HN_NDVK
ID HN_NDVK Reviewed; 577 AA.
AC Q9Q2W5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 100.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Newcastle disease virus (strain Kansas) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=332244;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10772993; DOI=10.1006/viro.2000.0263;
RA Takimoto T., Taylor G.L., Crennell S.J., Scroggs R.A., Portner A.;
RT "Crystallization of Newcastle disease virus hemagglutinin-neuraminidase
RT glycoprotein.";
RL Virology 270:208-214(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 124-577.
RX PubMed=11062565; DOI=10.1038/81002;
RA Crennell S., Takimoto T., Portner A., Taylor G.;
RT "Crystal structure of the multifunctional paramyxovirus hemagglutinin-
RT neuraminidase.";
RL Nat. Struct. Biol. 7:1068-1074(2000).
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; AF212323; AAF19984.1; -; Genomic_RNA.
DR PDB; 1E8T; X-ray; 2.50 A; A/B=124-577.
DR PDB; 1E8U; X-ray; 2.00 A; A/B=124-577.
DR PDB; 1E8V; X-ray; 2.00 A; A/B=124-577.
DR PDBsum; 1E8T; -.
DR PDBsum; 1E8U; -.
DR PDBsum; 1E8V; -.
DR SMR; Q9Q2W5; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR BRENDA; 3.2.1.18; 3631.
DR EvolutionaryTrace; Q9Q2W5; -.
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 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..577
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142614"
FT TOPO_DOM 1..22
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..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 144
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 TURN 130..134
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 202..213
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1E8V"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:1E8U"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1E8U"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:1E8V"
FT STRAND 523..534
FT /evidence="ECO:0007829|PDB:1E8U"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 539..549
FT /evidence="ECO:0007829|PDB:1E8U"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:1E8U"
FT STRAND 557..567
FT /evidence="ECO:0007829|PDB:1E8U"
SQ SEQUENCE 577 AA; 63111 MW; 6A1F03C8DD3F7753 CRC64;
MDRAVSQVAL ENDEREAKNT WRLIFRIAIL LLTVVTLATS VASLVYSMGA STPSDLVGIP
TRISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN
SGWGAPIHDP DFIGGIGKEL IVDNASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM
SATHYCYTHN VILSGCRDHS HSHQYLALGV LRTTATGRIF FSTLRSISLD DTQNRKSCSV
SATPLGCDML CSKVTETEEE DYNSAVPTLM AHGRLGFDGQ YHEKDLDVTT LFEDWVANYP
GVGGGSFIDG RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK
PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY
FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR
NHTLRGVFGT MLDSEQARLN PASAVFDSTS RSRITRVSSS STKAAYTTST CFKVVKTNKT
YCLSIAEISN TLFGEFRIVP LLVEILKNDG VREARSG
