HN_NDVB1
ID HN_NDVB1 Reviewed; 577 AA.
AC Q91UL0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 02-JUN-2021, entry version 94.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Newcastle disease virus (strain Chicken/United States/B1/48) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=652953;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sellers H.S., Seal B.S.;
RT "Complete sequence for the B1 strain of Newcastle disease virus.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=12438588; DOI=10.1128/jvi.76.24.12622-12633.2002;
RA McGinnes L.W., Gravel K., Morrison T.G.;
RT "Newcastle disease virus HN protein alters the conformation of the F
RT protein at cell surfaces.";
RL J. Virol. 76:12622-12633(2002).
RN [3]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-158; LEU-160; PHE-220; LEU-224;
RP LYS-536 AND ARG-557.
RX PubMed=12438628; DOI=10.1128/jvi.76.24.13028-13033.2002;
RA Takimoto T., Taylor G.L., Connaris H.C., Crennell S.J., Portner A.;
RT "Role of the hemagglutinin-neuraminidase protein in the mechanism of
RT paramyxovirus-cell membrane fusion.";
RL J. Virol. 76:13028-13033(2002).
RN [4]
RP FUNCTION, INTERACTION WITH F, AND MUTAGENESIS OF ILE-133 AND LEU-140.
RX PubMed=14512552; DOI=10.1128/jvi.77.20.11040-11049.2003;
RA Gravel K.A., Morrison T.G.;
RT "Interacting domains of the HN and F proteins of newcastle disease virus.";
RL J. Virol. 77:11040-11049(2003).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15016893; DOI=10.1128/jvi.78.7.3733-3741.2004;
RA Zaitsev V., von Itzstein M., Groves D., Kiefel M., Takimoto T., Portner A.,
RA Taylor G.;
RT "Second sialic acid binding site in Newcastle disease virus hemagglutinin-
RT neuraminidase: implications for fusion.";
RL J. Virol. 78:3733-3741(2004).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF TYR-526.
RX PubMed=19474107; DOI=10.1128/jvi.00536-09;
RA Khattar S.K., Yan Y., Panda A., Collins P.L., Samal S.K.;
RT "A Y526Q mutation in the Newcastle disease virus HN protein reduces its
RT functional activities and attenuates virus replication and pathogenicity.";
RL J. Virol. 83:7779-7782(2009).
RN [7]
RP FUNCTION, INTERACTION WITH F, AND MUTAGENESIS OF ARG-83 AND LEU-97.
RX PubMed=23740987; DOI=10.1128/jvi.01066-13;
RA Mirza A.M., Iorio R.M.;
RT "A mutation in the stalk of the newcastle disease virus hemagglutinin-
RT neuraminidase (HN) protein prevents triggering of the F protein despite
RT allowing efficient HN-F complex formation.";
RL J. Virol. 87:8813-8815(2013).
RN [8]
RP GLYCOSYLATION AT ASN-341; ASN-433 AND ASN-481.
RX PubMed=27928741; DOI=10.1007/s10719-016-9750-7;
RA Pegg C.L., Hoogland C., Gorman J.J.;
RT "Site-specific glycosylation of the Newcastle disease virus haemagglutinin-
RT neuraminidase.";
RL Glycoconj. J. 34:181-197(2017).
RN [9]
RP INTERACTION WITH HOST GALECTIN-1B/CG-1B, AND SUBCELLULAR LOCATION.
RX PubMed=28978647; DOI=10.1074/jbc.m116.772897;
RA Sun J., Han Z., Qi T., Zhao R., Liu S.;
RT "Chicken galectin-1B inhibits Newcastle disease virus adsorption and
RT replication through binding to hemagglutinin-neuraminidase (HN)
RT glycoprotein.";
RL J. Biol. Chem. 292:20141-20161(2017).
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:0000269|PubMed:12438588,
CC ECO:0000269|PubMed:12438628, ECO:0000269|PubMed:14512552,
CC ECO:0000269|PubMed:15016893, ECO:0000269|PubMed:19474107,
CC ECO:0000269|PubMed:23740987}.
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:0000269|PubMed:19474107}.
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 -!- SUBUNIT: Homodimer (PubMed:12438628). Forms homotetramers
CC (PubMed:15016893). Interacts with fusion/F protein (PubMed:14512552,
CC PubMed:23740987). Interacts with host CG-1B; this interaction inhibits
CC viral adsorption and replication rather than internalization
CC (PubMed:28978647). {ECO:0000269|PubMed:12438628,
CC ECO:0000269|PubMed:14512552, ECO:0000269|PubMed:15016893,
CC ECO:0000269|PubMed:23740987, ECO:0000269|PubMed:28978647}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:28978647};
CC Single-pass type II membrane protein {ECO:0000305}. Host cell membrane
CC {ECO:0000269|PubMed:28978647}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC family. {ECO:0000305}.
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DR EMBL; AF309418; AAG36979.1; -; Genomic_RNA.
DR RefSeq; NP_071470.1; NC_002617.1.
DR SMR; Q91UL0; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR iPTMnet; Q91UL0; -.
DR Proteomes; UP000002328; Genome.
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: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 Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW Host-virus interaction; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..577
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000390622"
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..577
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION 124..152
FT /note="Important for interaction with fusion/F protein"
FT /evidence="ECO:0000269|PubMed:14512552"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27928741"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27928741"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27928741"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 83
FT /note="R->T: About 95% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:23740987"
FT MUTAGEN 97
FT /note="L->T: About 95% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:23740987"
FT MUTAGEN 133
FT /note="I->A: About 80% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:14512552"
FT MUTAGEN 140
FT /note="L->A: About 80% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:14512552"
FT MUTAGEN 158
FT /note="E->A: About 98% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 160
FT /note="L->A: About 97% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 220
FT /note="F->A: About 97% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 224
FT /note="L->A: About 97% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 526
FT /note="Y->Q: About 30% to 50% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 536
FT /note="K->A: About 96% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
FT MUTAGEN 557
FT /note="R->A: About 99% loss of the fusion promotion
FT activities."
FT /evidence="ECO:0000269|PubMed:12438628"
SQ SEQUENCE 577 AA; 63227 MW; 23DD6748352C8C17 CRC64;
MDRAVSQVAL ENDEREAKNT WRLIFRIAIL FLTVVTLAIS VASLLYSMGA STPSDLVGIP
TRISRAEEKI TSTLGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN
SGWGAPIHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
SATHYCYTHN VILSGCRDHS HSYQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV
SATPLGCDML CSKATETEEE DYNSAVPTRM VHGRLGFDGQ YHEKDLDVTT LFGDWVANYP
GVGGGSFIDS RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK
PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY
FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR
NHTLRGVFGT MLDGEQARLN PASAVFDSTS RSRITRVSSS SIKAAYTTST CFKVVKTNKT
YCLSIAEISN TLFGEFRIVP LLVEILKDDG VREARSG
