Reviewed, UniProtKB/Swiss-Prot P08492 (HN_PI3H4)

Names and origin

Protein names

Recommended name:
    Hemagglutinin-neuraminidase
    EC=3.2.1.18

Gene names

Name:

HN

Organism

Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human parainfluenza 3 virus (strain NIH 47885))

Taxonomic identifier

11217 [NCBI]

Taxonomic lineage

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

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	572 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 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 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 proteinPotential. Cell membrane; Single-pass type II membrane proteinPotential.
Sequence similarities	Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.7.

Ontologies

Keywords
Cellular component	Cell membrane Envelope protein Membrane Virion
Domain	Signal-anchor Transmembrane
Molecular function	Hemagglutinin Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	viral infectious cycle Inferred from electronic annotation. Source: InterPro
Cellular component	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: InterPro virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: InterPro 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 – 572	572	Hemagglutinin-neuraminidase		PRO_0000142625
Regions
	Topological domain	1 – 31	31	Cytoplasmic Potential
	Transmembrane	32 – 52	21	Potential
	Topological domain	53 – 572	520	Extracellular Potential
Amino acid modifications
	Glycosylation	308	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	523	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	193	1	T → I in strain: Isolate ZM1; 4-GU-DANA antiviral drug resistant and increased receptor binding avidity. Ref.5
	Natural variant	216	1	D → N in strain: Isolate C28; 50% loss of neuraminidase activity. Ref.4
	Natural variant	567	1	I → V in strain: Isolate ZM1.
Experimental info
	Sequence conflict	135	1	Q → R in AAA46853. Ref.2
	Sequence conflict	146	1	V → A in AAA46853. Ref.2
	Sequence conflict	489	1	S → G in AAA46856. Ref.3
	Sequence conflict	512	1	S → A Ref.2
	Sequence conflict	512	1	S → A Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P08492-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: BDCA6F9A41E20369	FASTA	572	64,247
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	M17641 mRNA. Translation: AAA46846.1. M21649 Genomic RNA. Translation: AAA46853.1. M20402 mRNA. Translation: AAA46856.1.
PIR	HNNZP3. A27765.
3D structure databases
SMR	P08492. Positions 142-572.
ModBase	Search...
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_PI3H4

Accession

Primary (citable) accession number: P08492

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)