ID   HN_PI3B                 Reviewed;         572 AA.
AC   P06167;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-JUN-2021, entry version 120.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Bovine parainfluenza 3 virus (BPIV-3).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11215;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=910N;
RX   PubMed=3031615; DOI=10.1093/nar/15.7.2945;
RA   Suzu S., Sakai Y., Shioda T., Shibuta H.;
RT   "Nucleotide sequence of the bovine parainfluenza 3 virus genome: the genes
RT   of the F and HN glycoproteins.";
RL   Nucleic Acids Res. 15:2945-2958(1987).
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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000305}.
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DR   EMBL; Y00114; CAA68298.1; -; Genomic_RNA.
DR   EMBL; D84095; BAA12218.1; -; Genomic_RNA.
DR   SMR; P06167; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   Proteomes; UP000133413; 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   Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW   Host-virus interaction; Hydrolase; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..572
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142624"
FT   TOPO_DOM        1..30
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..572
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   572 AA;  64590 MW;  DDF84E90C4EC87B4 CRC64;
     MEYWKHTNST KDTNNELGTT RDRHSSKATN IIMYIFWTTT STILSVIFIM ILINLIQENN
     HNKLMLQEIR KEFAAIDTKI QKTSDDIGTS IQSGINTRLL TIQSHVQNYI PLSLTQQMSD
     LRKFINDLTT KREHQEVPIQ RMTHDSGIEP LNPDKFWRCT SGNPSLTSSP KIRLIPGPGL
     LATSTTVNGC IRLPSLAINN LIYAYTSNLI TQGCQDIGKS YQVLQIGIIT INSDLVPDLN
     PRVTHTFNID DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASTGIEDIVL DIVTSNGLII
     TTRFTNNNIT FDKPYAALYP SVGPGIYYKD KVIFLGYGGL EHEENGDVIC NTTGCPGKTQ
     RDCNQASYSP WFSNRRMVNS IIVVDKGIDT TFSLRVWTIP MRQNYWGSEG RLLLLGDRIY
     IYTRSTSWHS KLQLGVIDIS DFNNIRINWT WHNVLSRPGN DECPWGHSCP DGCITGVYTD
     AYPLNPSGSI VSSVILDSQK SRENPIITYS TATNRVNELA IYNRTLPAAY TTTNCITHYD
     KGYCFHIVEI NHRSLNTFQP MLFKTEVPKN CS