UniProtKB - P32884 (HN_NDVB)
Protein
Hemagglutinin-neuraminidase
Gene
HN
Organism
Newcastle disease virus (strain Beaudette C/45) (NDV)
Status
Functioni
Mediates the viral entry into the host cell together with fusion/F protein. Attaches the virus to sialic acid-containing cell receptors and thereby initiates 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 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.By similarity EC:3.2.1.18
GO - Molecular functioni
- exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
- exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
- exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
- host cell surface receptor binding Source: InterPro
GO - Biological processi
- viral entry into host cell Source: UniProtKB-KW
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Molecular function | Hemagglutinin, Hydrolase |
Biological process | Host-virus interaction, Viral attachment to host cell, Virus entry into host cell |
Protein family/group databases
CAZyi | GH83, Glycoside Hydrolase Family 83 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:HN |
Organismi | Newcastle disease virus (strain Beaudette C/45) (NDV) |
Taxonomic identifieri | 11178 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Haploviricotina › Monjiviricetes › Mononegavirales › Paramyxoviridae › Avulavirus › |
Virus hosti | Gallus gallus (Chicken) [TaxID: 9031] |
Subcellular locationi
- Virion membrane By similarity; Single-pass type II membrane protein By similarity
- Host cell membrane By similarity; Single-pass type II membrane protein By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 26 | IntravirionSequence analysisAdd BLAST | 26 | |
Transmembranei | 27 – 48 | HelicalSequence analysisAdd BLAST | 22 | |
Topological domaini | 49 – 577 | Virion surfaceSequence analysisAdd BLAST | 529 |
GO - Cellular componenti
- host cell plasma membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
- viral envelope Source: UniProtKB-KW
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Viral envelope protein, VirionPathology & Biotechi
Chemistry databases
DrugBanki | DB03991, 2-deoxy-2,3-dehydro-N-acetylneuraminic acid DB04508, Methyl(6s)-1-Thio-L-Manno-Hexodialdo-6,2-Pyranoside DB03740, N-acetyl-alpha-D-glucosamine DB03721, N-acetyl-alpha-neuraminic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000142607 | 1 – 577 | Hemagglutinin-neuraminidaseAdd BLAST | 577 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | Blocked amino end (Met); by host | 1 | |
Glycosylationi | 119 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 341 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 433 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 481 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 538 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 |
Keywords - PTMi
GlycoproteinInteractioni
Subunit structurei
Homodimer. Forms homotetramers.
Interacts with fusion/F protein.
Interacts with host CG-1B; this interaction inhibits viral adsorption and replication rather than internalization.
By similarityStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P32884 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32884 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 124 – 152 | Important for interaction with fusion/F proteinBy similarityAdd BLAST | 29 |
Sequence similaritiesi
Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixFamily and domain databases
CDDi | cd15469, HN, 1 hit |
InterProi | View protein in InterPro IPR016285, Hemagglutn-neuramid IPR000665, Hemagglutn/HN IPR036278, Sialidase_sf |
Pfami | View protein in Pfam PF00423, HN, 1 hit |
PIRSFi | PIRSF001072, Hemagglut-neuramid_paramyxoV, 1 hit |
SUPFAMi | SSF50939, SSF50939, 1 hit |
i Sequence
Sequence statusi: Complete.
P32884-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDRAVSQVAL ENDEREAKNT WRLIFRIAIL LLTVVTLATS VASLVYSMGA
60 70 80 90 100
STPSDLVGIP TRISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE
110 120 130 140 150
TTIMNAITSL SYQINGAANN SGWGAPIHDP DFIGGIGKEL IVDDASDVTS
160 170 180 190 200
FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM SATHYCYTHN VILSGCRDHS
210 220 230 240 250
HSHQYLALGV LRTTATGRIF FSTLRSISLD DTQNRKSCSV SATPLGCDML
260 270 280 290 300
CSKVTETEEE DYNSAVPTLM AHGRLGFDGQ YHEKDLDVTT LFEDWVANYP
310 320 330 340 350
GVGGGSFIDG RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY
360 370 380 390 400
QIRMAKSSYK PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA
410 420 430 440 450
EGRILTVGTS HFLYQRGSSY FSPALLYPMT VSNKTATLHS PYTFNAFTRP
460 470 480 490 500
GSIPCQASAR CPNSCVTGVY TDPYPLIFYR NHTLRGVFGT MLDSEQARLN
510 520 530 540 550
PTSAVFDSTS RSRITRVSSS STKAAYTTST CFKVVKTNKT YCLSIAEISN
560 570
TLFGEFRIVP LLVEILKNDG VREARSG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X04355 Genomic RNA Translation: CAA27880.1 M24710 Genomic RNA Translation: AAA46660.1 |
PIRi | F46328 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X04355 Genomic RNA Translation: CAA27880.1 M24710 Genomic RNA Translation: AAA46660.1 |
PIRi | F46328 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1USR | X-ray | 2.00 | A/B | 124-577 | [»] | |
1USX | X-ray | 2.70 | A/B/C | 124-577 | [»] | |
SMRi | P32884 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB03991, 2-deoxy-2,3-dehydro-N-acetylneuraminic acid DB04508, Methyl(6s)-1-Thio-L-Manno-Hexodialdo-6,2-Pyranoside DB03740, N-acetyl-alpha-D-glucosamine DB03721, N-acetyl-alpha-neuraminic acid |
Protein family/group databases
CAZyi | GH83, Glycoside Hydrolase Family 83 |
Miscellaneous databases
EvolutionaryTracei | P32884 |
Family and domain databases
CDDi | cd15469, HN, 1 hit |
InterProi | View protein in InterPro IPR016285, Hemagglutn-neuramid IPR000665, Hemagglutn/HN IPR036278, Sialidase_sf |
Pfami | View protein in Pfam PF00423, HN, 1 hit |
PIRSFi | PIRSF001072, Hemagglut-neuramid_paramyxoV, 1 hit |
SUPFAMi | SSF50939, SSF50939, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HN_NDVB | |
Accessioni | P32884Primary (citable) accession number: P32884 Secondary accession number(s): P06158 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | October 7, 2020 | |
This is version 113 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries