ID   HN_PI1HW                Reviewed;         575 AA.
AC   P16071;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   13-SEP-2023, entry version 115.
DE   RecName: Full=Hemagglutinin-neuraminidase;
DE            EC=3.2.1.18;
GN   Name=HN;
OS   Human parainfluenza 1 virus (strain Washington/1957) (HPIV-1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus; Respirovirus laryngotracheitidis.
OX   NCBI_TaxID=11211;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1689918; DOI=10.1016/0042-6822(90)90201-2;
RA   Gorman W.L., Gill D.S., Scroggs R.A., Portner A.;
RT   "The hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus
RT   type 1 and Sendai virus have high structure-function similarity with
RT   limited antigenic cross-reactivity.";
RL   Virology 175:211-221(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; M31228; AAA46798.1; -; Genomic_RNA.
DR   PIR; A34682; HNNZ39.
DR   SMR; P16071; -.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GlyCosmos; P16071; 3 sites, No reported glycans.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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   Gene3D; 2.120.10.10; -; 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; Sialidases; 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..575
FT                   /note="Hemagglutinin-neuraminidase"
FT                   /id="PRO_0000142621"
FT   TOPO_DOM        1..34
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..575
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   575 AA;  63981 MW;  63E55E481A0DB322 CRC64;
     MAEKGKTNSS YWSTTRNDNS TVNTYIDTPA GKTHIWLLIA TTMHTILSFI IMILCIDLII
     KQDTCMKTNI MTVSSMNESA KTIKETITEL IRQEVISRTI NIQSSVQSGI PILLNKQSRD
     LTQLIEKSCN RQELAQICEN TIAIHHADGI SPLDPHDFWR CPVGEPLLSN NPNISLLPGP
     SLLSGSTTIS GCVRLPSLSI GDAIYAYSSN LITQGCADIG KSYQVLQLGY ISLNSDMYPD
     LKPVISHTYD INDNRKSCSV IAAGTRGYQL CSLPTVNETT DYSSEGIEDL VFDILDLKGK
     TKSHRYKNED ITFDHPFSAM YPSVGSGIKI ENTLIFLGYG GLTTPLQGDT KCVTNRCANV
     NQSVCNDALK ITWLKKRQVV NVLIRINNYL SDRPKIVVET IPITQNYLGA EGRLLKLGKK
     IYIYTRSSGW HSHLQIGSLD INNPMTIKWA PHEVLSRPGN QDCNWYNRCP RECISGVYTD
     AYPLSPDAVN VATTTLYANT SRVNPTIMYS NTSEIINMLR LKNVQLEAAY TTTSCITHFG
     KGYCFHIVEI NQTSLNTLQP MLFKTSIPKI CKITS
//