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UniProtKB/Swiss-Prot entry P04853


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HN_SENDZ
Primary accession number P04853
Secondary accession numbers P06863 P27562
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 63)
Name and origin of the protein
Protein name Hemagglutinin-neuraminidase
Synonyms HN protein
EC 3.2.1.18
Gene name
Name: HN
From
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) [TaxID: 11198] 
Taxonomy Viruses; ssRNA negative-strand viruses; Mononegavirales; Paramyxoviridae; Paramyxovirinae; Respirovirus.
Virus hosts Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1016/0014-5793(85)80885-1; PubMed=2991016 [NCBI, ExPASy, EBI, Israel, Japan]
Miura N., Nakatani Y., Ishiura M., Uchida T., Okada Y.;
"Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus.";
FEBS Lett. 188:112-116(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1093/nar/14.4.1545; PubMed=3005975 [NCBI, ExPASy, EBI, Israel, Japan]
Shioda T., Iwasaki K., Shibuta H.;
"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.";
Nucleic Acids Res. 14:1545-1563(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R, and Mutant ts-f1;
DOI=10.1016/0042-6822(90)90040-X; PubMed=2161155 [NCBI, ExPASy, EBI, Israel, Japan]
Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E., Klenk H.-D., Rott R., Seto J.T.;
"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus.";
Virology 176:656-657(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R / T-5 revertant;
DOI=10.1016/0042-6822(91)90839-4; PubMed=1651590 [NCBI, ExPASy, EBI, Israel, Japan]
Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R., Seto J.T.;
"Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus.";
Virology 184:227-234(1991).
[5]
BINDING TO SIALIC ACID-CONTAINING CELL RECEPTORS.
PubMed=6255459 [NCBI, ExPASy, EBI, Israel, Japan]
Markwell M.A.K., Paulson J.C.;
"Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants.";
Proc. Natl. Acad. Sci. U.S.A. 77:5693-5697(1980).
[6]
GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511.
PubMed=6263875 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshima H., Nakanishi M., Okada Y., Kobata A.;
"Carbohydrate structures of HVJ (Sendai virus) glycoproteins.";
J. Biol. Chem. 256:5355-5361(1981).
[7]
MUTAGENESIS OF CYS-55.
DOI=10.1006/viro.1994.1564; PubMed=7941317 [NCBI, ExPASy, EBI, Israel, Japan]
Bousse T., Takimoto T., Gorman W.L., Takahashi T., Portner A.;
"Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion.";
Virology 204:506-514(1994).
[8]
INTERACTION WITH F PROTEIN.
PubMed=8709235 [NCBI, ExPASy, EBI, Israel, Japan]
Tanabayashi K., Compans R.W.;
"Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion.";
J. Virol. 70:6112-6118(1996).
[9]
INCORPORATION IN THE VIRION.
PubMed=9811709 [NCBI, ExPASy, EBI, Israel, Japan]
Takimoto T., Bousse T., Coronel E.C., Scroggs R.A., Portner A.;
"Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions.";
J. Virol. 72:9747-9754(1998).
[10]
GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511, AND MUTAGENESIS OF ASN-77; ASN-448; ASN-499 AND ASN-511.
PubMed=10876159 [NCBI, ExPASy, EBI, Israel, Japan]
Segawa H., Yamashita T., Kawakita M., Taira H.;
"Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein.";
J. Biochem. 128:65-72(2000).
[11]
INTERACTION WITH M PROTEIN.
DOI=10.1006/viro.2000.0556; PubMed=11040121 [NCBI, ExPASy, EBI, Israel, Japan]
Ali A., Nayak D.P.;
"Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein.";
Virology 276:289-303(2000).
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.
  • FUNCTION: 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: Homotetramer; composed of disulfide-linked homodimers (Probable). Interacts with F protein trimer.
  • SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein (Potential). Cell membrane; Single-pass type II membrane protein (Potential). Note=Folded in the endoplasmic reticulum (By similarity).
  • PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides.
  • SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03614; CAA27274.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30202; AAB06282.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30203; AAB06288.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30204; AAB06200.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M69046; AAB06294.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02808; CAA26576.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00878; HNNZSZ.
A24004; HNNZSH.
3D structure databases
ModBase P04853.
PTM databases
GlycoSuiteDB P04853; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0055036; Cellular component: virion membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR000665; Hemagglutn-neuramid_glycoprot.
IPR016285; Hemagglutn-neuramid_paramyxo.
Graphical view of domain structure.
Pfam PF00423; HN; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
BLOCKS P04853.
ProtoNet P04853.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Envelope protein; Glycoprotein; Hemagglutinin; Hydrolase; Membrane; Signal-anchor; Transmembrane; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   575  575     Hemagglutinin-neuraminidase. PRO_0000142640
TOPO_DOM   1    37  37     Cytoplasmic (Potential). 
TRANSMEM   38    58  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   59   575  517     Extracellular (Potential). 
REGION   10    14  5     Incorporation in virion. 
REGION   59   140  82     Interaction with F protein. 
CARBOHYD   77    77        N-linked (GlcNAc...). 
CARBOHYD   499   499        N-linked (GlcNAc...). 
CARBOHYD   511   511        N-linked (GlcNAc...). 
DISULFID   129   129        Interchain (Potential). 
VARIANT   23    23  1     P -> L (in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant). 
VARIANT   33    33  1     A -> V (in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant). 
VARIANT   148   148  1     D -> E (in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant). 
VARIANT   238   238  1     F -> I. 
VARIANT   405   405  1     Q -> E (in strain: mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant). 
MUTAGEN   55    55        C->W: 45% loss of cell surface expression; 88% loss of fusion promotion activity. 
MUTAGEN   77    77        N->G: Loss of glycosylation. 
MUTAGEN   448   448        N->G: No effect. 
MUTAGEN   499   499        N->G: Loss of glycosylation; 88% loss of neuraminidase activity. 
MUTAGEN   511   511        N->G: Loss of glycosylation; 88% loss of neuraminidase activity. 
Sequence information
Length: 575 AA [This is the length of the unprocessed precursor] Molecular weight: 63410 Da [This is the MW of the unprocessed precursor] CRC64: 721DC135844636CC [This is a checksum on the sequence]
        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 

P04853 in FASTA format

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