[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3003381 [NCBI, ExPASy, EBI, Israel, Japan] Elango N., Coligan J.E., Jambou R.C., Venkatesan S.; "Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: nucleotide sequence of mRNA and limited amino acid sequence of the purified protein."; J. Virol. 57:481-489(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. DOI=10.1016/0168-1702(87)90016-5; PubMed=2825443 [NCBI, ExPASy, EBI, Israel, Japan] Galinski M.S., Mink M.A., Pons M.W.; "Molecular cloning and sequence analysis of the human parainfluenza 3 virus genes encoding the surface glycoproteins, F and HN."; Virus Res. 8:205-215(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2822598 [NCBI, ExPASy, EBI, Israel, Japan] Storey D.G., Cote M.-J., Dimock K., Kang C.Y.; "Nucleotide sequence of the coding and flanking regions of the human parainfluenza virus 3 hemagglutinin-neuraminidase gene: comparison with other paramyxoviruses."; Intervirology 27:69-80(1987).
[4]	VARIANT NEURAMINIDASE-DEFICIENT ASN-216. STRAIN=Isolate C28; DOI=10.1006/viro.1995.9925; PubMed=8525632 [NCBI, ExPASy, EBI, Israel, Japan] Huberman K., Peluso R.W., Moscona A.; "Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle."; Virology 214:294-300(1995).
[5]	VARIANT 4-GU-DANA-RESISTANT ILE-193. STRAIN=Isolate ZM1; DOI=10.1128/JVI.77.1.309-317.2003; PubMed=12477836 [NCBI, ExPASy, EBI, Israel, Japan] Murrell M., Porotto M., Weber T., Greengard O., Moscona A.; "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)."; J. Virol. 77:309-317(2003).

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).
FUNCTION: 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.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 4.7;
SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein (Potential). Cell membrane; Single-pass type II membrane protein (Potential).
SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M17641; AAA46846.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21649; AAA46853.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20402; AAA46856.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27765; HNNZP3.

3D structure databases

SMR

P08492; 142-572.

ModBase

P08492.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0055036;	Cellular component: virion membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR000665; Hemagglutn-neuramid_glycoprot.
IPR016285; Hemagglutn-neuramid_paramyxo.
Graphical view of domain structure.

Pfam

PF00423; HN; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Envelope protein; Glycoprotein; Hemagglutinin; Hydrolase; Membrane; Signal-anchor; Transmembrane; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 572`	`572`	`Hemagglutinin-neuraminidase.`	`PRO_0000142625`
`TOPO_DOM`	`1 31`	`31`	`Cytoplasmic (Potential).`
`TRANSMEM`	`32 52`	`21`	`Potential.`
`TOPO_DOM`	`53 572`	`520`	`Extracellular (Potential).`
`CARBOHYD`	`308 308`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`351 351`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`523 523`		`N-linked (GlcNAc...) (Potential).`
`VARIANT`	`193 193`	`1`	`T -> I (in strain: Isolate ZM1; 4-GU-DANA antiviral drug resistant and increased receptor binding avidity).`
`VARIANT`	`216 216`	`1`	`D -> N (in strain: Isolate C28; 50% loss of neuraminidase activity).`
`VARIANT`	`567 567`	`1`	`I -> V (in strain: Isolate ZM1).`
`CONFLICT`	`135 135`		`Q -> R (in Ref. 2; AAA46853).`
`CONFLICT`	`146 146`		`V -> A (in Ref. 2; AAA46853).`
`CONFLICT`	`489 489`		`S -> G (in Ref. 3; AAA46856).`
`CONFLICT`	`512 512`		`S -> A (in Ref. 2 and 3).`

Sequence information

Length: 572 AA [This is the length of the unprocessed precursor]

Molecular weight: 64247 Da [This is the MW of the unprocessed precursor]

CRC64: BDCA6F9A41E20369 [This is a checksum on the sequence]

        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

P08492 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools