ID HN_MUMPM Reviewed; 582 AA. AC P11235; Q783V7; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 08-NOV-2023, entry version 121. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Mumps virus (strain Miyahara vaccine) (MuV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae; OC Orthorubulavirus; Orthorubulavirus parotitidis; Mumps orthorubulavirus. OX NCBI_TaxID=11171; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2762157; DOI=10.1093/nar/17.14.5840; RA Takeuchi K., Tanabayashi K., Hishiyama M., Yamada A., Sugiura A.; RT "Cloning and sequencing of the haemagglutinin-neuraminidase gene of mumps RT virus (Miyahara strain)."; RL Nucleic Acids Res. 17:5840-5840(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1585659; DOI=10.1016/0042-6822(92)90555-4; RA Okazaki K., Tanabayashi K., Takeuchi K., Hishiyama M., Okazaki K., RA Yamada A.; RT "Molecular cloning and sequence analysis of the mumps virus gene encoding RT the L protein and the trailer sequence."; RL Virology 188:926-930(1992). 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; X15284; CAA33358.1; -; mRNA. DR EMBL; AB040874; BAA94390.1; -; Genomic_RNA. DR PIR; A34054; HNNZMM. DR SMR; P11235; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P11235; 7 sites, No reported glycans. DR Proteomes; UP000002331; 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; 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 2: Evidence at transcript 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..582 FT /note="Hemagglutinin-neuraminidase" FT /id="PRO_0000142603" FT TOPO_DOM 1..34 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 35..55 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 56..582 FT /note="Virion surface" FT /evidence="ECO:0000255" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 400 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 448 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 464 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 507 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" SQ SEQUENCE 582 AA; 64044 MW; 9902600339625499 CRC64; MEPSKLFTMS DNATFAPGPV INAADKKTFR TCFRILVLSV QAVTLILVIV TLGELVRMIN DQGLSNQLSS IADKIRESAT MIASAVGVMN QVIHGVTVSL PLQIEGNQNQ LLSTLATICT GKKQVSNCST NIPLVNDLRF INGINKFIIE DYATHDFSIG HPLNMPSFIP TATSPNGCTR IPSFSLGKTH WCYTHNVINA NCKDHTSSNQ YISMGILVQT ASGYPMFKTL KIQYLSDGLN RKSCSIATVP DGCAMYCYVS TQLETDDYAG SSPPTQKLTL LFYNDTVTER TISPTGLEGN WATLVPGVGS GIYFENKLIF PAYGGVLPNS SLGVKSAREF FRPVNPYNPC SGPQQDLDQR ALRSYFPSYF SNRRVQSAFL VCAWNQILVT NCELVVPSNN QTLMGAEGRV LLINNRLLYY QRSTSWWPYE LLYEISFTFT NSGQSSVNMS WIPIYSFTRP GSGNCSGENV CPTACVSGVY LDPWPLTPYS HQSGINRNFY FTGALLNSST TRVNPTLYVS ALNNLKVLAP YGNQGLFASY TTTTCFQDTG DASVYCVYIM ELASNIVGEF QILPVLTRLT IT //