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P19758 (HN_SENDF) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemagglutinin-neuraminidase

Short name=HN protein
EC=3.2.1.18
Gene names
Name:HN
OrganismSendai virus (strain Fushimi) (SeV) [Complete proteome]
Taxonomic identifier11195 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRespirovirus
Virus hostCavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Hemagglutinin-neuraminidase
PRO_0000142637

Regions

Topological domain1 – 3737Intravirion By similarity
Transmembrane38 – 5821Helical; By similarity
Topological domain59 – 575517Virion surface By similarity
Region10 – 145Incorporation in virion By similarity
Region59 – 14082Involved in interaction with F protein By similarity

Amino acid modifications

Glycosylation771N-linked (GlcNAc...); by host By similarity
Glycosylation4991N-linked (GlcNAc...); by host By similarity
Glycosylation5111N-linked (GlcNAc...); by host By similarity
Disulfide bond129Interchain Potential

Natural variations

Natural variant861S → T.
Natural variant5251Q → K.

Sequences

Sequence LengthMass (Da)Tools
P19758 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 93FD0532F6147BF6

FASTA57563,348
        10         20         30         40         50         60 
MDGDRGKRDS YWSTSPSGST TKLASGWERS SKVDTWLLIL SFTQWALSIA TVIICIIISA 

        70         80         90        100        110        120 
RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD 

       130        140        150        160        170        180 
VIQMIDKSCS RQELTQLCES TIAVHHAEGI APLEPHSFWR CPVGEPYLSS DPKISLLPGP 

       190        200        210        220        230        240 
SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD 

       250        260        270        280        290        300 
LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGS 

       310        320        330        340        350        360 
TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV 

       370        380        390        400        410        420 
SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR 

       430        440        450        460        470        480 
VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN EECNWYNTCP KECISGVYTD 

       490        500        510        520        530        540 
AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG 

       550        560        570 
KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES 

« Hide

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.
PIRS12135.

3D structure databases

ProteinModelPortalP19758.
SMRP19758. Positions 144-572.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR000665. Hemagglutn-neuramid.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Sialidases.
[Graphical view]
PfamPF00423. HN. 1 hit.
[Graphical view]
PIRSFPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHN_SENDF
AccessionPrimary (citable) accession number: P19758
Secondary accession number(s): Q88413
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries