ID HN_NDVB1 Reviewed; 577 AA. AC Q91UL0; DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 08-NOV-2023, entry version 97. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Newcastle disease virus (strain Chicken/United States/B1/48) (NDV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae; OC Orthoavulavirus; Orthoavulavirus javaense; Avian orthoavulavirus 1. OX NCBI_TaxID=652953; OH NCBI_TaxID=9031; Gallus gallus (Chicken). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Sellers H.S., Seal B.S.; RT "Complete sequence for the B1 strain of Newcastle disease virus."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION. RX PubMed=12438588; DOI=10.1128/jvi.76.24.12622-12633.2002; RA McGinnes L.W., Gravel K., Morrison T.G.; RT "Newcastle disease virus HN protein alters the conformation of the F RT protein at cell surfaces."; RL J. Virol. 76:12622-12633(2002). RN [3] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-158; LEU-160; PHE-220; LEU-224; RP LYS-536 AND ARG-557. RX PubMed=12438628; DOI=10.1128/jvi.76.24.13028-13033.2002; RA Takimoto T., Taylor G.L., Connaris H.C., Crennell S.J., Portner A.; RT "Role of the hemagglutinin-neuraminidase protein in the mechanism of RT paramyxovirus-cell membrane fusion."; RL J. Virol. 76:13028-13033(2002). RN [4] RP FUNCTION, INTERACTION WITH F, AND MUTAGENESIS OF ILE-133 AND LEU-140. RX PubMed=14512552; DOI=10.1128/jvi.77.20.11040-11049.2003; RA Gravel K.A., Morrison T.G.; RT "Interacting domains of the HN and F proteins of newcastle disease virus."; RL J. Virol. 77:11040-11049(2003). RN [5] RP FUNCTION, AND SUBUNIT. RX PubMed=15016893; DOI=10.1128/jvi.78.7.3733-3741.2004; RA Zaitsev V., von Itzstein M., Groves D., Kiefel M., Takimoto T., Portner A., RA Taylor G.; RT "Second sialic acid binding site in Newcastle disease virus hemagglutinin- RT neuraminidase: implications for fusion."; RL J. Virol. 78:3733-3741(2004). RN [6] RP FUNCTION, AND MUTAGENESIS OF TYR-526. RX PubMed=19474107; DOI=10.1128/jvi.00536-09; RA Khattar S.K., Yan Y., Panda A., Collins P.L., Samal S.K.; RT "A Y526Q mutation in the Newcastle disease virus HN protein reduces its RT functional activities and attenuates virus replication and pathogenicity."; RL J. Virol. 83:7779-7782(2009). RN [7] RP FUNCTION, INTERACTION WITH F, AND MUTAGENESIS OF ARG-83 AND LEU-97. RX PubMed=23740987; DOI=10.1128/jvi.01066-13; RA Mirza A.M., Iorio R.M.; RT "A mutation in the stalk of the newcastle disease virus hemagglutinin- RT neuraminidase (HN) protein prevents triggering of the F protein despite RT allowing efficient HN-F complex formation."; RL J. Virol. 87:8813-8815(2013). RN [8] RP GLYCOSYLATION AT ASN-341; ASN-433 AND ASN-481. RX PubMed=27928741; DOI=10.1007/s10719-016-9750-7; RA Pegg C.L., Hoogland C., Gorman J.J.; RT "Site-specific glycosylation of the Newcastle disease virus haemagglutinin- RT neuraminidase."; RL Glycoconj. J. 34:181-197(2017). RN [9] RP INTERACTION WITH HOST GALECTIN-1B/CG-1B, AND SUBCELLULAR LOCATION. RX PubMed=28978647; DOI=10.1074/jbc.m116.772897; RA Sun J., Han Z., Qi T., Zhao R., Liu S.; RT "Chicken galectin-1B inhibits Newcastle disease virus adsorption and RT replication through binding to hemagglutinin-neuraminidase (HN) RT glycoprotein."; RL J. Biol. Chem. 292:20141-20161(2017). 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:0000269|PubMed:12438588, CC ECO:0000269|PubMed:12438628, ECO:0000269|PubMed:14512552, CC ECO:0000269|PubMed:15016893, ECO:0000269|PubMed:19474107, CC ECO:0000269|PubMed:23740987}. 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:0000269|PubMed:19474107}. 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 -!- SUBUNIT: Homodimer (PubMed:12438628). Forms homotetramers CC (PubMed:15016893). Interacts with fusion/F protein (PubMed:14512552, CC PubMed:23740987). Interacts with host CG-1B; this interaction inhibits CC viral adsorption and replication rather than internalization CC (PubMed:28978647). {ECO:0000269|PubMed:12438628, CC ECO:0000269|PubMed:14512552, ECO:0000269|PubMed:15016893, CC ECO:0000269|PubMed:23740987, ECO:0000269|PubMed:28978647}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:28978647}; CC Single-pass type II membrane protein {ECO:0000305}. Host cell membrane CC {ECO:0000269|PubMed:28978647}; Single-pass type II membrane protein CC {ECO:0000305}. 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; AF309418; AAG36979.1; -; Genomic_RNA. DR RefSeq; NP_071470.1; NC_002617.1. DR SMR; Q91UL0; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; Q91UL0; 4 sites, No reported glycans. DR iPTMnet; Q91UL0; -. DR Proteomes; UP000002328; Segment. 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 Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane; KW Host-virus interaction; Hydrolase; Membrane; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix; KW Viral attachment to host cell; Viral envelope protein; Virion; KW Virus entry into host cell. FT CHAIN 1..577 FT /note="Hemagglutinin-neuraminidase" FT /id="PRO_0000390622" 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:0000269|PubMed:14512552" FT CARBOHYD 341 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:27928741" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:27928741" FT CARBOHYD 481 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:27928741" FT CARBOHYD 538 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT MUTAGEN 83 FT /note="R->T: About 95% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:23740987" FT MUTAGEN 97 FT /note="L->T: About 95% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:23740987" FT MUTAGEN 133 FT /note="I->A: About 80% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:14512552" FT MUTAGEN 140 FT /note="L->A: About 80% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:14512552" FT MUTAGEN 158 FT /note="E->A: About 98% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 160 FT /note="L->A: About 97% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 220 FT /note="F->A: About 97% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 224 FT /note="L->A: About 97% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 526 FT /note="Y->Q: About 30% to 50% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 536 FT /note="K->A: About 96% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" FT MUTAGEN 557 FT /note="R->A: About 99% loss of the fusion promotion FT activities." FT /evidence="ECO:0000269|PubMed:12438628" SQ SEQUENCE 577 AA; 63227 MW; 23DD6748352C8C17 CRC64; MDRAVSQVAL ENDEREAKNT WRLIFRIAIL FLTVVTLAIS VASLLYSMGA STPSDLVGIP TRISRAEEKI TSTLGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN SGWGAPIHDP DYIGGIGKEL IVDDASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM SATHYCYTHN VILSGCRDHS HSYQYLALGV LRTSATGRVF FSTLRSINLD DTQNRKSCSV SATPLGCDML CSKATETEEE DYNSAVPTRM VHGRLGFDGQ YHEKDLDVTT LFGDWVANYP GVGGGSFIDS RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR NHTLRGVFGT MLDGEQARLN PASAVFDSTS RSRITRVSSS SIKAAYTTST CFKVVKTNKT YCLSIAEISN TLFGEFRIVP LLVEILKDDG VREARSG //