HN_SENDZ
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 25-MAY-2022, entry version 127.
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.
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 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: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; 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 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 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
