ID   HN_SV41                 Reviewed;         568 AA.
AC   P25180;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   07-APR-2021, entry version 117.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Simian virus 41 (SV41).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus.
OX   NCBI_TaxID=2560766;
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Toshiba/Chanock;
RX   PubMed=2173260; DOI=10.1016/0042-6822(90)90141-d;
RA   Tsurudome M., Bando H., Nishio M., Iwamoto Y., Kawano M., Kondo K.,
RA   Komada H., Ito Y.;
RT   "Antigenic and structural properties of a paramyxovirus simian virus 41
RT   (SV41) reveal a close relationship with human parainfluenza type 2 virus.";
RL   Virology 179:738-748(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}.
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DR   EMBL; M62733; AAA47451.1; -; Genomic_RNA.
DR   EMBL; X64275; CAA45568.1; -; Genomic_RNA.
DR   PIR; A36419; HNNZ41.
DR   SMR; P25180; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   PRIDE; P25180; -.
DR   Proteomes; UP000108270; 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   3: Inferred from homology;
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..568
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142645"
FT   TOPO_DOM        1..18
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..568
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   568 AA;  61733 MW;  7C09738E2715F548 CRC64;
     MSGAEGNTNK RTFRAVFRTL IILITLTILA LSAAILYEVT HTSNGSESNN QVFDPTDTLN
     AITGNIKSMI ALLNQILYNA AIALPLKIDS TESVLLAAIK DLQFSNPASQ NCSSGGNLLN
     DALYINGINQ YLLSNSFAGT VGLGPLLNIP SFIPSATAPG GCTRIPSFSL TKTHWCYSHN
     VILAGCADSK ASNQYLAMGI VEQSSADFPF FRTMRTLYLS DGINRKSCSI VAIPGGCALY
     CYVATKTEQE DYAATTPSEL RLTFYYYNET LVERTLTIPN VTGNWATLNP AVGSGVYHLG
     YLAFPVYGGL IQNSAAWNSQ FGSYFLPQNP AVQCSGSAEQ QINTAKGSYV VNWFSGRLIQ
     SAVLVCPLSD QLTDQCRVVL FNNSETMMGA EGRLYTIGGD LYYYQRSSSW WTASLLYKIN
     TDFSQGLPPL IEAQWVPTYL VPRPGAQPCS AGNFCPANCI TGVYADVWPM NNPFPAGSSG
     VNPNYLFGGA FLWADVARVN PTFYMASATQ YKNTTGFPNS NQKAAYTSTT CFQNTGSKKI
     YCLFIIEMGS SLMGEFQIVP FLREVIIT