ID HN_NDVC Reviewed; 571 AA. AC P35740; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 08-NOV-2023, entry version 106. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Newcastle disease virus (strain Chi/85) (NDV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae; OC Orthoavulavirus; Orthoavulavirus javaense; Avian orthoavulavirus 1. OX NCBI_TaxID=11179; 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}. 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; M24716; AAA46666.1; -; Genomic_RNA. DR PIR; C36829; C36829. DR SMR; P35740; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P35740; 6 sites, No reported glycans. 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 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_0000142608" 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; 62901 MW; 3110CD668D71EF76 CRC64; MDRAVNRVVL ENEEREAKNT WRLVFRIAVL LLMVMTLAIS AAALVYSMGA STPRDLAGIS TVISKTEDKV TSLLSSKQDV IDRIYKQVAL ESPLALLNTE SIIMNAITSL SYQINGAANN SGCGEPVHDP DYIGGIGKEL IVDDISDVTS FYPSAYQEHL NFIPAPTTGS GCTRIPSFDM STTHYCYTHN VILSGCRDHS HSHQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV SATPLGCDML CSKVTETEEE DYKSVTPTSM VHGRLGFDGQ YHEKDLDTTV LFKDWVANYP GVGGGSFIDD RVWFPVYGGL KPNSPSDTAQ EGKYVIYKRY NNTCPDEQDY QIRMAKSSYK PGRFGGKRVQ QAILSIKVST SLGEDPVLTI PPNTITLMGA EGRVLTVGTS HFLYQRGSSY FSPALLYPMT VNNKTATLHS PYTFNAFTRP GSVPCQASAR CPNSCITGVY TDPYPLIFHR NHTLRGVFGT MLDDEQARLN PVSAVFDNIS RSRVTRVSSS STKAAYTTST CFKVVKTNKA YCLSIAEISN TLFGEFRIVP LLVEILKDDR V //