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Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Human parainfluenza 2 virus (HPIV-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (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)
Gene namesi
Name:HN
OrganismiHuman parainfluenza 2 virus (HPIV-2)
Taxonomic identifieri11212 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525IntravirionSequence AnalysisAdd
BLAST
Transmembranei26 – 4621HelicalSequence AnalysisAdd
BLAST
Topological domaini47 – 571525Virion surfaceSequence AnalysisAdd
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 – 571571Hemagglutinin-neuraminidasePRO_0000142622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi272 – 2721N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi386 – 3861N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi454 – 4541N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi498 – 4981N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi501 – 5011N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi517 – 5171N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi522 – 5221N-linked (GlcNAc...); by hostSequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP25465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.

P25465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDYSNLSLK SIPKRTCRII FRTATILGIC TLIVLCSSIL HEIIHLDVSS
60 70 80 90 100
GLMDSDDSQQ GIIQPIIESL KSLIALANQI LYNVAIIIPL KIDSIETVIY
110 120 130 140 150
SALKDMHTGS MSNTNCTPGN LLLHDAAYIN GLNKFLVLKS YNGTPKYGPL
160 170 180 190 200
LNIPSFIPSA TSPNGCTRIP SFSLIKTHWC YTHNVILGDC LDFTTSNQYL
210 220 230 240 250
AMGIIQQSAA AFPIFRTMKT IYLSDGINRK SCSVTAIPGG CVLYCYVATR
260 270 280 290 300
SEKEDYATTD LAELRLAFYY YNDTFIERVI SLPNTTGQWA TINPAVGSGI
310 320 330 340 350
YHLGFILFPV YGGLIKGTPS YNKQSSRYFI PKHPNITCAG KSSEQAAAAR
360 370 380 390 400
SSYVIRYHSN RLLQSAVLIC PLSDMHTARC NLVMFNNSQV MMGAEGRLYV
410 420 430 440 450
IDNNLYYYQR SSSWWSASLF YRINTDFSKG IPPIIEAQWV PSYQVPRPGV
460 470 480 490 500
MPCNATSFCP ANCITGVYAD VWPLNDPEPT SQNALNPNYR FAGAFLRNES
510 520 530 540 550
NRTNPTFYTA SASALLNTTG FNNTNHKAAY TSSTCFKNTG TQKIYCLIII
560 570
EMGSSLLGEF QIIPFLRELI P
Length:571
Mass (Da):63,316
Last modified:May 1, 1992 - v1
Checksum:i56B4DCFA4337F392
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00865 mRNA. Translation: BAA00739.1.
PIRiA34767. HNNZT2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00865 mRNA. Translation: BAA00739.1.
PIRiA34767. HNNZT2.

3D structure databases

ProteinModelPortaliP25465.
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. "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].

Entry informationi

Entry nameiHN_PI2H
AccessioniPrimary (citable) accession number: P25465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 86 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

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.