMFGFTQGCLPMYRWDELNAF FKKSGAEIIFGLNALTGRSMKSDGSAVGAWNYSNAESFISYTIKKNYSIYGWELGNELCGSGVGTRVAAAQYASDTISLYNIVKKIYSSIEPKPLVIAPG GFYDANWFKEFVDKTGNSVDAITHHIYNLGPGVDTHLIEKILNPSYLDGEARTFNSLQSTLKSSATSAVAWVGESGGAYNSGRNLVTNAFVFSFWYLDQL GMASSYDTKTYCRQSLIGGNYGLLNTTTFVPNPDYYSALLWHRLMGRNVLSTSFSGTKKIRAYTHCAKQSV |
Full Sequence |
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Protein Sequence Length: 438 Download |
MIYLQNWQMG LCLLVCIISC CFISVSSQSA VAGNDNNSVV EGTVFIDGKS SIGKIDENSI 60 CATLDWWPPE KCDYGTCSWD HASLINLDLN NSILLNAIKA FSPLKIRIGG TLQDKVIYDT 120 EDNKQPCVQF VKNTREMFGF TQGCLPMYRW DELNAFFKKS GAEIIFGLNA LTGRSMKSDG 180 SAVGAWNYSN AESFISYTIK KNYSIYGWEL GNELCGSGVG TRVAAAQYAS DTISLYNIVK 240 KIYSSIEPKP LVIAPGGFYD ANWFKEFVDK TGNSVDAITH HIYNLGPGVD THLIEKILNP 300 SYLDGEARTF NSLQSTLKSS ATSAVAWVGE SGGAYNSGRN LVTNAFVFSF WYLDQLGMAS 360 SYDTKTYCRQ SLIGGNYGLL NTTTFVPNPD YYSALLWHRL MGRNVLSTSF SGTKKIRAYT 420 HCAKQSVKGD HITTNQP* |
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 | 40 | 357 | 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 | CBI25561.1 | 0 | 9 | 426 | 1 | 414 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 7 | 426 | 10 | 425 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 42 | 426 | 1 | 385 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 9 | 426 | 1 | 411 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533671.1 | 0 | 10 | 426 | 9 | 423 | heparanase, 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 | 0.0000001 | 151 | 411 | 122 | 371 | A Chain A, Crystal Structure Of Human Aflatoxin B1 Aldehyde Reductase Member 3 |
PDB | 3vnz_A | 0.0000001 | 151 | 411 | 122 | 371 | A Chain A, Crystal Structure Of Human Aflatoxin B1 Aldehyde Reductase Member 3 |
PDB | 3vny_A | 0.0000001 | 151 | 411 | 122 | 371 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |