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P25465 (HN_PI2H) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 namesRecommended name:
Hemagglutinin-neuraminidase

EC=3.2.1.18
Gene names
Name:HN
OrganismHuman parainfluenza 2 virus (HPIV-2)
Taxonomic identifier11212 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Hemagglutinin-neuraminidase
PRO_0000142622

Regions

Topological domain1 – 2525Intravirion Potential
Transmembrane26 – 4621Helical; Potential
Topological domain47 – 571525Virion surface Potential

Amino acid modifications

Glycosylation2721N-linked (GlcNAc...); by host Potential
Glycosylation2841N-linked (GlcNAc...); by host Potential
Glycosylation3351N-linked (GlcNAc...); by host Potential
Glycosylation3861N-linked (GlcNAc...); by host Potential
Glycosylation4541N-linked (GlcNAc...); by host Potential
Glycosylation4981N-linked (GlcNAc...); by host Potential
Glycosylation5011N-linked (GlcNAc...); by host Potential
Glycosylation5171N-linked (GlcNAc...); by host Potential
Glycosylation5221N-linked (GlcNAc...); by host Potential

Sequences

Sequence LengthMass (Da)Tools
P25465 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 56B4DCFA4337F392

FASTA57163,316
        10         20         30         40         50         60 
MEDYSNLSLK SIPKRTCRII FRTATILGIC TLIVLCSSIL HEIIHLDVSS GLMDSDDSQQ 

        70         80         90        100        110        120 
GIIQPIIESL KSLIALANQI LYNVAIIIPL KIDSIETVIY SALKDMHTGS MSNTNCTPGN 

       130        140        150        160        170        180 
LLLHDAAYIN GLNKFLVLKS YNGTPKYGPL LNIPSFIPSA TSPNGCTRIP SFSLIKTHWC 

       190        200        210        220        230        240 
YTHNVILGDC LDFTTSNQYL AMGIIQQSAA AFPIFRTMKT IYLSDGINRK SCSVTAIPGG 

       250        260        270        280        290        300 
CVLYCYVATR SEKEDYATTD LAELRLAFYY YNDTFIERVI SLPNTTGQWA TINPAVGSGI 

       310        320        330        340        350        360 
YHLGFILFPV YGGLIKGTPS YNKQSSRYFI PKHPNITCAG KSSEQAAAAR SSYVIRYHSN 

       370        380        390        400        410        420 
RLLQSAVLIC PLSDMHTARC NLVMFNNSQV MMGAEGRLYV IDNNLYYYQR SSSWWSASLF 

       430        440        450        460        470        480 
YRINTDFSKG IPPIIEAQWV PSYQVPRPGV MPCNATSFCP ANCITGVYAD VWPLNDPEPT 

       490        500        510        520        530        540 
SQNALNPNYR FAGAFLRNES NRTNPTFYTA SASALLNTTG FNNTNHKAAY TSSTCFKNTG 

       550        560        570 
TQKIYCLIII EMGSSLLGEF QIIPFLRELI P 

« Hide

References

[1]"Sequence analysis of the HN gene of parainfluenza virus type 2."
Precious B., Southern J.A., Randall R.E.
J. Gen. Virol. 71:1163-1168(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00865 mRNA. Translation: BAA00739.1.
PIRHNNZT2. A34767.

3D structure databases

ProteinModelPortalP25465.
ModBaseSearch...
MobiDBSearch...

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_PI2H
AccessionPrimary (citable) accession number: P25465
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 81 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries