ID   HN_NDVH3                Reviewed;         571 AA.
AC   P35741;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18 {ECO:0000250|UniProtKB:Q9WAF5};
GN   Name=HN;
OS   Newcastle disease virus (strain Her/33) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Orthoavulavirus javaense; Avian paramyxovirus 1.
OX   NCBI_TaxID=11187;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2705297; DOI=10.1016/0042-6822(89)90151-7;
RA   Sakaguchi T., Toyoda T., Gotoh B., Inocencio N.M., Kuma K., Miyata T.,
RA   Nagai Y.;
RT   "Newcastle disease virus evolution. I. Multiple lineages defined by
RT   sequence variability of the hemagglutinin-neuraminidase gene.";
RL   Virology 169:260-272(1989).
CC   -!- FUNCTION: Mediates the viral entry into the host cell together with
CC       fusion/F protein. Attaches the virus to sialic acid-containing cell
CC       receptors and thereby initiates infection. Binding of HN protein to the
CC       receptor induces a conformational change that allows the F protein to
CC       trigger virion/cell membranes fusion. {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- FUNCTION: Neuraminidase activity ensures the efficient spread of the
CC       virus by dissociating the mature virions from the neuraminic acid
CC       containing glycoproteins. {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000250|UniProtKB:Q91UL0};
CC   -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers (By
CC       similarity). Interacts with F protein trimer (By similarity). Interacts
CC       with host CG-1B; this interaction inhibits viral adsorption and
CC       replication rather than internalization (By similarity).
CC       {ECO:0000250|UniProtKB:P04853, ECO:0000250|UniProtKB:Q91UL0,
CC       ECO:0000250|UniProtKB:Q9WAF5}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q91UL0};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91UL0}.
CC       Host cell membrane {ECO:0000250|UniProtKB:Q91UL0}; Single-pass type II
CC       membrane protein {ECO:0000250|UniProtKB:Q91UL0}.
CC   -!- DOMAIN: The C-terminus (head domain) is involved in binding the
CC       cellular receptor. {ECO:0000250|UniProtKB:Q9WAF5}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; M24714; AAA46664.1; -; Genomic_RNA.
DR   PIR; A36829; A36829.
DR   AlphaFoldDB; P35741; -.
DR   SMR; P35741; -.
DR   GlyCosmos; P35741; 6 sites, No reported glycans.
DR   GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; ISS:UniProtKB.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd15469; HN; 1.
DR   FunFam; 2.120.10.10:FF:000004; Hemagglutinin-neuraminidase; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR016285; Hemagglutn-neuramid.
DR   InterPro; IPR000665; Hemagglutn/HN.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00423; HN; 1.
DR   PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
KW   Host membrane; Host-virus interaction; Hydrolase; Membrane; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   CHAIN           1..571
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142610"
FT   TOPO_DOM        1..26
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..571
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          124..152
FT                   /note="Important for interaction with fusion/F protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   REGION          234..239
FT                   /note="Involved in neuraminidase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        172..196
FT                   /evidence="ECO:0000250|UniProtKB:Q9WAF5"
FT   DISULFID        186..247
FT                   /evidence="ECO:0000250|UniProtKB:Q9WAF5"
FT   DISULFID        238..251
FT                   /evidence="ECO:0000250|UniProtKB:Q9WAF5"
FT   DISULFID        344..461
FT                   /evidence="ECO:0000250|UniProtKB:Q9WAF5"
FT   DISULFID        455..465
FT                   /evidence="ECO:0000250|UniProtKB:Q9WAF5"
SQ   SEQUENCE   571 AA;  62610 MW;  60EBC6A508C6A1BF CRC64;
     MDRAVSRVAL ENEEREAKNT WRFVFRIAIL LLIVITLAIS AAALVYSMEA STPGDLVGIP
     TVISRAEEKI TSALSSNQDV VDRIYKQVAL ESPLALLNTE SVIMNAITSL SYQINGAANN
     SGCGAPVHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDI
     SATHYCYTHN VILSGCRDHS HSHQYLALGV LRTSATGRVF FSTLRSINLD DNQNRKSCSV
     SATPLGCDML CSKITETEEE DYSSVTPTSM VHGRLGFDGQ YHEKDLDVIT LFKDWVANYP
     GVGGGSFIDN RVWFPVYGGL KPNSPSDTVQ EGRYVIYKRY NDTCPDEQDY QIRMAKSSYK
     PGRFGGKRVQ QAILSIKVST SLGEDPVLTI PPNTVTLMGA EGRVLTVGTS HFLYQRGSSY
     FSPALLYPMT VNNKTATLHS PYTFNAFTRP GSVPCQASAR CPNSCVTGVY TDPYPLIFHR
     NHTLRGVFGT MLDDGQARLN PVSAVFDNIS RSRITRVSSS RTKAAYTTST CFKVVKTNKT
     YVLSIAEISN TLFGEFRIVP LLVEILKNDG V
//