HN_NDVH3
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 07-APR-2021, entry version 102.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Newcastle disease virus (strain Her/33) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 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: 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; M24714; AAA46664.1; -; Genomic_RNA.
DR PIR; A36829; A36829.
DR SMR; P35741; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR PRIDE; P35741; -.
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 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_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 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"
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
