ID HN_PIV5 Reviewed; 565 AA. AC P04850; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 04-NOV-2026, entry version 163. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18 {ECO:0000250|UniProtKB:P25465}; GN Name=HN; OS Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae; OC Orthorubulavirus; Orthorubulavirus mammalis; Mammalian orthorubulavirus 5. OX NCBI_TaxID=11208; OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris). OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3973974; DOI=10.1128/jvi.54.1.1-6.1985; RA Hiebert S.W., Paterson R.G., Lamb R.A.; RT "Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5: RT nucleotide sequence of the mRNA predicts an N-terminal membrane anchor."; RL J. Virol. 54:1-6(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1765772; DOI=10.1099/0022-1317-72-12-3103; RA Baty D.U., Southern J.A., Randall R.E.; RT "Sequence comparison between the haemagglutinin-neuraminidase genes of RT simian, canine and human isolates of simian virus 5."; RL J. Gen. Virol. 72:3103-3107(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=15893670; DOI=10.1016/j.str.2005.02.019; RA Yuan P., Thompson T.B., Wurzburg B.A., Paterson R.G., Lamb R.A., RA Jardetzky T.S.; RT "Structural studies of the parainfluenza virus 5 hemagglutinin- RT neuraminidase tetramer in complex with its receptor, sialyllactose."; RL Structure 13:803-815(2005). 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 Evidence={ECO:0000250|UniProtKB:P25465}; CC -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers (By CC similarity). Interacts with F protein trimer (By similarity). CC {ECO:0000250|UniProtKB:P04853, ECO:0000250|UniProtKB:Q9WAF5}. CC -!- INTERACTION: CC P04850; P04850: HN; NbExp=4; IntAct=EBI-15552318, EBI-15552318; 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 -!- DOMAIN: The C-terminus (head domain) is involved in binding the CC cellular receptor. {ECO:0000250|UniProtKB:Q9WAF5}. 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; S76876; AAB21114.1; -; mRNA. DR EMBL; K02870; AAA47878.1; -; Genomic_RNA. DR EMBL; AF052755; AAC95517.1; -; Genomic_RNA. DR PIR; A00879; HNNZSV. DR PDB; 1Z4V; X-ray; 2.30 A; A=37-565. DR PDB; 1Z4W; X-ray; 2.70 A; A=37-565. DR PDB; 1Z4X; X-ray; 2.50 A; A=37-565. DR PDB; 1Z4Y; X-ray; 2.60 A; A=37-565. DR PDB; 1Z4Z; X-ray; 2.50 A; A=37-565. DR PDB; 1Z50; X-ray; 2.80 A; A=37-565. DR PDB; 3TSI; X-ray; 2.65 A; A/B/C/D=56-117. DR PDB; 4JF7; X-ray; 2.50 A; A/B/C/D=55-565. DR AlphaFoldDB; P04850; -. DR SMR; P04850; -. DR DIP; DIP-48442N; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P04850; 3 sites, No reported glycans. DR KEGG; vg:3160803; -. DR EvolutionaryTrace; P04850; -. DR Proteomes; UP000007232; Segment. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004308; F:exo-alpha-sialidase activity; ISS:UniProtKB. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd15469; HN; 1. DR FunFam; 2.120.10.10:FF:000004; Hemagglutinin-neuraminidase; 1. DR Gene3D; 1.20.5.110; -; 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; Disulfide bond; Glycoprotein; Hemagglutinin; KW Host cell membrane; Host membrane; Host-virus interaction; Hydrolase; KW Membrane; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein; KW Virion; Virus entry into host cell. FT CHAIN 1..565 FT /note="Hemagglutinin-neuraminidase" FT /id="PRO_0000142641" FT TOPO_DOM 1..19 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 41..565 FT /note="Virion surface" FT /evidence="ECO:0000255" FT REGION 223..228 FT /note="Involved in neuraminidase activity" FT /evidence="ECO:0000250|UniProtKB:Q91UL0" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine; by host" FT CARBOHYD 267 FT /note="N-linked (GlcNAc...) asparagine; by host" FT CARBOHYD 504 FT /note="N-linked (GlcNAc...) asparagine; by host" FT DISULFID 161..185 FT DISULFID 175..236 FT DISULFID 227..240 FT DISULFID 333..454 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 365..375 FT DISULFID 448..458 FT DISULFID 528..539 FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:4JF7" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:4JF7" FT HELIX 78..82 FT /evidence="ECO:0007829|PDB:4JF7" FT HELIX 83..99 FT /evidence="ECO:0007829|PDB:4JF7" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:4JF7" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:4JF7" FT TURN 121..125 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 161..169 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 174..184 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 192..202 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 206..218 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 224..232 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 247..252 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 258..265 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 270..275 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 300..309 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 314..319 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 337..346 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 351..355 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 356..367 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 376..379 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 382..384 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 391..396 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 399..404 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 414..434 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 466..470 FT /evidence="ECO:0007829|PDB:1Z4V" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 475..477 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 478..481 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 483..489 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 491..496 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 498..506 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 508..513 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 520..531 FT /evidence="ECO:0007829|PDB:1Z4V" FT TURN 532..535 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 536..546 FT /evidence="ECO:0007829|PDB:1Z4V" FT STRAND 548..564 FT /evidence="ECO:0007829|PDB:1Z4V" SQ SEQUENCE 565 AA; 62205 MW; 30A4A7068A25B563 CRC64; MVAEDAPVRA TCRVLFRTTT LIFLCTLLAL SISILYESLI TQKQIMSQAG STGSNSGLGS ITDLLNNILS VANQIIYNSA VALPLQLDTL ESTLLTAIKS LQTSDKLEQN CSWSAALIND NRYINGINQF YFSIAEGRNL TLGPLLNMPS FIPTATTPEG CTRIPSFSLT KTHWCYTHNV ILNGCQDHVS SNQFVSMGII EPTSAGFPFF RTLKTLYLSD GVNRKSCSIS TVPGGCMMYC FVSTQPERDD YFSAAPPEQR IIIMYYNDTI VERIINPPGV LDVWATLNPG TGSGVYYLGW VLFPIYGGVI KGTSLWNNQA NKYFIPQMVA ALCSQNQATQ VQNAKSSYYS SWFGNRMIQS GILACPLRQD LTNECLVLPF SNDQVLMGAE GRLYMYGDSV YYYQRSNSWW PMTMLYKVTI TFTNGQPSAI SAQNVPTQQV PRPGTGDCSA TNRCPGFCLT GVYADAWLLT NPSSTSTFGS EATFTGSYLN TATQRINPTM YIANNTQIIS SQQFGSSGQE AAYGHTTCFR DTGSVMVYCI YIIELSSSLL GQFQIVPFIR QVTLS //