P19758 (HN_SENDF) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 88.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Hemagglutinin-neuraminidase Short name=HN protein EC=3.2.1.18 | ||
| Gene names |
| ||
| Organism | Sendai virus (strain Fushimi) (SeV) [Complete proteome] | ||
| Taxonomic identifier | 11195 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Respirovirus ›  | ||
| Virus host | Cavia cutleri (Guinea pig) [TaxID: 10144] Cricetidae sp. (Hamster) [TaxID: 36483] Mus musculus (Mouse) [TaxID: 10090] Rattus norvegicus (Rat) [TaxID: 10116] |
Protein attributes
| Sequence length | 575 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion By similarity. Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins By similarity. |
| Catalytic activity | Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. |
| Subunit structure | Homotetramer; composed of disulfide-linked homodimers. Interacts with F protein trimer By similarity. Ref.3 |
| Subcellular location | Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential. |
| Post-translational modification | N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides By similarity. |
| Sequence similarities | Belongs to the paramyxoviruses hemagglutinin-neuraminidase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 575 | 575 | Hemagglutinin-neuraminidase | PRO_0000142637 | |||||
Regions | |||||||||
| Topological domain | 1 – 37 | 37 | Intravirion By similarity | ||||||
| Transmembrane | 38 – 58 | 21 | Helical; By similarity | ||||||
| Topological domain | 59 – 575 | 517 | Virion surface By similarity | ||||||
| Region | 10 – 14 | 5 | Incorporation in virion By similarity | ||||||
| Region | 59 – 140 | 82 | Involved in interaction with F protein By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 77 | 1 | N-linked (GlcNAc...); by host By similarity | ||||||
| Glycosylation | 499 | 1 | N-linked (GlcNAc...); by host By similarity | ||||||
| Glycosylation | 511 | 1 | N-linked (GlcNAc...); by host By similarity | ||||||
| Disulfide bond | 129 | Interchain Potential | |||||||
Natural variations | |||||||||
| Natural variant | 86 | 1 | S → T. | ||||||
| Natural variant | 525 | 1 | Q → K. | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and sequencing of the HN gene of Sendai virus (strain Fushimi)." Neubert W.J., Willenbrink W. Nucleic Acids Res. 18:6427-6427(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein." Heminaway B.R., Yang Y., Tanaka Y., Panin M., Huang Y.T., Galinski M.S. Virus Res. 36:15-35(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [3] | "Kinetics of interactions of sendai virus envelope glycoproteins, F and HN, with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin, and calreticulin." Tomita Y., Yamashita T., Sato H., Taira H. J. Biochem. 126:1090-1100(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHAPERONES. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X56131 Genomic RNA. Translation: CAA39596.1. U06433 Genomic RNA. Translation: AAC54272.1. |
| PIR | S12135. |
3D structure databases | |
| ProteinModelPortal | P19758. |
| SMR | P19758. Positions 144-572. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH83. Glycoside Hydrolase Family 83. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 2.120.10.10. 1 hit. |
| InterPro | IPR000665. Hemagglutn-neuramid. IPR016285. Hemagglutn-neuramid_paramyxo. IPR011040. Sialidases. [Graphical view] |
| Pfam | PF00423. HN. 1 hit. [Graphical view] |
| PIRSF | PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit. |
| SUPFAM | SSF50939. Sialidase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HN_SENDF | ||||||||
| Accession | Primary (citable) accession number: P19758 Secondary accession number(s): Q88413 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |