ID   HN_NDVQ                 Reviewed;         616 AA.
AC   P13850;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-NOV-2023, entry version 116.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Newcastle disease virus (strain Queensland/66) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Orthoavulavirus javaense; Avian orthoavulavirus 1.
OX   NCBI_TaxID=11186;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3045120; DOI=10.1016/s0021-9258(18)37786-x;
RA   Gorman J.J., Nestorowicz A., Mitchell S.J., Corino G.L., Selleck P.W.;
RT   "Characterization of the sites of proteolytic activation of Newcastle
RT   disease virus membrane glycoprotein precursors.";
RL   J. Biol. Chem. 263:12522-12531(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; J03911; AAA46654.1; -; Genomic_RNA.
DR   EMBL; M24706; AAA46656.1; -; Genomic_RNA.
DR   PIR; A31110; HNNZQD.
DR   PIR; B46328; B46328.
DR   SMR; P13850; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyCosmos; P13850; 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..616
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142617"
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..616
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        538
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   VARIANT         87
FT                   /note="Q -> H"
FT   VARIANT         113
FT                   /note="R -> Q"
FT   VARIANT         151
FT                   /note="Y -> F"
FT   VARIANT         432
FT                   /note="S -> G"
FT   VARIANT         495
FT                   /note="K -> E"
SQ   SEQUENCE   616 AA;  67656 MW;  CBF556EB3B8C060F CRC64;
     MDRAVSQVAL ENDEREAKNT WRLVFRIAIL LSTVVTLAIS AAALAYSMEA STPSDLVGIP
     TAISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE STIMNAITSL SYRINGAANS
     SGCGAPIHDP DYIGGIGKEL IVDDASDVTS YYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
     SATHYCYTHN VILSGCRDHS HSHQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV
     SATPLGCDML CSKVTETEEE DYNSAIPTSM VHGRLGFDGQ YHEKDLDVTT LFEDWVANYP
     GVGGGSFIDN RVWFPVYGGL KPNSPSDTAQ EGKYVIYKRY NDTCPDEQDY QIQMAKSSYK
     PGRFGGKRVQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRVLTVGTS HFLYQRGSSY
     FSPALLYPMI VSNKTATLHS PYTFNAFTRP GSVPCQASAR CPNSCVTGVY TDPYPLVFYR
     NHTLRGVFGT MLDDKQARLN PVSAVFDSIS RSRITRVSSS STKAAYTTST CFKVVKTNKT
     YCLSIAEISN TLFGEFRIVP LLVEILKDDG VREARSSRLS QLREGWKDDI VSPIFCDAKN
     QTEYRRELES YAASWP
//