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Reviewed, UniProtKB/Swiss-Prot Q783Y1 (HN_SENDA)

Last modified January 19, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hemagglutinin-neuraminidase
      Short name=HN protein
    EC=3.2.1.18
Gene names
Name: HN
OrganismSendai virus (strain Hamamatsu) (SeV) [Complete proteome]
Taxonomic identifier302271 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRespirovirus
Virus hostMus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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.

Subcellular location

Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential. Note: Folded in the endoplasmic reticulum By similarity.

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_0000142636

Regions

Topological domain1 – 3737Cytoplasmic By similarity
Transmembrane38 – 5821 By similarity
Topological domain59 – 575517Extracellular 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 variant4611E → G in strain: Isolate E30cl2; egg passage attenuated.
Natural variant4621D → G in strain: Isolate E30cl2, Isolate E50cl9 and Isolate E30M15cl5; egg passage attenuated.

Sequences

Sequence LengthMass (Da)Tools
Q783Y1-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BDA9E1B72431058A

FASTA57563,212
        10         20         30         40         50         60 
MDGDRSKRDS YWSTSPGGST TKLVSDSERS GKVDTWLLIL AFTQWALSIA TVIICIVIAA 

        70         80         90        100        110        120 
RQGYSMERYS MTVEALNTSN KEVKESLTSL IRQEVITRAV NIQSSVQTGI PVLLNKNSRD 

       130        140        150        160        170        180 
VIQLIEKSCN RQELTQLCDS TIAVHHAEGI APLEPHSFWR CPAGEPYLSS DPEVSLLPGP 

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

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

       310        320        330        340        350        360 
TKSHRYSNSE IDLDHPFSAL YPSVGSGIAT EGSLIFLGYG GLTTPLQGDT KCRIQGCQQV 

       370        380        390        400        410        420 
SQDTCNEALK ITWLGGKQVV SVLIQVNDYL SERPRIRVTT VPITQNYLGA EGRLLKLGDQ 

       430        440        450        460        470        480 
VYIYTRSSGW HSQLQIGVLD VSHPLTISWT PHEALSRPGN EDCNWYNTCP KECISGVYTD 

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

       550        560        570 
KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES 

« Hide

References

[1]"A field isolate of Sendai virus: its high virulence to mice and genetic divergence from prototype strains."
Sakaguchi T., Fujii Y., Kiyotani K., Sasaki M., Yoshida T.
Arch. Virol. 135:159-164(1994) [PubMed: 8198441] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Conserved and non-conserved regions in the Sendai virus genome: evolution of a gene possessing overlapping reading frames."
Fujii Y., Kiyotani K., Yoshida T., Sakaguchi T.
Virus Genes 22:47-52(2001) [PubMed: 11210938] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Involvement of the leader sequence in Sendai virus pathogenesis revealed by recovery of a pathogenic field isolate from cDNA."
Fujii Y., Sakaguchi T., Kiyotani K., Huang C., Fukuhara N., Egi Y., Yoshida T.
J. Virol. 76:8540-8547(2002) [PubMed: 12163573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate E15cl2.
[4]"Identification of mutations associated with attenuation of virulence of a field Sendai virus isolate by egg passage."
Fujii Y., Sakaguchi T., Kiyotani K., Huang C., Fukuhara N., Yoshida T.
Virus Genes 25:189-193(2002) [PubMed: 12416681] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate E15cl2, Isolate E30cl2 and Isolate E30M15cl5.
[5]Fujii Y., Kiyotani K., Huang C., Fukuhara N., Egi K., Yoshida T., Sakaguchi T.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate E50cl9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57213 Genomic RNA. Translation: CAA40499.1.
AB039658 Genomic RNA. Translation: BAB20025.1.
AB065186 Genomic RNA. Translation: BAC79131.1.
AB065187 Genomic RNA. Translation: BAC07511.1.
AB065188 Genomic RNA. Translation: BAC79139.1.
AB065189 Genomic RNA. Translation: BAC79147.1.
PIRS14532.

3D structure databases

SMRQ783Y1. Positions 144-572.
ModBaseSearch...

Family and domain databases

InterProIPR000665. Hemagglutn-neuramid_glycoprot.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Neuraminidase.
[Graphical view]
PfamPF00423. HN. 1 hit.
[Graphical view]
PIRSFPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHN_SENDA
AccessionPrimary (citable) accession number: Q783Y1
Secondary accession number(s): Q7T415, Q7TB20, Q82459
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: January 19, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents