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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: 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

GO - Biological processi

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 virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeRespirovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 31IntravirionSequence analysisAdd BLAST31
Transmembranei32 – 52HelicalSequence analysisAdd BLAST21
Topological domaini53 – 572Virion surfaceSequence analysisAdd BLAST520

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001426251 – 572Hemagglutinin-neuraminidaseAdd BLAST572

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi308N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi351N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi523N-linked (GlcNAc...); by hostSequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi148 – 150Combined sources3
Helixi153 – 156Combined sources4
Beta strandi160 – 162Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi190 – 198Combined sources9
Beta strandi203 – 215Combined sources13
Beta strandi221 – 231Combined sources11
Beta strandi235 – 247Combined sources13
Turni249 – 251Combined sources3
Beta strandi254 – 261Combined sources8
Beta strandi264 – 270Combined sources7
Helixi276 – 281Combined sources6
Beta strandi282 – 284Combined sources3
Beta strandi288 – 293Combined sources6
Beta strandi299 – 304Combined sources6
Helixi306 – 308Combined sources3
Beta strandi309 – 313Combined sources5
Beta strandi315 – 320Combined sources6
Beta strandi326 – 328Combined sources3
Beta strandi331 – 342Combined sources12
Helixi360 – 366Combined sources7
Helixi370 – 372Combined sources3
Beta strandi377 – 386Combined sources10
Helixi388 – 390Combined sources3
Beta strandi392 – 398Combined sources7
Turni401 – 403Combined sources3
Beta strandi410 – 415Combined sources6
Beta strandi418 – 423Combined sources6
Beta strandi427 – 429Combined sources3
Beta strandi433 – 438Combined sources6
Beta strandi446 – 449Combined sources4
Beta strandi461 – 463Combined sources3
Beta strandi481 – 485Combined sources5
Beta strandi488 – 496Combined sources9
Beta strandi498 – 503Combined sources6
Beta strandi505 – 513Combined sources9
Beta strandi515 – 522Combined sources8
Beta strandi526 – 538Combined sources13
Beta strandi541 – 552Combined sources12
Turni553 – 556Combined sources4
Beta strandi557 – 566Combined sources10
Beta strandi569 – 571Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MZAX-ray1.65A/B136-572[»]
4MZEX-ray1.80A/B136-572[»]
4XJRX-ray3.00A/B125-572[»]
ProteinModelPortaliP08492.
SMRiP08492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
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)DescriptionActionsGraphical viewLength
Sequence conflicti135Q → R in AAA46853 (PubMed:2825443).Curated1
Sequence conflicti146V → A in AAA46853 (PubMed:2825443).Curated1
Sequence conflicti489S → G in AAA46856 (PubMed:2822598).Curated1
Sequence conflicti512S → A (PubMed:2825443).Curated1
Sequence conflicti512S → A (PubMed:2822598).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti193T → I in strain: Isolate ZM1; 4-GU-DANA antiviral drug resistant and increased receptor binding avidity. 1 Publication1
Natural varianti216D → N in strain: Isolate C28; 50% loss of neuraminidase activity. 1 Publication1
Natural varianti567I → V in strain: Isolate ZM1. 1

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.
PIRiA27765. HNNZP3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MZAX-ray1.65A/B136-572[»]
4MZEX-ray1.80A/B136-572[»]
4XJRX-ray3.00A/B125-572[»]
ProteinModelPortaliP08492.
SMRiP08492.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR016285. Hemagglutn-neuramid.
IPR000665. Hemagglutn/HN.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00423. HN. 1 hit.
[Graphical view]
PIRSFiPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.