ID   HN_PI4HA                Reviewed;         573 AA.
AC   P21526;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   07-APR-2021, entry version 105.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Human parainfluenza 4a virus (strain Toshiba) (HPIV-4a).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Human orthorubulavirus 4.
OX   NCBI_TaxID=11225;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2155512; DOI=10.1016/0042-6822(90)90213-b;
RA   Bando H., Kondo K., Kawano M., Komada H., Tsurudome M., Nishio M., Ito Y.;
RT   "Molecular cloning and sequence analysis of human parainfluenza type 4A
RT   virus HN gene: its irregularities on structure and activities.";
RL   Virology 175:307-312(1990).
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; M34033; AAA46799.1; -; Genomic_RNA.
DR   PIR; A34683; HNNZ4A.
DR   SMR; P21526; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   PRIDE; P21526; -.
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..573
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142632"
FT   TOPO_DOM        1..27
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..573
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   573 AA;  65544 MW;  3540F24F17931AC4 CRC64;
     MQDSHGNTQI LNQANSMVKR TWRLLFRIAT LILLVSIFVL SLIIVLQSTP GNLQNDINII
     RKELNELMEN FETTSKSLLS VSNQITYDVS VLTPIRQEAI ETNIISKIKD HCKDRVIKEG
     STCTLNRSPL HDVSFLNGFN KFYFTYKDNM QIKFKSLLDY PNFIPTATTP HGCIRIPSFS
     LGQTHWCYTH NINLLGCADP ASSNQYVSLG TLQVLKMGDP YFKVEHSHYL NDGRNRKSCS
     VVAVPDGCLR NCVTMTKNET ENFKDLNWQH NYLHTYHIMV PLKTRIINPP GSSRDWVHIA
     PGVGSGLLYA KLLIFPLYGG LTEKSVIHNN QSGKYFFPNS TKLQCRNSTM EKIKGAKDSY
     TITYFSGRLI QSAFLVCDLR QFLSEDCEIL IPSNDYMMVG AEGRLYNIEN NIFYYQRGSS
     WWPYPSLYRI RLNLSKKYPR ITEIKFTKIE IAPRPGNKDC PGNKACPKEC ITGVYQDILP
     LSYPNTAFPH LKQAYYTGFY LNNSLERRNP TFYTADNLDY HQQERLGKFN LTAGYSTTTC
     FKQTTTARLY CLYIIEVGDS VIGDFQITLF LAA