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Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Sendai virus (strain Hamamatsu) (SeV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity).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 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-neuraminidase (EC:3.2.1.18)
Short name:
HN protein
Gene namesi
Name:HN
OrganismiSendai virus (strain Hamamatsu) (SeV)
Taxonomic identifieri302271 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA 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]
ProteomesiUP000008857 Componenti: Genome UP000008510 Componenti: Genome UP000007191 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3737IntravirionBy similarityAdd
BLAST
Transmembranei38 – 5821HelicalBy similarityAdd
BLAST
Topological domaini59 – 575517Virion surfaceBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Hemagglutinin-neuraminidasePRO_0000142636Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer; composed of disulfide-linked homodimers. Interacts with F protein trimer (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ783Y1.
SMRiQ783Y1. Positions 144-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 145Incorporation in virionBy similarity
Regioni59 – 14082Involved in interaction with F proteinBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q783Y1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGDRSKRDS YWSTSPGGST TKLVSDSERS GKVDTWLLIL AFTQWALSIA
60 70 80 90 100
TVIICIVIAA RQGYSMERYS MTVEALNTSN KEVKESLTSL IRQEVITRAV
110 120 130 140 150
NIQSSVQTGI PVLLNKNSRD VIQLIEKSCN RQELTQLCDS TIAVHHAEGI
160 170 180 190 200
APLEPHSFWR CPAGEPYLSS DPEVSLLPGP SLLSGSTTIS GCVRLPSLSI
210 220 230 240 250
GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD LNPVVSHTYD
260 270 280 290 300
INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDILDLKGR
310 320 330 340 350
TKSHRYSNSE IDLDHPFSAL YPSVGSGIAT EGSLIFLGYG GLTTPLQGDT
360 370 380 390 400
KCRIQGCQQV SQDTCNEALK ITWLGGKQVV SVLIQVNDYL SERPRIRVTT
410 420 430 440 450
VPITQNYLGA EGRLLKLGDQ VYIYTRSSGW HSQLQIGVLD VSHPLTISWT
460 470 480 490 500
PHEALSRPGN EDCNWYNTCP KECISGVYTD AYPLSPDAAN VATVTLYANT
510 520 530 540 550
SRVNPTIMYS NTTNIINMLR IKDVKLEAAY TTTSCITHFG KGYCFHIIEI
560 570
NQKSLNTLQP MLFKTSIPKL CKAES
Length:575
Mass (Da):63,212
Last modified:July 5, 2004 - v1
Checksum:iBDA9E1B72431058A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611E → G in strain: Isolate E30cl2; egg passage attenuated.
Natural varianti462 – 4621D → G in strain: Isolate E30cl2, Isolate E50cl9 and Isolate E30M15cl5; egg passage attenuated.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS14532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS14532.

3D structure databases

ProteinModelPortaliQ783Y1.
SMRiQ783Y1. Positions 144-572.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiHN_SENDA
AccessioniPrimary (citable) accession number: Q783Y1
Secondary accession number(s): Q7T415, Q7TB20, Q82459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.