[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2161050 [NCBI, ExPASy, EBI, Israel, Japan] Precious B., Southern J.A., Randall R.E.; "Sequence analysis of the HN gene of parainfluenza virus type 2."; J. Gen. Virol. 71:1163-1168(1990).

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.
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

D00865; BAA00739.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34767; HNNZT2.

3D structure databases

ModBase

P25465.

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:0019031;	Cellular component: viral envelope (inferred from electronic annotation from InterPro).
GO:0055036;	Cellular component: virion membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004308;	Molecular function: exo-alpha-sialidase activity (inferred from electronic annotation from InterPro).
GO:0046789;	Molecular function: host cell surface receptor binding (inferred from electronic annotation from InterPro).
GO:0019058;	Biological process: viral infectious cycle (inferred from electronic annotation from InterPro).
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.

ProtoNet

P25465.

Other

UniRef

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`	`1 571`	`571`	`Hemagglutinin-neuraminidase.`	`PRO_0000142622`
`TOPO_DOM`	`1 25`	`25`	`Cytoplasmic (Potential).`
`TRANSMEM`	`26 46`	`21`	`Potential.`
`TOPO_DOM`	`47 571`	`525`	`Extracellular (Potential).`
`CARBOHYD`	`272 272`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`284 284`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`335 335`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`386 386`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`454 454`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`498 498`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`501 501`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`517 517`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`522 522`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 571 AA [This is the length of the unprocessed precursor]

Molecular weight: 63316 Da [This is the MW of the unprocessed precursor]

CRC64: 56B4DCFA4337F392 [This is a checksum on the sequence]

        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

P25465 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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