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P08492

- HN_PI3H4

UniProt

P08492 - HN_PI3H4

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Protein

Hemagglutinin-neuraminidase

Gene

HN

Organism
Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human parainfluenza 3 virus (strain NIH 47885))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).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 activityi

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.

pH dependencei

Optimum pH is 4.7.

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

GO - Biological processi

  1. viral entry into host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-neuraminidase (EC:3.2.1.18)
Gene namesi
Name:HN
OrganismiHuman parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human parainfluenza 3 virus (strain NIH 47885))
Taxonomic identifieri11217 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRespirovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3131IntravirionSequence AnalysisAdd
BLAST
Transmembranei32 – 5221HelicalSequence AnalysisAdd
BLAST
Topological domaini53 – 572520Virion surfaceSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Hemagglutinin-neuraminidasePRO_0000142625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi308 – 3081N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi523 – 5231N-linked (GlcNAc...); by hostSequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi148 – 1503Combined sources
Helixi153 – 1564Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi203 – 21513Combined sources
Beta strandi221 – 23111Combined sources
Beta strandi235 – 24713Combined sources
Turni249 – 2513Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi264 – 2707Combined sources
Helixi276 – 2816Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi299 – 3046Combined sources
Helixi306 – 3083Combined sources
Beta strandi309 – 3135Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi331 – 34212Combined sources
Helixi360 – 3667Combined sources
Helixi370 – 3723Combined sources
Beta strandi377 – 38610Combined sources
Helixi388 – 3903Combined sources
Beta strandi392 – 3987Combined sources
Turni401 – 4033Combined sources
Beta strandi410 – 4156Combined sources
Beta strandi418 – 4236Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi446 – 4494Combined sources
Beta strandi461 – 4633Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi488 – 4969Combined sources
Beta strandi498 – 5036Combined sources
Beta strandi505 – 5139Combined sources
Beta strandi515 – 5228Combined sources
Beta strandi526 – 53813Combined sources
Beta strandi541 – 55212Combined sources
Turni553 – 5564Combined sources
Beta strandi557 – 56610Combined sources
Beta strandi569 – 5713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MZAX-ray1.65A/B136-572[»]
4MZEX-ray1.80A/B136-572[»]
ProteinModelPortaliP08492.
SMRiP08492. Positions 142-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR000665. Hemagglutn-neuramid.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

P08492-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYWKHTNHG KDAGNELETS MATHGNKITN KITYILWTII LVLLSIVFII
60 70 80 90 100
VLINSIKSEK AHESLLQDVN NEFMEVTEKI QMASDNINDL IQSGVNTRLL
110 120 130 140 150
TIQSHVQNYI PISLTQQMSD LRKFISEITI RNDNQEVPPQ RITHDVGIKP
160 170 180 190 200
LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL LAMPTTVDGC VRTPSLVIND
210 220 230 240 250
LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN PRISHTFNIN
260 270 280 290 300
DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNHDGSIS
310 320 330 340 350
TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPINENAIC
360 370 380 390 400
NTTGCPGKTQ RDCNQASHSP WFSDRRMVNS IIVVDKGLNS IPKLKVWTIS
410 420 430 440 450
MRQNYWGSEG RLLLLGNKIY IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT
460 470 480 490 500
WHNVLSRPGN NECPWGHSCP DGCITGVYTD AYPLNPTGSI VSSVILDSQK
510 520 530 540 550
SRVNPVITYS TSTERVNELA IRNKTLSAGY TTTSCITHYN KGYCFHIVEI
560 570
NHKSLDTFQP MLFKTEIPKS CS
Length:572
Mass (Da):64,247
Last modified:August 1, 1988 - v1
Checksum:iBDCA6F9A41E20369
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351Q → R in AAA46853. (PubMed:2825443)Curated
Sequence conflicti146 – 1461V → A in AAA46853. (PubMed:2825443)Curated
Sequence conflicti489 – 4891S → G in AAA46856. (PubMed:2822598)Curated
Sequence conflicti512 – 5121S → A(PubMed:2825443)Curated
Sequence conflicti512 – 5121S → A(PubMed:2822598)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931T → I in strain: Isolate ZM1; 4-GU-DANA antiviral drug resistant and increased receptor binding avidity. 1 Publication
Natural varianti216 – 2161D → N in strain: Isolate C28; 50% loss of neuraminidase activity. 1 Publication
Natural varianti567 – 5671I → V in strain: Isolate ZM1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17641 mRNA. Translation: AAA46846.1.
M21649 Genomic RNA. Translation: AAA46853.1.
M20402 mRNA. Translation: AAA46856.1.
PIRiA27765. HNNZP3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17641 mRNA. Translation: AAA46846.1 .
M21649 Genomic RNA. Translation: AAA46853.1 .
M20402 mRNA. Translation: AAA46856.1 .
PIRi A27765. HNNZP3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MZA X-ray 1.65 A/B 136-572 [» ]
4MZE X-ray 1.80 A/B 136-572 [» ]
ProteinModelPortali P08492.
SMRi P08492. Positions 142-572.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR000665. Hemagglutn-neuramid.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00423. HN. 1 hit.
[Graphical view ]
PIRSFi PIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: VARIANT 4-GU-DANA-RESISTANT ILE-193.
    Strain: Isolate ZM1.

Entry informationi

Entry nameiHN_PI3H4
AccessioniPrimary (citable) accession number: P08492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3