ID HN_PI3H4 Reviewed; 572 AA. AC P08492; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 13-SEP-2023, entry version 124. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human OS parainfluenza 3 virus (strain NIH 47885)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae; OC Respirovirus; Respirovirus pneumoniae. OX NCBI_TaxID=11217; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3003381; DOI=10.1128/jvi.57.2.481-489.1986; RA Elango N., Coligan J.E., Jambou R.C., Venkatesan S.; RT "Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: RT nucleotide sequence of mRNA and limited amino acid sequence of the purified RT protein."; RL J. Virol. 57:481-489(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2825443; DOI=10.1016/0168-1702(87)90016-5; RA Galinski M.S., Mink M.A., Pons M.W.; RT "Molecular cloning and sequence analysis of the human parainfluenza 3 virus RT genes encoding the surface glycoproteins, F and HN."; RL Virus Res. 8:205-215(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2822598; DOI=10.1159/000149722; RA Storey D.G., Cote M.-J., Dimock K., Kang C.Y.; RT "Nucleotide sequence of the coding and flanking regions of the human RT parainfluenza virus 3 hemagglutinin-neuraminidase gene: comparison with RT other paramyxoviruses."; RL Intervirology 27:69-80(1987). RN [4] RP VARIANT NEURAMINIDASE-DEFICIENT ASN-216. RC STRAIN=Isolate C28; RX PubMed=8525632; DOI=10.1006/viro.1995.9925; RA Huberman K., Peluso R.W., Moscona A.; RT "Hemagglutinin-neuraminidase of human parainfluenza 3: role of the RT neuraminidase in the viral life cycle."; RL Virology 214:294-300(1995). RN [5] RP VARIANT 4-GU-DANA-RESISTANT ILE-193. RC STRAIN=Isolate ZM1; RX PubMed=12477836; DOI=10.1128/jvi.77.1.309-317.2003; RA Murrell M., Porotto M., Weber T., Greengard O., Moscona A.; RT "Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase RT causing increased receptor binding activity and resistance to the RT transition state sialic acid analog 4-GU-DANA (Zanamivir)."; RL J. Virol. 77:309-317(2003). 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 4.7.; 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; M17641; AAA46846.1; -; mRNA. DR EMBL; M21649; AAA46853.1; -; Genomic_RNA. DR EMBL; M20402; AAA46856.1; -; mRNA. DR PIR; A27765; HNNZP3. DR PDB; 4MZA; X-ray; 1.65 A; A/B=136-572. DR PDB; 4MZE; X-ray; 1.80 A; A/B=136-572. DR PDB; 4XJR; X-ray; 3.00 A; A/B=125-572. DR PDBsum; 4MZA; -. DR PDBsum; 4MZE; -. DR PDBsum; 4XJR; -. DR SMR; P08492; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P08492; 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 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..572 FT /note="Hemagglutinin-neuraminidase" FT /id="PRO_0000142625" 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" FT VARIANT 193 FT /note="T -> I (in strain: Isolate ZM1; 4-GU-DANA antiviral FT drug resistant and increased receptor binding avidity)" FT /evidence="ECO:0000269|PubMed:12477836" FT VARIANT 216 FT /note="D -> N (in strain: Isolate C28; 50% loss of FT neuraminidase activity)" FT /evidence="ECO:0000269|PubMed:8525632" FT VARIANT 567 FT /note="I -> V (in strain: Isolate ZM1)" FT CONFLICT 135 FT /note="Q -> R (in Ref. 2; AAA46853)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="V -> A (in Ref. 2; AAA46853)" FT /evidence="ECO:0000305" FT CONFLICT 489 FT /note="S -> G (in Ref. 3; AAA46856)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="S -> A (in Ref. 2 and 3)" FT /evidence="ECO:0000305" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 153..156 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:4MZE" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 190..198 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 203..215 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 221..231 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 235..247 FT /evidence="ECO:0007829|PDB:4MZA" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 254..261 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 264..270 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 276..281 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 299..304 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 331..342 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 360..366 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 377..386 FT /evidence="ECO:0007829|PDB:4MZA" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 392..398 FT /evidence="ECO:0007829|PDB:4MZA" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 410..415 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 418..423 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:4XJR" FT STRAND 433..438 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 481..485 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 488..496 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 498..503 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 505..513 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 515..522 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 526..538 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 541..552 FT /evidence="ECO:0007829|PDB:4MZA" FT TURN 553..556 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 557..566 FT /evidence="ECO:0007829|PDB:4MZA" FT STRAND 569..571 FT /evidence="ECO:0007829|PDB:4MZA" SQ SEQUENCE 572 AA; 64247 MW; BDCA6F9A41E20369 CRC64; MEYWKHTNHG KDAGNELETS MATHGNKITN KITYILWTII LVLLSIVFII VLINSIKSEK AHESLLQDVN NEFMEVTEKI QMASDNINDL IQSGVNTRLL TIQSHVQNYI PISLTQQMSD LRKFISEITI RNDNQEVPPQ RITHDVGIKP LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL LAMPTTVDGC VRTPSLVIND LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN PRISHTFNIN DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNHDGSIS TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPINENAIC NTTGCPGKTQ RDCNQASHSP WFSDRRMVNS IIVVDKGLNS IPKLKVWTIS MRQNYWGSEG RLLLLGNKIY IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT WHNVLSRPGN NECPWGHSCP DGCITGVYTD AYPLNPTGSI VSSVILDSQK SRVNPVITYS TSTERVNELA IRNKTLSAGY TTTSCITHYN KGYCFHIVEI NHKSLDTFQP MLFKTEIPKS CS //