HN_MUMPM
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-JUN-2021, entry version 117.
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; 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}.
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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 Proteomes; UP000002331; Genome.
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; 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
