ID   HN_MUMPR                Reviewed;         582 AA.
AC   P10866;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   07-APR-2021, entry version 106.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Mumps virus (strain RW) (MuV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Mumps orthorubulavirus.
OX   NCBI_TaxID=11172;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3369084; DOI=10.1016/0042-6822(88)90544-2;
RA   Waxham M.N., Aronowski J., Server A.C., Wolinsky J.S., Smith J.A.,
RA   Goodman H.M.;
RT   "Sequence determination of the mumps virus HN gene.";
RL   Virology 164:318-325(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}.
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DR   EMBL; M19933; AAA46609.1; -; mRNA.
DR   PIR; A28917; HNNZMP.
DR   SMR; P10866; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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   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; SSF50939; 1.
PE   2: Evidence at transcript level;
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..582
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142604"
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        507
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   582 AA;  64045 MW;  6BCCB6990E65F869 CRC64;
     MEPSKLFTIS DNATFAPGPV NNAADKKTFR TCFRILVLSV QAVTLILVIV TLGELVRMIN
     DQGLSNQLSS ITDKIRESAT MIASAVGVMN QVIHGVTVSL PLQIEGNQNQ LLSTLATICT
     SKKQISNCST NIPLVNDLRF INGINKFIIE DYANHDFSIG HPLNMPSFIP TATSPNGCTR
     IPSFSLGKTH WCYTHNVINA NCKDHTSSNQ YVSMGILVQT ASGYPMFKTL KIQYLSDGLN
     RKSCSIATVP DGCAMYCYVS TQLETDDYAG SSPPTQKLTL LFYNDTVTER TISPSGLEGN
     WATLVPGVGS GIYFENKLIF PAYGGVLPNS TLGVKLAREF FRPVNPYNPC SGPQQDLDQR
     ALRSYFPSYL SNRRVQSAFL VCAWNQILVT NCELVVPSNN QTLMGAEGRV LLINNRLLYY
     QRSTSWWPYE LLYEISFTFT NSGQSSVNMS WIPIYSFTRP GSGKCSGENV CPIACVSGVY
     LDPWPLTPYS HQSGINRNFY FTGALLNSST TRVNPTLYVS ALNNLKVLAP YGTQGLSASY
     TTTTCFQDTG DASVYCVYIM ELASNIVGEF QILPVLTRLT IT