HN_SENDH
ID HN_SENDH Reviewed; 576 AA.
AC P03425;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 114.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE Short=HN protein;
DE EC=3.2.1.18;
GN Name=HN;
OS Sendai virus (strain Harris) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11196;
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=2986845; DOI=10.1016/0092-8674(85)90080-7;
RA Blumberg B.M., Giorgi C., Roux L., Raju R., Dowling P., Chollet A.,
RA Kolakofsky D.;
RT "Sequence determination of the Sendai virus HN gene and its comparison to
RT the influenza virus glycoproteins.";
RL Cell 41:269-278(1985).
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; M12397; AAA47810.1; -; Genomic_RNA.
DR PIR; A00877; HNNZS.
DR SMR; P03425; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
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; Signal-anchor;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT CHAIN 1..576
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142638"
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..576
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"
SQ SEQUENCE 576 AA; 63515 MW; 01CD8067E038FC5B CRC64;
MDGDRGKRDS YWSTSPSGST TKLASGWERS SKVDTWLLIL SFTQWALSIA TVIICIIISA
RQGYSTKEYS MTVEALNMSS REVKESLTSL IRQEVIARAV NIQSSVQTGI PVLLNKNSRD
VIQMIDKSCS RQELTQLCES TIAVHHAEGI APLEPHSFWR CPVGEPYLSS DPKISLLLGP
SLLSGSTTIS GCVRLPSLSI GEAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMFPD
LNPVVSHTYD INDNRKSCSV VATGTRGYQL CSMPTVDERT DYSSDGIEDL VLDVLDLKGS
TKSHRYRNSE VDLDHPFSAL YPSVGNGIAT EGSLIFLGYG GLTTPLQGDT KCRTQGCQQV
SQDTCNEALK ITWLGGKQVV NVIIRVNDYL SERPKIRVTT IPITQNYLGA EGRLLKLGDR
VYIYTRSSGW HSQLQIGVLD VSHPLTINWT PHEALSRPGN KECNWYNTCP KECISGVYTD
AYPLSPDAAN VATVTLYANT SRVNPTIMYS NTTNIINMLR IKDVQLEVAY TTISSCITHF
GKGYCFHIIE INQKSLNTLQ PMLFKTSIPK LCKAES
