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P04853 (HN_SENDZ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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 Z) (SeV) (Sendai virus (strain HVJ))
Taxonomic identifier11198 [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.

Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins.

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 Probable. Interacts with F protein trimer. Ref.8 Ref.11

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. Ref.6 Ref.10

Sequence similarities

Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Hemagglutinin-neuraminidase
PRO_0000142640

Regions

Topological domain1 – 3737Intravirion Potential
Transmembrane38 – 5821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain59 – 575517Virion surface Potential
Region10 – 145Incorporation in virion
Region59 – 14082Interaction with F protein

Amino acid modifications

Glycosylation771N-linked (GlcNAc...); by host Ref.6 Ref.10
Glycosylation4991N-linked (GlcNAc...); by host Ref.6 Ref.10
Glycosylation5111N-linked (GlcNAc...); by host Ref.6 Ref.10
Disulfide bond129Interchain Potential

Natural variations

Natural variant231P → L in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
Natural variant331A → V in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
Natural variant1481D → E in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
Natural variant2381F → I.
Natural variant4051Q → E in strain: mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.

Experimental info

Mutagenesis551C → W: 45% loss of cell surface expression; 88% loss of fusion promotion activity. Ref.7
Mutagenesis771N → G: Loss of glycosylation. Ref.10
Mutagenesis4481N → G: No effect. Ref.10
Mutagenesis4991N → G: Loss of glycosylation; 88% loss of neuraminidase activity. Ref.10
Mutagenesis5111N → G: Loss of glycosylation; 88% loss of neuraminidase activity. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P04853 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 721DC135844636CC

FASTA57563,410
        10         20         30         40         50         60 
MDGDRGKRDS YWSTSPSGST TKPASGWERS SKADTWLLIL SFTQWALSIA TVIICIIISA 

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

       130        140        150        160        170        180 
VIQMIDKSCS RQELTQHCES TIAVHHADGI APLEPHSFWR CPVGEPYLSS DPEISLLPGP 

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

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

       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 KECNWYNKCP KECISGVYTD 

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

       550        560        570 
KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES 

« Hide

References

[1]"Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus."
Miura N., Nakatani Y., Ishiura M., Uchida T., Okada Y.
FEBS Lett. 188:112-116(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins."
Shioda T., Iwasaki K., Shibuta H.
Nucleic Acids Res. 14:1545-1563(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus."
Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E., Klenk H.-D., Rott R., Seto J.T.
Virology 176:656-657(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Mutant F1-R and Mutant ts-f1.
[4]"Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus."
Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R., Seto J.T.
Virology 184:227-234(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Mutant F1-R / T-5 revertant.
[5]"Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants."
Markwell M.A.K., Paulson J.C.
Proc. Natl. Acad. Sci. U.S.A. 77:5693-5697(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO SIALIC ACID-CONTAINING CELL RECEPTORS.
[6]"Carbohydrate structures of HVJ (Sendai virus) glycoproteins."
Yoshima H., Nakanishi M., Okada Y., Kobata A.
J. Biol. Chem. 256:5355-5361(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511.
[7]"Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion."
Bousse T., Takimoto T., Gorman W.L., Takahashi T., Portner A.
Virology 204:506-514(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-55.
[8]"Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion."
Tanabayashi K., Compans R.W.
J. Virol. 70:6112-6118(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH F PROTEIN.
[9]"Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions."
Takimoto T., Bousse T., Coronel E.C., Scroggs R.A., Portner A.
J. Virol. 72:9747-9754(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INCORPORATION IN THE VIRION.
[10]"Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein."
Segawa H., Yamashita T., Kawakita M., Taira H.
J. Biochem. 128:65-72(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511, MUTAGENESIS OF ASN-77; ASN-448; ASN-499 AND ASN-511.
[11]"Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein."
Ali A., Nayak D.P.
Virology 276:289-303(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH M PROTEIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03614 Genomic RNA. Translation: CAA27274.1.
M30202 Genomic RNA. Translation: AAB06282.1.
M30203 Genomic RNA. Translation: AAB06288.1.
M30204 Genomic RNA. Translation: AAB06200.1.
M69046 Genomic RNA. Translation: AAB06294.1.
X02808 mRNA. Translation: CAA26576.1.
PIRHNNZSZ. A00878.
HNNZSH. A24004.

3D structure databases

ProteinModelPortalP04853.
SMRP04853. 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_SENDZ
AccessionPrimary (citable) accession number: P04853
Secondary accession number(s): P06863, P27562
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 96 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