ID   HN_SENDF                Reviewed;         575 AA.
AC   P19758; Q88413;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   08-NOV-2023, entry version 122.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            Short=HN protein;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Sendai virus (strain Fushimi) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus; Respirovirus muris.
OX   NCBI_TaxID=11195;
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].
RX   PubMed=2173829; DOI=10.1093/nar/18.21.6427;
RA   Neubert W.J., Willenbrink W.;
RT   "Cloning and sequencing of the HN gene of Sendai virus (strain Fushimi).";
RL   Nucleic Acids Res. 18:6427-6427(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7625124; DOI=10.1016/0168-1702(94)00102-i;
RA   Heminaway B.R., Yang Y., Tanaka Y., Panin M., Huang Y.T., Galinski M.S.;
RT   "Role of basic residues in the proteolytic activation of Sendai virus
RT   fusion glycoprotein.";
RL   Virus Res. 36:15-35(1995).
RN   [3]
RP   INTERACTION WITH CHAPERONES.
RX   PubMed=10578061; DOI=10.1093/oxfordjournals.jbchem.a022554;
RA   Tomita Y., Yamashita T., Sato H., Taira H.;
RT   "Kinetics of interactions of sendai virus envelope glycoproteins, F and HN,
RT   with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin,
RT   and calreticulin.";
RL   J. Biochem. 126:1090-1100(1999).
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}.
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; X56131; CAA39596.1; -; Genomic_RNA.
DR   EMBL; U06433; AAC54272.1; -; Genomic_RNA.
DR   PIR; S12135; S12135.
DR   SMR; P19758; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyCosmos; P19758; 3 sites, No reported glycans.
DR   Proteomes; UP000006825; Genome.
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   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
KW   Host membrane; Host-virus interaction; Hydrolase; Membrane; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Virion; Virus entry into host cell.
FT   CHAIN           1..575
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142637"
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..24
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..24
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         86
FT                   /note="S -> T"
FT   VARIANT         525
FT                   /note="Q -> K"
SQ   SEQUENCE   575 AA;  63348 MW;  93FD0532F6147BF6 CRC64;
     MDGDRGKRDS YWSTSPSGST TKLASGWERS SKVDTWLLIL SFTQWALSIA TVIICIIISA
     RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD
     VIQMIDKSCS RQELTQLCES TIAVHHAEGI APLEPHSFWR CPVGEPYLSS DPKISLLPGP
     SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD
     LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGS
     TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV
     SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR
     VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN EECNWYNTCP KECISGVYTD
     AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG
     KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES
//