HN_NDVL
ID HN_NDVL Reviewed; 577 AA.
AC P35743;
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 Chicken/United States/LaSota/46) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=11184;
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; M24709; AAA46659.1; -; Genomic_RNA.
DR PIR; E46328; E46328.
DR SMR; P35743; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
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..577
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142615"
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: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 CONFLICT 310
FT /note="S -> G (in Ref. 1; AAA46659)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="A -> T (in Ref. 1; AAA46659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 63209 MW; E9939C6A8240364A CRC64;
MDRAVSQVAL ENDEREAKNT WRLIFRIAIL FLTVVTLAIS VASLLYSMGA STPSDLVGIP
TRISRAEEKI TSTLGSNQDV VDRIYKQVAL ESPLALLKTE TTIMNAITSL SYQINGAANN
SGWGAPIHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
SATHYCYTHN VILSGCRDHS HSYQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV
SATPLGCDML CSKVTETEEE DYNSAVPTRM AHGRLGFDGQ YHEKDLDVTT LFGDWVANYP
GVGGGSFIDS RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK
PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY
FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNPCVTGVY TDPYPLIFYR
NHTLRGVFGT MLDGVQARLN PASAVFDSTS RSRITRVSSS STKAAYTTST CFKVVKTNKT
YCLSIAEISN TLFGEFRIVP LLVEILKDDG VREARSG
