HN_SENDO
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 02-JUN-2021, entry version 112.
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.
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 GeneID; 1489776; -.
DR KEGG; vg:1489776; -.
DR Proteomes; UP000006563; Genome.
DR Proteomes; UP000007311; 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_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
