y
Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT5G61250.2 |
Family | GH79 |
Protein Properties | Length: 540 Molecular Weight: 59864.5 Isoelectric Point: 8.1369 |
Chromosome | Chromosome/Scaffold: 5 Start: 24632154 End: 24635303 |
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 | 41 | 533 | 0 |
DENFICATLDWWPPEKCNYDQCPWGYASLINLNLASPLLAKAIQAFRTLRIRIGGSLQDQVIYDVGDLKTPCTQFKKTDDGLFGFSEGCLYMKRWDEVNH FFNATGAIVTFGLNALHGRNKLNGTAWGGDWDHTNTQDFMNYTVSKGYAIDSWEFGNELSGSGIWASVSVELYGKDLIVLKNVIKNVYKNSRTKPLVVAP GGFFEEQWYSELLRLSGPGVLDVLTHHIYNLGPGNDPKLVNKILDPNYLSGISELFANVNQTIQEHGPWAAAWVGEAGGAFNSGGRQVSETFINSFWYLD QLGISSKHNTKVYCRQALVGGFYGLLEKETFVPNPDYYSALLWHRLMGKGILGVQTTASEYLRAYVHCSKRRAGITILLINLSKHTTFTVAVSNGVKVVL QAESMKRKSFLETIKSKVSWVGNKASDGYLNREEYHLSPKDGDLRSKIMLLNGKPLVPTATGDIPKLEPVRHGVKSPVYINPLSISFIVLPTF |
Full Sequence |
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Protein Sequence Length: 540 Download |
MGFNVVVFLS CLLLLPPVTF GSNMERTTLV IDGSRRIAET DENFICATLD WWPPEKCNYD 60 QCPWGYASLI NLNLASPLLA KAIQAFRTLR IRIGGSLQDQ VIYDVGDLKT PCTQFKKTDD 120 GLFGFSEGCL YMKRWDEVNH FFNATGAIVT FGLNALHGRN KLNGTAWGGD WDHTNTQDFM 180 NYTVSKGYAI DSWEFGNELS GSGIWASVSV ELYGKDLIVL KNVIKNVYKN SRTKPLVVAP 240 GGFFEEQWYS ELLRLSGPGV LDVLTHHIYN LGPGNDPKLV NKILDPNYLS GISELFANVN 300 QTIQEHGPWA AAWVGEAGGA FNSGGRQVSE TFINSFWYLD QLGISSKHNT KVYCRQALVG 360 GFYGLLEKET FVPNPDYYSA LLWHRLMGKG ILGVQTTASE YLRAYVHCSK RRAGITILLI 420 NLSKHTTFTV AVSNGVKVVL QAESMKRKSF LETIKSKVSW VGNKASDGYL NREEYHLSPK 480 DGDLRSKIML LNGKPLVPTA TGDIPKLEPV RHGVKSPVYI NPLSISFIVL PTFDAPACS* 540 600 |
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 | 24 | 343 | 320 | + 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:0012505 | endomembrane system |
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 | BAB08480.1 | 0 | 24 | 539 | 1 | 516 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CAB62595.1 | 0 | 20 | 539 | 1 | 521 | putative protein [Arabidopsis thaliana] |
RefSeq | NP_196400.2 | 0 | 1 | 539 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | NP_200933.2 | 0 | 1 | 539 | 1 | 539 | AtGUS1 (Arabidopsis thaliana glucuronidase 1); beta-glucuronidase |
RefSeq | XP_002514696.1 | 0 | 17 | 539 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |