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 02-SEP-2026, entry version 127. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18 {ECO:0000250|UniProtKB:Q9WAF5}; GN Name=HN; OS Mumps virus genotype B (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). RN [3] RP REVIEW. RX PubMed=35746805; DOI=10.3390/v14061335; RA Frost J.R., Shaikh S., Severini A.; RT "Exploring the Mumps Virus Glycoproteins: A Review."; RL Viruses 14:0-0(2022). CC -!- FUNCTION: Attaches the virus to alpha-2,3-linked sialic acid-containing CC cell receptors and thereby initiating infection (By similarity). CC Binding of HN protein to the receptor induces a conformational change CC that allows the F protein to trigger virion/cell membranes fusion (By CC similarity). Binds to the glycan motifs sialyl Lewis (SLe) and GM2 CC ganglioside (GM2-glycan) (By similarity). CC {ECO:0000250|UniProtKB:P19762, ECO:0000250|UniProtKB:Q786F2, CC ECO:0000250|UniProtKB:Q9WAF5}. CC -!- FUNCTION: Neuraminidase (sialidase) activity ensures the efficient CC spread of the virus by dissociating the mature virions from the CC neuraminic acid containing glycoproteins. CC {ECO:0000250|UniProtKB:Q91UL0}. 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:Q9WAF5}; 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 -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q8QV65}; CC Single-pass type II membrane protein {ECO:0000305}. Host cell membrane CC {ECO:0000305}; 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; X15284; CAA33358.1; -; mRNA. DR EMBL; AB040874; BAA94390.1; -; Genomic_RNA. DR PIR; A34054; HNNZMM. DR AlphaFoldDB; P11235; -. DR SMR; P11235; -. DR CAZy; GH83; Glycoside Hydrolase Family 83. DR GlyCosmos; P11235; 7 sites, No reported glycans. DR KEGG; vg:1489765; -. DR Proteomes; UP000002331; 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; ISS:UniProtKB. 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; IEA:UniProtKB-ARBA. DR GO; GO:0046718; P:symbiont 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 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 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane; KW Host membrane; Host-virus interaction; Hydrolase; Membrane; KW Reference proteome; 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 REGION 240..245 FT /note="Involved in neuraminidase activity" FT /evidence="ECO:0000250|UniProtKB:Q91UL0" FT SITE 180 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 242 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 264 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 323 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 369 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 407 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 422 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 512 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT SITE 540 FT /note="Binding to the glycan motifs of the host receptor" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 400 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 448 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 464 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT CARBOHYD 507 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 178..202 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 192..253 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 244..257 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 350..471 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 382..392 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 465..475 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" FT DISULFID 545..556 FT /evidence="ECO:0000250|UniProtKB:Q9WAF5" 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 //