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   16-JUN-2009, entry version 65.
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; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; Respirovirus.
OX   NCBI_TaxID=11196;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=36483; Cricetidae sp. (Hamster).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=85201677; 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
RT   to the influenza virus glycoproteins.";
RL   Cell 41:269-278(1985).
CC   -!- FUNCTION: Attaches the virus to sialic acid-containing cell
CC       receptors and thereby initiating infection. Binding of HN protein
CC       to the receptor induces a conformational change that allows the F
CC       protein to trigger virion/cell membranes fusion (By similarity).
CC   -!- FUNCTION: Neuraminidase activity ensures the efficient spread of
CC       the virus by dissociating the mature virions from the neuraminic
CC       acid containing glycoproteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates.
CC   -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers.
CC       Interacts with F protein trimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type II
CC       membrane protein (Potential). Host cell membrane; Single-pass type
CC       II membrane protein (Potential). Note=Folded in the endoplasmic
CC       reticulum (By similarity).
CC   -!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-
CC       type oligosaccharides and of complex-type oligosaccharides (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-
CC       neuraminidase family.
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DR   EMBL; M12397; AAA47810.1; -; Genomic_RNA.
DR   PIR; A00877; HNNZS.
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 to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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:0004308; F:exo-alpha-sialidase activity; IEA:EC.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0019058; P:viral infectious cycle; IEA:InterPro.
DR   InterPro; IPR000665; Hemagglutn-neuramid_glycoprot.
DR   InterPro; IPR016285; Hemagglutn-neuramid_paramyxo.
DR   Pfam; PF00423; HN; 1.
DR   PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Envelope protein; Glycoprotein;
KW   Hemagglutinin; Hydrolase; Membrane; Signal-anchor; Transmembrane;
KW   Virion.
FT   CHAIN         1    576       Hemagglutinin-neuraminidase.
FT                                /FTId=PRO_0000142638.
FT   TOPO_DOM      1     37       Cytoplasmic (By similarity).
FT   TRANSMEM     38     58       By similarity.
FT   TOPO_DOM     59    576       Extracellular (By similarity).
FT   REGION       10     14       Incorporation in virion (By similarity).
FT   REGION       59    140       Involved in interaction with F protein
FT                                (By similarity).
FT   CARBOHYD     77     77       N-linked (GlcNAc...); by host (By
FT                                similarity).
FT   CARBOHYD    499    499       N-linked (GlcNAc...); by host (By
FT                                similarity).
FT   CARBOHYD    511    511       N-linked (GlcNAc...); by host (By
FT                                similarity).
FT   DISULFID    129    129       Interchain (Potential).
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
//