NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Toshiba/Chanock;
DOI=10.1016/0042-6822(90)90141-D; PubMed=2173260 [NCBI, ExPASy, EBI, Israel, Japan]
Tsurudome M., Bando H., Nishio M., Iwamoto Y., Kawano M., Kondo K., Komada H., Ito Y.;
"Antigenic and structural properties of a paramyxovirus simian virus 41 (SV41) reveal a close relationship with human parainfluenza type 2 virus.";
Virology 179:738-748(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

M62733; AAA47451.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X64275; CAA45568.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36419; HNNZ41.

RefSeq

YP_138509.1; -.

3D structure databases

ModBase

P25180.

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

P25180.

Genome annotation databases

GeneID

3159463; -.

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`	`1 568`	`568`	`Hemagglutinin-neuraminidase.`	`PRO_0000142645`
`TOPO_DOM`	`1 18`	`18`	`Cytoplasmic (Potential).`
`TRANSMEM`	`19 39`	`21`	`Potential.`
`TOPO_DOM`	`40 568`	`529`	`Extracellular (Potential).`
`CARBOHYD`	`44 44`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`111 111`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`268 268`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`280 280`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`382 382`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`513 513`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 568 AA [This is the length of the unprocessed precursor]

Molecular weight: 61733 Da [This is the MW of the unprocessed precursor]

CRC64: 7C09738E2715F548 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGAEGNTNK RTFRAVFRTL IILITLTILA LSAAILYEVT HTSNGSESNN QVFDPTDTLN 

        70         80         90        100        110        120 
AITGNIKSMI ALLNQILYNA AIALPLKIDS TESVLLAAIK DLQFSNPASQ NCSSGGNLLN 

       130        140        150        160        170        180 
DALYINGINQ YLLSNSFAGT VGLGPLLNIP SFIPSATAPG GCTRIPSFSL TKTHWCYSHN 

       190        200        210        220        230        240 
VILAGCADSK ASNQYLAMGI VEQSSADFPF FRTMRTLYLS DGINRKSCSI VAIPGGCALY 

       250        260        270        280        290        300 
CYVATKTEQE DYAATTPSEL RLTFYYYNET LVERTLTIPN VTGNWATLNP AVGSGVYHLG 

       310        320        330        340        350        360 
YLAFPVYGGL IQNSAAWNSQ FGSYFLPQNP AVQCSGSAEQ QINTAKGSYV VNWFSGRLIQ 

       370        380        390        400        410        420 
SAVLVCPLSD QLTDQCRVVL FNNSETMMGA EGRLYTIGGD LYYYQRSSSW WTASLLYKIN 

       430        440        450        460        470        480 
TDFSQGLPPL IEAQWVPTYL VPRPGAQPCS AGNFCPANCI TGVYADVWPM NNPFPAGSSG 

       490        500        510        520        530        540 
VNPNYLFGGA FLWADVARVN PTFYMASATQ YKNTTGFPNS NQKAAYTSTT CFQNTGSKKI 

       550        560 
YCLFIIEMGS SLMGEFQIVP FLREVIIT

P25180 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