Q90YK5 (HPSE_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heparanase EC=3.2.-.- | ||||
| Gene names |
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| Organism | Gallus gallus (Chicken) | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 523 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling By similarity. Increases cell adhesion to the extacellular matrix (ECM), independent of its enzymatic activity. Ref.2 |
| Subunit structure | Heterodimer; the active enzyme is a heterodimer of the 60 kDa and 45 kDa proteolytic products. Ref.1 |
| Subcellular location | |
| Developmental stage | Expressed, as early as 12 h post fertilization, in cells migrating from the epiblast and forming the hypoblast layer. Later on at 72 h, preferentially expressed in cells of the developing vascular and nervous systems. Ref.1 |
| Post-translational modification | N-glycosylated By similarity. Proteolytically cleaved to produce a 60 kDa and a 45 kDa product. |
| Sequence similarities | Belongs to the glycosyl hydrolase 79 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell-matrix adhesionInferred from direct assay Ref.2. Source: UniProtKB |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bondsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||
| Chain | 19 – 523 | 505 | Heparanase | PRO_0000042259 | |||||
Regions | |||||||||
| Region | 137 – 141 | 5 | Heparin/HS-binding By similarity | ||||||
| Region | 250 – 260 | 11 | Heparin/HS-binding By similarity | ||||||
Sites | |||||||||
| Active site | 204 | 1 | Proton donor Potential | ||||||
| Active site | 323 | 1 | Nucleophile Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 141 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 196 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 436 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 439 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Expression pattern and secretion of human and chicken heparanase are determined by their signal peptide sequence." Goldshmidt O., Zcharia E., Aingorn H., Guatta-Rangini Z., Atzmon R., Michal I., Pecker I., Mitrani E., Vlodavsky I. J. Biol. Chem. 276:29178-29187(2001) [PubMed: 11387326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, ENZYME ACTIVITY, DEVELOPMENTAL STAGE. |
| [2] | "Heparanase mediates cell adhesion independent of its enzymatic activity." Goldshmidt O., Zcharia E., Cohen M., Aingorn H., Cohen I., Nadav L., Katz B.Z., Geiger B., Vlodavsky I. FASEB J. 17:1015-1025(2003) [PubMed: 12773484] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY037007 mRNA. Translation: AAK82648.1. |
| IPI | IPI00576082. |
| RefSeq | NP_989498.1. NM_204167.1. |
| UniGene | Gga.950. |
3D structure databases | |
| ProteinModelPortal | Q90YK5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q90YK5. |
Protein family/group databases | |
| CAZy | GH79. Glycoside Hydrolase Family 79. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 373981. |
| KEGG | gga:373981. |
Organism-specific databases | |
| CTD | 10855. |
Phylogenomic databases | |
| eggNOG | veNOG10976. |
| GeneTree | ENSGT00390000004874. |
| HOGENOM | HBG715522. |
| HOVERGEN | HBG081606. |
| InParanoid | Q90YK5. |
| OrthoDB | EOG45MN5C. |
Family and domain databases | |
| InterPro | IPR005199. Glyco_hydro_79. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| KO | K07964. |
| PANTHER | PTHR14363. Glyco_hydro_79_N. 1 hit. |
| Pfam | PF03662. Glyco_hydro_79n. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HPSE_CHICK | ||||||||
| Accession | Primary (citable) accession number: Q90YK5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with