Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04853

- HN_SENDZ

UniProt

P04853 - HN_SENDZ

Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 activityi

    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.

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. viral entry into host cell Source: UniProtKB-KW
    2. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hemagglutinin, Hydrolase

    Keywords - Biological processi

    Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

    Protein family/group databases

    CAZyiGH83. Glycoside Hydrolase Family 83.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemagglutinin-neuraminidase (EC:3.2.1.18)
    Short name:
    HN protein
    Gene namesi
    Name:HN
    OrganismiSendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
    Taxonomic identifieri11198 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRespirovirus
    Virus hostiCavia cutleri (Guinea pig) [TaxID: 10144]
    Cricetidae sp. (Hamster) [TaxID: 36483]
    Mus musculus (Mouse) [TaxID: 10090]
    Rattus norvegicus (Rat) [TaxID: 10116]

    Subcellular locationi

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

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551C → W: 45% loss of cell surface expression; 88% loss of fusion promotion activity. 1 Publication
    Mutagenesisi77 – 771N → G: Loss of glycosylation. 1 Publication
    Mutagenesisi448 – 4481N → G: No effect. 1 Publication
    Mutagenesisi499 – 4991N → G: Loss of glycosylation; 88% loss of neuraminidase activity. 1 Publication
    Mutagenesisi511 – 5111N → G: Loss of glycosylation; 88% loss of neuraminidase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575Hemagglutinin-neuraminidasePRO_0000142640Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...); by host2 Publications
    Disulfide bondi129 – 129InterchainSequence Analysis
    Glycosylationi499 – 4991N-linked (GlcNAc...); by host2 Publications
    Glycosylationi511 – 5111N-linked (GlcNAc...); by host2 Publications

    Post-translational modificationi

    N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer; composed of disulfide-linked homodimers Probable. Interacts with F protein trimer.2 PublicationsCurated

    Structurei

    3D structure databases

    ProteinModelPortaliP04853.
    SMRiP04853. Positions 144-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3737IntravirionSequence AnalysisAdd
    BLAST
    Topological domaini59 – 575517Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 145Incorporation in virion
    Regioni59 – 14082Interaction with F proteinAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR000665. Hemagglutn-neuramid.
    IPR016285. Hemagglutn-neuramid_paramyxo.
    IPR011040. Sialidases.
    [Graphical view]
    PfamiPF00423. HN. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P04853-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGDRGKRDS YWSTSPSGST TKPASGWERS SKADTWLLIL SFTQWALSIA    50
    TVIICIIISA RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV 100
    NIQSSVQTGI PVLLNKNSRD VIQMIDKSCS RQELTQHCES TIAVHHADGI 150
    APLEPHSFWR CPVGEPYLSS DPEISLLPGP SLLSGSTTIS GCVRLPSLSI 200
    GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD LNPVVSHTYD 250
    INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGR 300
    TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT 350
    KCRTQGCQQV SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT 400
    IPITQNYLGA EGRLLKLGDR VYIYTRSSGW HSQLQIGVLD VSHPLTINWT 450
    PHEALSRPGN KECNWYNKCP KECISGVYTD AYPLSPDAAN VATVTLYANT 500
    SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG KGYCFHIIEI 550
    NQKSLNTLQP MLFKTSIPKL CKAES 575
    Length:575
    Mass (Da):63,410
    Last modified:August 13, 1987 - v1
    Checksum:i721DC135844636CC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231P → L in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
    Natural varianti33 – 331A → V in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
    Natural varianti148 – 1481D → E in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
    Natural varianti238 – 2381F → I.
    Natural varianti405 – 4051Q → E in strain: mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA00878. HNNZSZ.
    A24004. HNNZSH.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A00878. HNNZSZ.
    A24004. HNNZSH.

    3D structure databases

    ProteinModelPortali P04853.
    SMRi P04853. Positions 144-572.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH83. Glycoside Hydrolase Family 83.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR000665. Hemagglutn-neuramid.
    IPR016285. Hemagglutn-neuramid_paramyxo.
    IPR011040. Sialidases.
    [Graphical view ]
    Pfami PF00423. HN. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiHN_SENDZ
    AccessioniPrimary (citable) accession number: P04853
    Secondary accession number(s): P06863, P27562
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3