Reviewed, UniProtKB/Swiss-Prot P04853 (HN_SENDZ)

Names and origin

Protein names

Recommended name:
    Hemagglutinin-neuraminidase
      Short name=HN protein
    EC=3.2.1.18

Gene names

Name:

HN

Organism

Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)) [Complete proteome]

Taxonomic identifier

11198 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Respirovirus

Virus host

Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins.
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.
Subunit structure	Homotetramer; composed of disulfide-linked homodimers Probable. Interacts with F protein trimer.
Subcellular location	Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential. Note: Folded in the endoplasmic reticulum By similarity.
Post-translational modification	N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. Ref.6 Ref.10
Sequence similarities	Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Ontologies

Keywords
Cellular component	Cell membrane Envelope protein Membrane Virion
Domain	Signal-anchor Transmembrane
Molecular function	Hemagglutinin Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	viral infectious cycle Inferred from electronic annotation. Source: InterPro
Cellular component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: EC host cell surface receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	Hemagglutinin-neuraminidase		PRO_0000142640
Regions
	Topological domain	1 – 37	37	Cytoplasmic Potential
	Transmembrane	38 – 58	21	Signal-anchor for type II membrane protein Potential
	Topological domain	59 – 575	517	Extracellular Potential
	Region	10 – 14	5	Incorporation in virion
	Region	59 – 140	82	Interaction with F protein
Amino acid modifications
	Glycosylation	77	1	N-linked (GlcNAc...); by host Ref.6 Ref.10
	Glycosylation	499	1	N-linked (GlcNAc...); by host Ref.6 Ref.10
	Glycosylation	511	1	N-linked (GlcNAc...); by host Ref.6 Ref.10
	Disulfide bond	129		Interchain Potential
Natural variations
	Natural variant	23	1	P → L in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
	Natural variant	33	1	A → V in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
	Natural variant	148	1	D → E in strain: wild-type, mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
	Natural variant	238	1	F → I
	Natural variant	405	1	Q → E in strain: mutant F1-R, mutant ts-f1 and mutant F1-R / T-5 revertant.
Experimental info
	Mutagenesis	55	1	C → W: 45% loss of cell surface expression; 88% loss of fusion promotion activity. Ref.7
	Mutagenesis	77	1	N → G: Loss of glycosylation. Ref.10
	Mutagenesis	448	1	N → G: No effect. Ref.10
	Mutagenesis	499	1	N → G: Loss of glycosylation; 88% loss of neuraminidase activity. Ref.10
	Mutagenesis	511	1	N → G: Loss of glycosylation; 88% loss of neuraminidase activity. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P04853-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 721DC135844636CC	FASTA	575	63,410
	10 20 30 40 50 60 MDGDRGKRDS YWSTSPSGST TKPASGWERS SKADTWLLIL SFTQWALSIA TVIICIIISA 70 80 90 100 110 120 RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD 130 140 150 160 170 180 VIQMIDKSCS RQELTQHCES TIAVHHADGI APLEPHSFWR CPVGEPYLSS DPEISLLPGP 190 200 210 220 230 240 SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD 250 260 270 280 290 300 LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGR 310 320 330 340 350 360 TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV 370 380 390 400 410 420 SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR 430 440 450 460 470 480 VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN KECNWYNKCP KECISGVYTD 490 500 510 520 530 540 AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG 550 560 570 KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES

References

[1]	"Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus." Miura N., Nakatani Y., Ishiura M., Uchida T., Okada Y. FEBS Lett. 188:112-116(1985) [PubMed: 2991016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins." Shioda T., Iwasaki K., Shibuta H. Nucleic Acids Res. 14:1545-1563(1986) [PubMed: 3005975] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus." Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E., Klenk H.-D., Rott R., Seto J.T. Virology 176:656-657(1990) [PubMed: 2161155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Mutant F1-R and Mutant ts-f1.
[4]	"Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus." Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R., Seto J.T. Virology 184:227-234(1991) [PubMed: 1651590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Mutant F1-R / T-5 revertant.
[5]	"Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants." Markwell M.A.K., Paulson J.C. Proc. Natl. Acad. Sci. U.S.A. 77:5693-5697(1980) [PubMed: 6255459] [Abstract] Cited for: BINDING TO SIALIC ACID-CONTAINING CELL RECEPTORS.
[6]	"Carbohydrate structures of HVJ (Sendai virus) glycoproteins." Yoshima H., Nakanishi M., Okada Y., Kobata A. J. Biol. Chem. 256:5355-5361(1981) [PubMed: 6263875] [Abstract] Cited for: GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511.
[7]	"Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion." Bousse T., Takimoto T., Gorman W.L., Takahashi T., Portner A. Virology 204:506-514(1994) [PubMed: 7941317] [Abstract] Cited for: MUTAGENESIS OF CYS-55.
[8]	"Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion." Tanabayashi K., Compans R.W. J. Virol. 70:6112-6118(1996) [PubMed: 8709235] [Abstract] Cited for: INTERACTION WITH F PROTEIN.
[9]	"Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions." Takimoto T., Bousse T., Coronel E.C., Scroggs R.A., Portner A. J. Virol. 72:9747-9754(1998) [PubMed: 9811709] [Abstract] Cited for: INCORPORATION IN THE VIRION.
[10]	"Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein." Segawa H., Yamashita T., Kawakita M., Taira H. J. Biochem. 128:65-72(2000) [PubMed: 10876159] [Abstract] Cited for: GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511, MUTAGENESIS OF ASN-77; ASN-448; ASN-499 AND ASN-511.
[11]	"Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein." Ali A., Nayak D.P. Virology 276:289-303(2000) [PubMed: 11040121] [Abstract] Cited for: INTERACTION WITH M PROTEIN.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03614 Genomic RNA. Translation: CAA27274.1. M30202 Genomic RNA. Translation: AAB06282.1. M30203 Genomic RNA. Translation: AAB06288.1. M30204 Genomic RNA. Translation: AAB06200.1. M69046 Genomic RNA. Translation: AAB06294.1. X02808 mRNA. Translation: CAA26576.1.
PIR	HNNZSZ. A00878. HNNZSH. A24004.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH83. Glycoside Hydrolase Family 83.
PTM databases
GlycoSuiteDB	P04853.
Family and domain databases
InterPro	IPR000665. Hemagglutn-neuramid_glycoprot. IPR016285. Hemagglutn-neuramid_paramyxo. [Graphical view]
Pfam	PF00423. HN. 1 hit. [Graphical view]
PIRSF	PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HN_SENDZ

Accession

Primary (citable) accession number: P04853
Secondary accession number(s): P06863, P27562

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)