HN_NDVA
ID HN_NDVA Reviewed; 570 AA.
AC P12554;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Newcastle disease virus (strain Chicken/Australia-Victoria/32) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=11177;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3037818; DOI=10.1016/0168-1702(87)90027-x;
RA McGinnes L.W., Wilde A., Morrison T.G.;
RT "Nucleotide sequence of the gene encoding the Newcastle disease virus
RT hemagglutinin-neuraminidase protein and comparisons of paramyxovirus
RT hemagglutinin-neuraminidase protein sequences.";
RL Virus Res. 7:187-202(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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 [3]
RP NUCLEOTIDE SEQUENCE.
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 -!- INTERACTION:
CC P12554; P12554: HN; NbExp=4; IntAct=EBI-15941682, EBI-15941682;
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; M22110; AAA46670.1; -; mRNA.
DR EMBL; M24712; AAA46662.1; -; Genomic_RNA.
DR PIR; B31110; HNNZAV.
DR PDB; 3T1E; X-ray; 3.30 A; A/B/E/F=49-570.
DR PDBsum; 3T1E; -.
DR SMR; P12554; -.
DR DIP; DIP-60382N; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR EvolutionaryTrace; P12554; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:0042802; F:identical protein binding; IPI:IntAct.
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 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; SSF50939; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..570
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142606"
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..570
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 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q91UL0"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 184
FT /note="H -> HY (in Ref. 3; AAA46662)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="D -> H (in Ref. 1; AAA46670)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="E -> Q (in Ref. 1; AAA46670)"
FT /evidence="ECO:0000305"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 92..111
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 172..192
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 287..293
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:3T1E"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 378..388
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 522..533
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 534..537
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 538..549
FT /evidence="ECO:0007829|PDB:3T1E"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:3T1E"
FT STRAND 553..565
FT /evidence="ECO:0007829|PDB:3T1E"
SQ SEQUENCE 570 AA; 62284 MW; 96EF3FFED67179D7 CRC64;
MNRAVCQVAL ENDEREAKNT WRLVFRIAIL LLTVMTLAIS AAALAYSMEA STPGDLVSIP
TAISRAEGKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE SIIMNAITSL SYQINGAANN
SGCGAPVHDP DYIGGIGKEL IVDDTSDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
SATHCYTHNV IFSGCRDHSH SHQYLALGVL RTSATGRVFF STLRSINLDD TQNRKSCSVS
ATPLGCDMLC SKVTETEEED YNSVIPTSMV HGRLGFDGQY HEKDLDVTTL FGDWVANYPG
VGGGSFIDNR VWFPVYGGLK PSSPSDTGQE GRYVIYKRYN DTCPDEQDYQ IRMAKSSYKP
GRFGGKRVQQ AILSIKVSTS LGEDPVLTIP PNTVTLMGAE GRVLTVGTSH FLYQRGSSYF
SPALLYPMTV NNNTATLHSP YTFNAFTRPG SVPCQASARC PNSCVTGVYT DPYPLVFHRN
HTLRGVFGTM LDDEQARLNL VSAVFDNISR SRITRVSSSR TKAAYTTSTC FKVVKTNKTY
CLSIAEISNT LFGEFRIVPL LVEILKDDGV
