ID   HN_NDVM                 Reviewed;         571 AA.
AC   P12557;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-NOV-2023, entry version 115.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Newcastle disease virus (strain Miyadera/51) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Orthoavulavirus javaense; Avian orthoavulavirus 1.
OX   NCBI_TaxID=11185;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2450424; DOI=10.1016/0042-6822(88)90244-9;
RA   Gotoh B., Sakaguchi T., Nishikawa K., Inocencio N.M., Hamaguchi M.,
RA   Toyoda T., Nagai Y.;
RT   "Structural features unique to each of the three antigenic sites on the
RT   hemagglutinin-neuraminidase protein of Newcastle disease virus.";
RL   Virology 163:174-182(1988).
RN   [2]
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: Homodimer. Forms homotetramers. Interacts with fusion/F
CC       protein. Interacts with host CG-1B; this interaction inhibits viral
CC       adsorption and replication rather than internalization.
CC       {ECO:0000250|UniProtKB:Q91UL0}.
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   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; M19479; AAA46674.1; -; Genomic_RNA.
DR   EMBL; M24713; AAA46663.1; -; Genomic_RNA.
DR   SMR; P12557; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyCosmos; P12557; 6 sites, No reported glycans.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0046718; P:viral 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   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   Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW   Host-virus interaction; Hydrolase; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..571
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142616"
FT   TOPO_DOM        1..26
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..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   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   CONFLICT        167
FT                   /note="T -> P (in Ref. 2; AAA46663)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   571 AA;  62523 MW;  F2891CE5137937D5 CRC64;
     MDRTVNQVAL ENDEREAKNT WRLVFRIATL LLIVMTLAFS AAALAYSMEA STPGDLVGIP
     TAISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE SIIMNAITSL SYQINGAANN
     SGCGAPVHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
     SATHYCYTHN VILSGCRDHS QSHQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV
     SATPLGCDML CSKVTETEEE DYNSVTPTSM VHGRLGFDGQ YHEKDLDVTT LFGDWVANYP
     GVGGGSFIDS RVWFPIYGGL KPNSPSDTAQ EGRYVIYKRY NDTCPDEQDY QIRMAKSSYK
     PRRFGGKRVQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRVLTVGTS HFLYQRGSSY
     FSPALLYPMT VNNKTATLHS PYTFNAFTRP GSVPCQASAR CPNSCVTGVY TDPYPLVFHA
     NHTLRGVFGT MLDDERARLN PVSAVFDNVS RSRITRVSSS STKAAYTTST CFKVVKTNKT
     YCLSIAEISN TLFGEFRIVP LLVEILKDDK V
//