ID   HN_PIV5L                Reviewed;         565 AA.
AC   P28885;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Parainfluenza virus 5 (isolate Human/LN) (PIV5) (Simian virus 5).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Mammalian orthorubulavirus 5.
OX   NCBI_TaxID=31610;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1765772; DOI=10.1099/0022-1317-72-12-3103;
RA   Baty D.U., Southern J.A., Randall R.E.;
RT   "Sequence comparison between the haemagglutinin-neuraminidase genes of
RT   simian, canine and human isolates of simian virus 5.";
RL   J. Gen. Virol. 72:3103-3107(1991).
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   PIR; JQ1307; HNNZC3.
DR   SMR; P28885; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   PRIDE; P28885; -.
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..565
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142644"
FT   TOPO_DOM        1..19
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..565
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   565 AA;  62138 MW;  8F531BB8704F281D CRC64;
     MVAEDAPVRG TCRVLFRTTT LLFLCTLLSL SISILYESLI TQNQIMSQAG STGSNSGLGS
     ITDLLNNILS VANQIIYNSA VALPLQLDTL ESTLLTAFKS LQTSDKLEQN CSWGAALIND
     NRYINGINQF YFSIAEGRNL TLGPLLNILS FIPTATTPEG CTRIPSFSLT KTHWCYTHNV
     ILNGCQDHVS SNQFVSMGII EPTSAGFPSF RTLKTLYLSD GVNRKSCSIS TVPGGCMMYC
     FVSTQPERDD YFSAAPPEQR IIIMYYNDTI VERIINPPGV LDVWATLNPG TGSGVYYLGW
     VLFPIYGGVI KDTSLWNSQA NKYFIPQMVA ALCSQNQATQ VQNAKSSYYS SWFGNRMIQS
     GILACPLQQD LTNECLVLPF SNDQVLMGAE GRLYMYGDSV YYYQRSNSWW PMTMLYKVTI
     TFTNGQPSAI SAQNVPTQQV PRPGTGDCSA TNRCPGFCLT GVYADAWLLT NPSSTSTFGS
     EATFTGSYLN TATQRINPTM YIANNTQIIS SQQFGSSGQE AAYGHTTCFR DTGSVMVYCI
     YIIELSSSLL GQFQIVPFIR QVTLS