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 08-NOV-2023, entry version 103. 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; Orthoavulavirus javaense; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9Q2W5; 6 sites, No reported glycans. 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:0016020; C: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 Gene3D; 2.120.10.10; -; 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; Sialidases; 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 //