HN_MUMP1
ID HN_MUMP1 Reviewed; 582 AA.
AC P19762; P33480;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 07-APR-2021, entry version 110.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Mumps virus (strain SBL-1) (MuV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mumps orthorubulavirus.
OX NCBI_TaxID=11173;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2718627; DOI=10.1016/0168-1702(89)90056-7;
RA Koevamees J., Norrby E., Elango N.;
RT "Complete nucleotide sequence of the hemagglutinin-neuraminidase (HN) mRNA
RT of mumps virus and comparison of paramyxovirus HN proteins.";
RL Virus Res. 12:87-96(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-153.
RX PubMed=2165137; DOI=10.1099/0022-1317-71-7-1555;
RA Elliott G.D., Yeo R.P., Afzal M.A., Simpson E.J.B., Curran J.A., Rima B.K.;
RT "Strain-variable editing during transcription of the P gene of mumps virus
RT may lead to the generation of non-structural proteins NS1 (V) and NS2.";
RL J. Gen. Virol. 71:1555-1560(1990).
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; M55065; AAA74751.1; -; Genomic_RNA.
DR EMBL; D00663; BAA00563.1; -; Genomic_RNA.
DR PIR; A42758; HNNZSB.
DR SMR; P19762; -.
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 3: Inferred from homology;
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_0000142605"
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 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; 63885 MW; 18F95300AA33DC7F CRC64;
MEPSKLFIMS DNATVAPGPV VNAAGKKTFR TCFRILVLSV QAVTLILVIV TLGELIRMIN
DQGLSNQLSS ITDKIRESAA VIASAVGVMN QVIHGVTVSL PLQIEGNQNQ LLSTLATICT
NRNQVSNCST NIPLVNDLRF INGINKFIIE DYATHDFSIG NPLNMPSFIP TATSPNGCTR
IPSFSLGKTH WCYTHNVINA NCKDHTSSNQ YVSMGILVQT ASGYPMFKTL KIQYLSDGLN
RKSCSIATVP DGCAMYCYVS TQLEANDYAG SSPPTQKLTL LFYNDTITER TISPSGLEGN
WATLVPGVGS GIYFENKLIF PAYGGVLPNS TLGVKSAREF FRPVNPYNPC SGPPQELDQR
ALRSYFPRYF SSRRVQSAFL VCAWNQILVT NCELVVPSNN QTLMGAEGRV LLINNRLLYY
QRSTSWWPYE LLYEISFTFT NSGQSSVNMS WIPIYSFTPP GSGNCSGKNV CPTVCVSGVY
LDPWPLTPYS HQSGINRNFY FTGALLNSST TRVNPTLYVS ALNNLKVLAP YGTQGLFASY
TTTTCFQDTG DASVYCVYIM ELASNIVGEF QILPVLARLT IT
