ID   HN_SENDZ                Reviewed;         575 AA.
AC   P04853; P06863; P27562;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-NOV-2023, entry version 132.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            Short=HN protein;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus; Respirovirus muris.
OX   NCBI_TaxID=11198;
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=2991016; DOI=10.1016/0014-5793(85)80885-1;
RA   Miura N., Nakatani Y., Ishiura M., Uchida T., Okada Y.;
RT   "Molecular cloning of a full-length cDNA encoding the hemagglutinin-
RT   neuraminidase glycoprotein of Sendai virus.";
RL   FEBS Lett. 188:112-116(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3005975; DOI=10.1093/nar/14.4.1545;
RA   Shioda T., Iwasaki K., Shibuta H.;
RT   "Determination of the complete nucleotide sequence of the Sendai virus
RT   genome RNA and the predicted amino acid sequences of the F, HN and L
RT   proteins.";
RL   Nucleic Acids Res. 14:1545-1563(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Mutant F1-R, and Mutant ts-f1;
RX   PubMed=2161155; DOI=10.1016/0042-6822(90)90040-x;
RA   Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
RA   Klenk H.-D., Rott R., Seto J.T.;
RT   "Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L
RT   proteins of two host range mutants of Sendai virus.";
RL   Virology 176:656-657(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Mutant F1-R / T-5 revertant;
RX   PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA   Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA   Seto J.T.;
RT   "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT   virus.";
RL   Virology 184:227-234(1991).
RN   [5]
RP   BINDING TO SIALIC ACID-CONTAINING CELL RECEPTORS.
RX   PubMed=6255459; DOI=10.1073/pnas.77.10.5693;
RA   Markwell M.A.K., Paulson J.C.;
RT   "Sendai virus utilizes specific sialyloligosaccharides as host cell
RT   receptor determinants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:5693-5697(1980).
RN   [6]
RP   GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511.
RX   PubMed=6263875; DOI=10.1016/s0021-9258(19)69207-0;
RA   Yoshima H., Nakanishi M., Okada Y., Kobata A.;
RT   "Carbohydrate structures of HVJ (Sendai virus) glycoproteins.";
RL   J. Biol. Chem. 256:5355-5361(1981).
RN   [7]
RP   MUTAGENESIS OF CYS-55.
RX   PubMed=7941317; DOI=10.1006/viro.1994.1564;
RA   Bousse T., Takimoto T., Gorman W.L., Takahashi T., Portner A.;
RT   "Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza
RT   virus type-1 and Sendai virus important for membrane fusion.";
RL   Virology 204:506-514(1994).
RN   [8]
RP   INTERACTION WITH F PROTEIN.
RX   PubMed=8709235; DOI=10.1128/jvi.70.9.6112-6118.1996;
RA   Tanabayashi K., Compans R.W.;
RT   "Functional interaction of paramyxovirus glycoproteins: identification of a
RT   domain in Sendai virus HN which promotes cell fusion.";
RL   J. Virol. 70:6112-6118(1996).
RN   [9]
RP   INCORPORATION IN THE VIRION.
RX   PubMed=9811709; DOI=10.1128/jvi.72.12.9747-9754.1998;
RA   Takimoto T., Bousse T., Coronel E.C., Scroggs R.A., Portner A.;
RT   "Cytoplasmic domain of Sendai virus HN protein contains a specific sequence
RT   required for its incorporation into virions.";
RL   J. Virol. 72:9747-9754(1998).
RN   [10]
RP   GLYCOSYLATION AT ASN-77; ASN-499 AND ASN-511, AND MUTAGENESIS OF ASN-77;
RP   ASN-448; ASN-499 AND ASN-511.
RX   PubMed=10876159; DOI=10.1093/oxfordjournals.jbchem.a022731;
RA   Segawa H., Yamashita T., Kawakita M., Taira H.;
RT   "Functional analysis of the individual oligosaccharide chains of sendai
RT   virus fusion protein.";
RL   J. Biochem. 128:65-72(2000).
RN   [11]
RP   INTERACTION WITH M PROTEIN.
RX   PubMed=11040121; DOI=10.1006/viro.2000.0556;
RA   Ali A., Nayak D.P.;
RT   "Assembly of Sendai virus: M protein interacts with F and HN proteins and
RT   with the cytoplasmic tail and transmembrane domain of F protein.";
RL   Virology 276:289-303(2000).
