Reviewed, UniProtKB/Swiss-Prot Q9MYY0 (HPSE_BOVIN)

Names and origin

Protein names

Recommended name:
    Heparanase
    EC=3.2.-.-
Cleaved into the following 2 chains:
    1- Recommended name:
            Heparanase 8 kDa subunit
    2- Recommended name:
            Heparanase 50 kDa subunit

Gene names

Name:

HPSE

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Endoglycosidase which is a cell surface and extracellular matrix-degrading enzyme. Cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Also implicated in the extravasation of leukocytes and tumor cell lines. Contributes to metastasis and angiogenesis By similarity.
Enzyme regulation	Inhibited by laminarin sulfate and, to a lower extent, by heparin, sulfamin and EDTA. Activated by calcium and magnesium By similarity.
Subunit structure	The active heterodimer is composed of the 8 and 50 kDa subunits, the proteolytic products By similarity.
Subcellular location	Lysosome membrane; Peripheral membrane protein By similarity. Secreted By similarity. Note: Secreted, internalised and transferred to late endosomes/lysosomes as a proheparanase. In lysosomes, it is processed into the active form, the heparanase. The uptake or internalisation of proheparanase is mediated by HSPGs. Heparin appears to be a competitor and retain proheparanase in the extracellular medium By similarity.
Tissue specificity	Highly expressed in placenta and weakly in the kidney, lung, spleen and uterus. Ref.1
Post-translational modification	Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, 8 kDa and 50 kDa product. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme By similarity. N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 79 family.

Ontologies

Keywords
Cellular component	Lysosome Membrane Secreted
Domain	Signal
Ligand	Calcium Magnesium
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	By similarity
	Chain	38 – 111	74	Heparanase 8 kDa subunit By similarity		PRO_0000042256
	Propeptide	112 – 159	48	Linker peptide		PRO_0000042257
	Chain	160 – 545	386	Heparanase 50 kDa subunit By similarity		PRO_0000042258
Regions
	Region	160 – 164	5	Heparin/HS-binding Potential
	Region	272 – 282	11	Heparin/HS-binding Potential
Sites
	Active site	227	1	Proton donor Potential
	Active site	345	1	Nucleophile Potential
Amino acid modifications
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9MYY0-1 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: FAC4BDFFD855B933	FASTA	545	61,077
	10 20 30 40 50 60 MLACRKPGLR PPLLLLLPLL GPLGPCSPGT PAAAAPADDA AELEFFTERP LHLVSPAFLS 70 80 90 100 110 120 FTIDANLATD PRFFTFLGSS KLRTLARGLA PAYLRFGGNK GDFLIFDPKK EPAFEERSYW 130 140 150 160 170 180 LSQSNQDICK SGSIPSDVEE KLRLEWPFQE QVLLREQYQK KFTNSTYSRS SVDMLYTFAS 190 200 210 220 230 240 CSGLNLIFGV NALLRTTDMH WDSSNAQLLL DYCSSKNYNI SWELGNEPNS FQRKAGIFIN 250 260 270 280 290 300 GRQLGEDFIE FRKLLGKSAF KNAKLYGPDI GQPRRNTVKM LKSFLKAGGE VIDSVTWHHY 310 320 330 340 350 360 YVNGRIATKE DFLNPDILDT FISSVQKTLR IVEKIRPLKK VWLGETSSAF GGGAPFLSNT 370 380 390 400 410 420 FAAGFMWLDK LGLSARMGIE VVMRQVLFGA GNYHLVDGNF EPLPDYWLSL LFKKLVGNKV 430 440 450 460 470 480 LMASVKGPDR SKFRVYLHCT NTKHPRYKEG DLTLYALNLH NVTKHLELPH HLFNKQVDKY 490 500 510 520 530 540 LIKPSGTDGL LSKSVQLNGQ ILKMVDEQTL PALTEKPLHP GSSLGMPPFS YGFFVIRNAK VAACI

References

[1]	"Expression of heparanase mRNA in bovine placenta during gestation." Kizaki K., Nakano H., Nakano H., Takahashi T., Imai K., Hashizume K. Reproduction 121:573-580(2001) [PubMed: 11277877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Placenta.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF281160 mRNA. Translation: AAF87301.2.
IPI	IPI00696957.
RefSeq	NP_776507.1.
UniGene	Bt.8127
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH79. Glycoside Hydrolase Family 79.
Genome annotation databases
Ensembl	ENSBTAG00000005745. Bos taurus. [Contig view]
GeneID	281230.
KEGG	bta:281230.
Phylogenomic databases
HOVERGEN	Q9MYY0.
Family and domain databases
InterPro	IPR005199. Glyco_hydro_79_N. [Graphical view]
PANTHER	PTHR14363. Glyco_hydro_79_N. 1 hit.
Pfam	PF03662. Glyco_hydro_79n. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HPSE_BOVIN

Accession

Primary (citable) accession number: Q9MYY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)