HN_PI2HT
ID HN_PI2HT Reviewed; 571 AA.
AC P25466;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 07-APR-2021, entry version 121.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Human parainfluenza 2 virus (strain Toshiba) (HPIV-2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Human parainfluenza 2 virus.
OX NCBI_TaxID=11214;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2152995; DOI=10.1016/0042-6822(90)90081-2;
RA Kawano M., Bando H., Yuasa T., Kondo K., Tsurudome M., Komada H.,
RA Nishio M., Ito Y.;
RT "Sequence determination of the hemagglutinin-neuraminidase (HN) gene of
RT human parainfluenza type 2 virus and the construction of a phylogenetic
RT tree for HN proteins of all the paramyxoviruses that are infectious to
RT humans.";
RL Virology 174:308-313(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; X57559; CAA40787.1; -; mRNA.
DR PIR; A33777; HNNZP2.
DR SMR; P25466; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR PRIDE; P25466; -.
DR Proteomes; UP000000472; 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 2: Evidence at transcript level;
KW Glycoprotein; Hemagglutinin; Host cell membrane; Host membrane;
KW Host-virus interaction; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..571
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142623"
FT TOPO_DOM 1..25
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..571
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION 228..233
FT /note="Important for neuraminidase activity"
FT /evidence="ECO:0000250"
FT REGION 393..398
FT /note="Sialic receptor-binding site"
FT /evidence="ECO:0000305"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 571 AA; 63263 MW; D7130A3BE6491406 CRC64;
MEDYSNLSLK SIPKRTCRII FRTATILGIC TLIVLCSSIL HEIIHLDVSS GLMDSDDSQQ
GIIQPIIESL KSLIALANQI LYNVAIIIPL KIDSIETVIF SALKDMHTGS MSNTNCTPGN
LLLHDAAYIN GINKFLVLKS YNGTPKYGPL LNIPSFIPSA TSPNGCTRIP SFSLIKTHWC
YTHNVMLGDC LDFTTSNQYL AMGIIQQSAA AFPIFRTMKT IYLSDGINRK SCSVTAIPGG
CVLYCYVATR SEKEDYATTD LAELRLAFYY YNDTFIERVI SLPNTTGQWA TINPAVGSGI
YHLGFILFPV YGGLISGTPS YNKQSSRYFI PKHPNITCAG NSSEQAAAAR SSYVIRYHSN
RLIQSAVLIC PLSDMHTARC NLVMFNNSQV MMGAEGRLYV IDNNLYYYQR SSSWWSASLF
YRINTDFSKG IPPIIEAQWV PSYQVPRPGV MPCNATSFCP ANCITGVYAD VWPLNDPEPT
SQNALNPNYR FAGAFLRNES NRTNPTFYTA SASALLNTTG FNNTNHKAAY TSSTCFKNTG
TQKIYCLIII EMGSSLLGEF QIIPFLRELI P
