ID HN_PI3HT Reviewed; 572 AA. AC P12562; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 13-SEP-2023, entry version 109. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Human parainfluenza 3 virus (strain Tex/545/80) (HPIV-3). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae; OC Respirovirus; Respirovirus pneumoniae. OX NCBI_TaxID=11219; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2827373; DOI=10.1016/0042-6822(88)90402-3; RA van Wyke Coelingh K.L., Winter C.C., Murphy B.R.; RT "Nucleotide and deduced amino acid sequence of hemagglutinin-neuraminidase RT genes of human type 3 parainfluenza viruses isolated from 1957 to 1983."; RL Virology 162:137-143(1988). CC -!- FUNCTION: Attaches the virus to sialic acid-containing cell receptors CC and thereby initiating infection. Binding of HN protein to the receptor CC induces a conformational change that allows the F protein to trigger CC virion/cell membranes fusion (By similarity). {ECO:0000250}. 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}. 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 -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type CC II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; CC Single-pass type II membrane protein {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; M18762; AAA46849.1; -; Genomic_RNA. DR PIR; D29970; HNNZ80. DR SMR; P12562; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P12562; 3 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..572 FT /note="Hemagglutinin-neuraminidase" FT /id="PRO_0000142627" FT TOPO_DOM 1..31 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 53..572 FT /note="Virion surface" FT /evidence="ECO:0000255" FT CARBOHYD 308 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 351 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 523 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" SQ SEQUENCE 572 AA; 64259 MW; 57892E312D5F5F1B CRC64; MEYWKHTNHG KDAGNELETS MATHGNKLTN KIIYILWTII LVLLSIVFII VLTNSIKSEK AHESLLRDIN NEFIGITEKI QMASDNTNDL IQSGVNTRLL TIQSHVQNYI PISLTQQMSD LRKFISEITI RNDNQEVLPQ RITHDVGIKP LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL LAMPTTVDGC IRTPSLVIND LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN PRISHTFNIN DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNYDGSIS TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPIDENVIC NTTGCPGKTQ RDCNQASHSP WFSDRRMVNS IIVVDKGLNS TPKLKVWTIS MRQNYWGSEG RLLLLGNKIY IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT WHNVLSRPGN NECPWGHSCP DGCITGVYTD AYPLNPTGSI VSSVILDSQK SRVNPVITYS TATERVNELA IRNRTLSAGY TTTSCITHYN KGYCFHIVEI NHKSSNTFQP MLFKTEIPKS CS //