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Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SABIO-RKP04853.

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 virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeRespirovirus
Virus hostiCavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 37IntravirionSequence analysisAdd BLAST37
Transmembranei38 – 58Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini59 – 575Virion surfaceSequence analysisAdd BLAST517

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi55C → W: 45% loss of cell surface expression; 88% loss of fusion promotion activity. 1 Publication1
Mutagenesisi77N → G: Loss of glycosylation. 1 Publication1
Mutagenesisi448N → G: No effect. 1 Publication1
Mutagenesisi499N → G: Loss of glycosylation; 88% loss of neuraminidase activity. 1 Publication1
Mutagenesisi511N → G: Loss of glycosylation; 88% loss of neuraminidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001426401 – 575Hemagglutinin-neuraminidaseAdd BLAST575

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi77N-linked (GlcNAc...); by host2 Publications1
Disulfide bondi129InterchainSequence analysis
Glycosylationi499N-linked (GlcNAc...); by host2 Publications1
Glycosylationi511N-linked (GlcNAc...); by host2 Publications1

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

PTM databases

UniCarbKBiP04853.

Interactioni

Subunit structurei

Homotetramer; composed of disulfide-linked homodimers (Probable). Interacts with F protein trimer.Curated2 Publications

Structurei

3D structure databases

ProteinModelPortaliP04853.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 14Incorporation in virion5
Regioni59 – 140Interaction with F proteinAdd BLAST82

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.

P04853-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGDRGKRDS YWSTSPSGST TKPASGWERS SKADTWLLIL SFTQWALSIA
60 70 80 90 100
TVIICIIISA RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV
110 120 130 140 150
NIQSSVQTGI PVLLNKNSRD VIQMIDKSCS RQELTQHCES TIAVHHADGI
160 170 180 190 200
APLEPHSFWR CPVGEPYLSS DPEISLLPGP SLLSGSTTIS GCVRLPSLSI
210 220 230 240 250
GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD LNPVVSHTYD
260 270 280 290 300
INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGR
310 320 330 340 350
TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT
360 370 380 390 400
KCRTQGCQQV SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT
410 420 430 440 450
IPITQNYLGA EGRLLKLGDR VYIYTRSSGW HSQLQIGVLD VSHPLTINWT
460 470 480 490 500
PHEALSRPGN KECNWYNKCP KECISGVYTD AYPLSPDAAN VATVTLYANT
510 520 530 540 550
SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG KGYCFHIIEI
560 570
NQKSLNTLQP MLFKTSIPKL CKAES
Length:575
Mass (Da):63,410
Last modified:August 13, 1987 - v1
Checksum:i721DC135844636CC
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti23P → L in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant. 1
Natural varianti33A → V in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant. 1
Natural varianti148D → E in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant. 1
Natural varianti238F → I.1
Natural varianti405Q → E in strain: mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP04853.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

PTM databases

UniCarbKBiP04853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SABIO-RKP04853.

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...

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: November 2, 2016
This is version 107 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

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 one 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.