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.
CC   -!- FUNCTION: Neuraminidase activity ensures the efficient spread of the
CC       virus by dissociating the mature virions from the neuraminic acid
CC       containing glycoproteins.
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       (Probable). Interacts with F protein trimer.
CC       {ECO:0000269|PubMed:11040121, ECO:0000269|PubMed:8709235, ECO:0000305}.
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.
CC       {ECO:0000269|PubMed:10876159, ECO:0000269|PubMed:6263875}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; X03614; CAA27274.1; -; Genomic_RNA.
DR   EMBL; M30202; AAB06282.1; -; Genomic_RNA.
DR   EMBL; M30203; AAB06288.1; -; Genomic_RNA.
DR   EMBL; M30204; AAB06200.1; -; Genomic_RNA.
DR   EMBL; M69046; AAB06294.1; -; Genomic_RNA.
DR   EMBL; X02808; CAA26576.1; -; mRNA.
DR   PIR; A00878; HNNZSZ.
DR   PIR; A24004; HNNZSH.
DR   SMR; P04853; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyConnect; 210; 8 N-Linked glycans.
DR   GlyCosmos; P04853; 3 sites, 15 glycans.
DR   iPTMnet; P04853; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SABIO-RK; P04853; -.
DR   Proteomes; UP000110830; Genome.
DR   Proteomes; UP000163956; Genome.
DR   Proteomes; UP000169749; Genome.
DR   Proteomes; UP000181310; 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; TAS:Reactome.
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_0000142640"
FT   TOPO_DOM        1..37
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..575
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          10..14
FT                   /note="Incorporation in virion"
FT   REGION          59..140
FT                   /note="Interaction with F protein"
FT   COMPBIAS        10..27
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:0000269|PubMed:10876159,
FT                   ECO:0000269|PubMed:6263875"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:10876159,
FT                   ECO:0000269|PubMed:6263875"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:10876159,
FT                   ECO:0000269|PubMed:6263875"
FT   DISULFID        129
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   VARIANT         23
FT                   /note="P -> L (in strain: wild-type, mutant F1-R, mutant
FT                   ts-f1 and mutant F1-R / T-5 revertant)"
FT   VARIANT         33
FT                   /note="A -> V (in strain: wild-type, mutant F1-R, mutant
FT                   ts-f1 and mutant F1-R / T-5 revertant)"
FT   VARIANT         148
FT                   /note="D -> E (in strain: wild-type, mutant F1-R, mutant
FT                   ts-f1 and mutant F1-R / T-5 revertant)"
FT   VARIANT         238
FT                   /note="F -> I"
FT   VARIANT         405
FT                   /note="Q -> E (in strain: mutant F1-R, mutant ts-f1 and
FT                   mutant F1-R / T-5 revertant)"
FT   MUTAGEN         55
FT                   /note="C->W: 45% loss of cell surface expression; 88% loss
FT                   of fusion promotion activity."
FT                   /evidence="ECO:0000269|PubMed:7941317"
FT   MUTAGEN         77
FT                   /note="N->G: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:10876159"
FT   MUTAGEN         448
FT                   /note="N->G: No effect."
FT                   /evidence="ECO:0000269|PubMed:10876159"
FT   MUTAGEN         499
FT                   /note="N->G: Loss of glycosylation; 88% loss of
FT                   neuraminidase activity."
FT                   /evidence="ECO:0000269|PubMed:10876159"
FT   MUTAGEN         511
FT                   /note="N->G: Loss of glycosylation; 88% loss of
FT                   neuraminidase activity."
FT                   /evidence="ECO:0000269|PubMed:10876159"
SQ   SEQUENCE   575 AA;  63410 MW;  721DC135844636CC CRC64;
     MDGDRGKRDS YWSTSPSGST TKPASGWERS SKADTWLLIL SFTQWALSIA TVIICIIISA
     RQGYSMKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD
     VIQMIDKSCS RQELTQHCES TIAVHHADGI APLEPHSFWR CPVGEPYLSS DPEISLLPGP
     SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD
     LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGR
     TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV
     SQDTCNEALK ITWLGGKQVV SVIIQVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR
     VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN KECNWYNKCP KECISGVYTD
     AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEAAY TTTSCITHFG
     KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES
//