ID   HN_SENDO                Reviewed;         575 AA.
AC   Q88261; O57288;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   08-NOV-2023, entry version 116.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            Short=HN protein;
DE            Short=Protein HANA;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Sendai virus (strain Ohita) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus; Respirovirus muris.
OX   NCBI_TaxID=302272;
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate vaccinal MVCES1;
RX   PubMed=8151795; DOI=10.1128/jvi.68.5.3369-3373.1994;
RA   Wang X.-L., Itoh M., Hotta H., Homma M.;
RT   "A protease activation mutant, MVCES1, as a safe and potent live vaccine
RT   derived from currently prevailing Sendai virus.";
RL   J. Virol. 68:3369-3373(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate MVC11;
RX   PubMed=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA   Itoh M., Isegawa Y., Hotta H., Homma M.;
RT   "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT   mutations from a highly virulent field strain through adaptation to LLC-MK2
RT   cells.";
RL   J. Gen. Virol. 78:3207-3215(1997).
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   -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers.
CC       Interacts with F protein trimer (By similarity). {ECO:0000250}.
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}. Note=Folded in the
CC       endoplasmic reticulum. {ECO:0000250}.
CC   -!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-type
CC       oligosaccharides and of complex-type oligosaccharides. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; D26475; BAA05487.1; -; Genomic_RNA.
DR   EMBL; AB005795; BAA24391.1; -; Genomic_RNA.
DR   EMBL; AB005796; BAA24400.1; -; Genomic_RNA.
DR   RefSeq; NP_056878.1; NC_001552.1.
DR   SMR; Q88261; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyCosmos; Q88261; 3 sites, No reported glycans.
DR   KEGG; vg:1489776; -.
DR   Proteomes; UP000006563; Genome.
DR   Proteomes; UP000007311; Segment.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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   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   3: Inferred from homology;
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..575
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142639"
FT   TOPO_DOM        1..37
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        59..575
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          10..14
FT                   /note="Incorporation in virion"
FT                   /evidence="ECO:0000250"
FT   REGION          59..140
FT                   /note="Involved in interaction with F protein"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        10..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250"
FT   DISULFID        129
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   VARIANT         123
FT                   /note="R -> Q (in strain: Isolate vaccinal MVCES1)"
SQ   SEQUENCE   575 AA;  63238 MW;  36AA3CD8BFF817D2 CRC64;
     MDGDRSKRDS YWSTSPGGST TKLVSDSERS GKVDTWLLIL AFTQWALSIA TVIICIVIAA
     RQGYSMERYS MTVEALNTSN KEVKESLTSL IRQEVITRAA NIQSSVQTGI PVLLNKNSRD
     VIRLIEKSCN RQELTQLCDS TIAVHHAEGI APLEPHSFWR CPAGEPYLSS DPEVSLLPGP
     SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD
     LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPIVDERT DYSSDGIEDL VLDILDLKGR
     TKSHRYSNSE IDLDHPFSAL YPSVGSGIAT EGSLIFLGYG GLTTPLQGDT KCRIQGCQQV
     SQDTCNEALK ITWLGGKQVV SVLIQVNDYL SERPRIRVTT IPITQNYLGA EGRLLKLGDQ
     VYIYTRSSGW HSQLQIGVLD VSHPLTISWT PHEALSRPGN EDCNWYNTCP KECISGVYTD
     AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG
     KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES
//