ID   HN_PI3HT                Reviewed;         572 AA.
AC   P12562;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   07-OCT-2020, entry version 106.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Human parainfluenza 3 virus (strain Tex/545/80) (HPIV-3).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11219;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2827373; DOI=10.1016/0042-6822(88)90402-3;
RA   van Wyke Coelingh K.L., Winter C.C., Murphy B.R.;
RT   "Nucleotide and deduced amino acid sequence of hemagglutinin-neuraminidase
RT   genes of human type 3 parainfluenza viruses isolated from 1957 to 1983.";
RL   Virology 162:137-143(1988).
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; M18762; AAA46849.1; -; Genomic_RNA.
DR   PIR; D29970; HNNZ80.
DR   SMR; P12562; -.
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   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_0000142627"
FT   TOPO_DOM        1..31
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..572
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
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        523
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   572 AA;  64259 MW;  57892E312D5F5F1B CRC64;
     MEYWKHTNHG KDAGNELETS MATHGNKLTN KIIYILWTII LVLLSIVFII VLTNSIKSEK
     AHESLLRDIN NEFIGITEKI QMASDNTNDL IQSGVNTRLL TIQSHVQNYI PISLTQQMSD
     LRKFISEITI RNDNQEVLPQ RITHDVGIKP LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL
     LAMPTTVDGC IRTPSLVIND LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN
     PRISHTFNIN DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNYDGSIS
     TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPIDENVIC NTTGCPGKTQ
     RDCNQASHSP WFSDRRMVNS IIVVDKGLNS TPKLKVWTIS MRQNYWGSEG RLLLLGNKIY
     IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT WHNVLSRPGN NECPWGHSCP DGCITGVYTD
     AYPLNPTGSI VSSVILDSQK SRVNPVITYS TATERVNELA IRNRTLSAGY TTTSCITHYN
     KGYCFHIVEI NHKSSNTFQP MLFKTEIPKS CS