Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Human parainfluenza 2 virus (strain Toshiba) (HPIV-2)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHemagglutinin, Hydrolase
Biological processHost-virus interaction, Viral attachment to host cell, Virus entry into host cell

Protein family/group databases

CAZyiGH83 Glycoside Hydrolase Family 83

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-neuraminidase (EC:3.2.1.18)
Gene namesi
Name:HN
OrganismiHuman parainfluenza 2 virus (strain Toshiba) (HPIV-2)
Taxonomic identifieri11214 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeRubulavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000472 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 25IntravirionSequence analysisAdd BLAST25
Transmembranei26 – 46HelicalSequence analysisAdd BLAST21
Topological domaini47 – 571Virion surfaceSequence analysisAdd BLAST525

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001426231 – 571Hemagglutinin-neuraminidaseAdd BLAST571

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi272N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi284N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi335N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi341N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi386N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi454N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi498N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi501N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi517N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi522N-linked (GlcNAc...) asparagine; by hostSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP25466

Structurei

3D structure databases

ProteinModelPortaliP25466
SMRiP25466
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni228 – 233Important for neuraminidase activityBy similarity6
Regioni393 – 398Sialic receptor-binding siteCurated6

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19247
OrthoDBiVOG090000BM

Family and domain databases

InterProiView protein in InterPro
IPR016285 Hemagglutn-neuramid
IPR000665 Hemagglutn/HN
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF00423 HN, 1 hit
PIRSFiPIRSF001072 Hemagglut-neuramid_paramyxoV, 1 hit
SUPFAMiSSF50939 SSF50939, 1 hit

Sequencei

Sequence statusi: Complete.

P25466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDYSNLSLK SIPKRTCRII FRTATILGIC TLIVLCSSIL HEIIHLDVSS
60 70 80 90 100
GLMDSDDSQQ GIIQPIIESL KSLIALANQI LYNVAIIIPL KIDSIETVIF
110 120 130 140 150
SALKDMHTGS MSNTNCTPGN LLLHDAAYIN GINKFLVLKS YNGTPKYGPL
160 170 180 190 200
LNIPSFIPSA TSPNGCTRIP SFSLIKTHWC YTHNVMLGDC 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 YGGLISGTPS YNKQSSRYFI PKHPNITCAG NSSEQAAAAR
360 370 380 390 400
SSYVIRYHSN RLIQSAVLIC 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):63,263
Last modified:May 1, 1992 - v1
Checksum:iD7130A3BE6491406
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57559 mRNA Translation: CAA40787.1
PIRiA33777 HNNZP2
RefSeqiNP_598405.1, NC_003443.1

Genome annotation databases

GeneIDi935188
KEGGivg:935188

Similar proteinsi

Entry informationi

Entry nameiHN_PI2HT
AccessioniPrimary (citable) accession number: P25466
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 20, 2018
This is version 107 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health