HN_SENDA
ID HN_SENDA Reviewed; 575 AA.
AC Q783Y1; Q7T415; Q7TB20; Q82459;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE Short=HN protein;
DE EC=3.2.1.18;
GN Name=HN;
OS Sendai virus (strain Hamamatsu) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=302271;
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=8198441; DOI=10.1007/bf01309773;
RA Sakaguchi T., Fujii Y., Kiyotani K., Sasaki M., Yoshida T.;
RT "A field isolate of Sendai virus: its high virulence to mice and genetic
RT divergence from prototype strains.";
RL Arch. Virol. 135:159-164(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11210938; DOI=10.1023/a:1008130318633;
RA Fujii Y., Kiyotani K., Yoshida T., Sakaguchi T.;
RT "Conserved and non-conserved regions in the Sendai virus genome: evolution
RT of a gene possessing overlapping reading frames.";
RL Virus Genes 22:47-52(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate E15cl2;
RX PubMed=12163573; DOI=10.1128/jvi.76.17.8540-8547.2002;
RA Fujii Y., Sakaguchi T., Kiyotani K., Huang C., Fukuhara N., Egi Y.,
RA Yoshida T.;
RT "Involvement of the leader sequence in Sendai virus pathogenesis revealed
RT by recovery of a pathogenic field isolate from cDNA.";
RL J. Virol. 76:8540-8547(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate E15cl2, Isolate E30cl2, and Isolate E30M15cl5;
RX PubMed=12416681; DOI=10.1023/a:1020165919672;
RA Fujii Y., Sakaguchi T., Kiyotani K., Huang C., Fukuhara N., Yoshida T.;
RT "Identification of mutations associated with attenuation of virulence of a
RT field Sendai virus isolate by egg passage.";
RL Virus Genes 25:189-193(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate E50cl9;
RA Fujii Y., Kiyotani K., Huang C., Fukuhara N., Egi K., Yoshida T.,
RA Sakaguchi T.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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; X57213; CAA40499.1; -; Genomic_RNA.
DR EMBL; AB039658; BAB20025.1; -; Genomic_RNA.
DR EMBL; AB065186; BAC79131.1; -; Genomic_RNA.
DR EMBL; AB065187; BAC07511.1; -; Genomic_RNA.
DR EMBL; AB065188; BAC79139.1; -; Genomic_RNA.
DR EMBL; AB065189; BAC79147.1; -; Genomic_RNA.
DR PIR; S14532; S14532.
DR SMR; Q783Y1; -.
DR Proteomes; UP000007191; Genome.
DR Proteomes; UP000008510; Genome.
DR Proteomes; UP000008857; Genome.
DR Proteomes; UP000180650; Genome.
DR Proteomes; UP000180718; 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 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_0000142636"
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 461
FT /note="E -> G (in strain: Isolate E30cl2; egg passage
FT attenuated)"
FT VARIANT 462
FT /note="D -> G (in strain: Isolate E30cl2, Isolate E50cl9
FT and Isolate E30M15cl5; egg passage attenuated)"
SQ SEQUENCE 575 AA; 63212 MW; BDA9E1B72431058A CRC64;
MDGDRSKRDS YWSTSPGGST TKLVSDSERS GKVDTWLLIL AFTQWALSIA TVIICIVIAA
RQGYSMERYS MTVEALNTSN KEVKESLTSL IRQEVITRAV NIQSSVQTGI PVLLNKNSRD
VIQLIEKSCN RQELTQLCDS TIAVHHAEGI APLEPHSFWR CPAGEPYLSS DPEVSLLPGP
SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD
LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDILDLKGR
TKSHRYSNSE IDLDHPFSAL YPSVGSGIAT EGSLIFLGYG GLTTPLQGDT KCRIQGCQQV
SQDTCNEALK ITWLGGKQVV SVLIQVNDYL SERPRIRVTT VPITQNYLGA EGRLLKLGDQ
VYIYTRSSGW HSQLQIGVLD VSHPLTISWT PHEALSRPGN EDCNWYNTCP KECISGVYTD
AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVKLEAAY TTTSCITHFG
KGYCFHIIEI NQKSLNTLQP MLFKTSIPKL CKAES
