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P08492 (HN_PI3H4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 attributes

Sequence length572 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 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 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.

Subcellular location

Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.7.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Hemagglutinin-neuraminidase
PRO_0000142625

Regions

Topological domain1 – 3131Intravirion Potential
Transmembrane32 – 5221Helical; Potential
Topological domain53 – 572520Virion surface Potential

Amino acid modifications

Glycosylation3081N-linked (GlcNAc...); by host Potential
Glycosylation3511N-linked (GlcNAc...); by host Potential
Glycosylation5231N-linked (GlcNAc...); by host Potential

Natural variations

Natural variant1931T → I in strain: Isolate ZM1; 4-GU-DANA antiviral drug resistant and increased receptor binding avidity. Ref.5
Natural variant2161D → N in strain: Isolate C28; 50% loss of neuraminidase activity. Ref.4
Natural variant5671I → V in strain: Isolate ZM1.

Experimental info

Sequence conflict1351Q → R in AAA46853. Ref.2
Sequence conflict1461V → A in AAA46853. Ref.2
Sequence conflict4891S → G in AAA46856. Ref.3
Sequence conflict5121S → A Ref.2
Sequence conflict5121S → A Ref.3

Secondary structure

................................................................................... 572
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08492 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: BDCA6F9A41E20369

FASTA57264,247
        10         20         30         40         50         60 
MEYWKHTNHG KDAGNELETS MATHGNKITN KITYILWTII LVLLSIVFII VLINSIKSEK 

        70         80         90        100        110        120 
AHESLLQDVN NEFMEVTEKI QMASDNINDL IQSGVNTRLL TIQSHVQNYI PISLTQQMSD 

       130        140        150        160        170        180 
LRKFISEITI RNDNQEVPPQ RITHDVGIKP LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL 

       190        200        210        220        230        240 
LAMPTTVDGC VRTPSLVIND LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN 

       250        260        270        280        290        300 
PRISHTFNIN DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNHDGSIS 

       310        320        330        340        350        360 
TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPINENAIC NTTGCPGKTQ 

       370        380        390        400        410        420 
RDCNQASHSP WFSDRRMVNS IIVVDKGLNS IPKLKVWTIS MRQNYWGSEG RLLLLGNKIY 

       430        440        450        460        470        480 
IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT WHNVLSRPGN NECPWGHSCP DGCITGVYTD 

       490        500        510        520        530        540 
AYPLNPTGSI VSSVILDSQK SRVNPVITYS TSTERVNELA IRNKTLSAGY TTTSCITHYN 

       550        560        570 
KGYCFHIVEI NHKSLDTFQP MLFKTEIPKS CS 

« Hide

References

[1]"Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: nucleotide sequence of mRNA and limited amino acid sequence of the purified protein."
Elango N., Coligan J.E., Jambou R.C., Venkatesan S.
J. Virol. 57:481-489(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and sequence analysis of the human parainfluenza 3 virus genes encoding the surface glycoproteins, F and HN."
Galinski M.S., Mink M.A., Pons M.W.
Virus Res. 8:205-215(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Nucleotide sequence of the coding and flanking regions of the human parainfluenza virus 3 hemagglutinin-neuraminidase gene: comparison with other paramyxoviruses."
Storey D.G., Cote M.-J., Dimock K., Kang C.Y.
Intervirology 27:69-80(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle."
Huberman K., Peluso R.W., Moscona A.
Virology 214:294-300(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NEURAMINIDASE-DEFICIENT ASN-216.
Strain: Isolate C28.
[5]"Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (Zanamivir)."
Murrell M., Porotto M., Weber T., Greengard O., Moscona A.
J. Virol. 77:309-317(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT 4-GU-DANA-RESISTANT ILE-193.
Strain: Isolate ZM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17641 mRNA. Translation: AAA46846.1.
M21649 Genomic RNA. Translation: AAA46853.1.
M20402 mRNA. Translation: AAA46856.1.
PIRHNNZP3. A27765.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4MZAX-ray1.65A/B136-572[»]
4MZEX-ray1.80A/B136-572[»]
ProteinModelPortalP08492.
SMRP08492. Positions 142-572.
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_PI3H4
AccessionPrimary (citable) accession number: P08492
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 94 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries