HN_PI3H4
ID HN_PI3H4 Reviewed; 572 AA.
AC P08492;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 02-JUN-2021, entry version 121.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human
OS parainfluenza 3 virus (strain NIH 47885)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11217;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3003381; DOI=10.1128/jvi.57.2.481-489.1986;
RA Elango N., Coligan J.E., Jambou R.C., Venkatesan S.;
RT "Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein:
RT nucleotide sequence of mRNA and limited amino acid sequence of the purified
RT protein.";
RL J. Virol. 57:481-489(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2825443; DOI=10.1016/0168-1702(87)90016-5;
RA Galinski M.S., Mink M.A., Pons M.W.;
RT "Molecular cloning and sequence analysis of the human parainfluenza 3 virus
RT genes encoding the surface glycoproteins, F and HN.";
RL Virus Res. 8:205-215(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2822598; DOI=10.1159/000149722;
RA Storey D.G., Cote M.-J., Dimock K., Kang C.Y.;
RT "Nucleotide sequence of the coding and flanking regions of the human
RT parainfluenza virus 3 hemagglutinin-neuraminidase gene: comparison with
RT other paramyxoviruses.";
RL Intervirology 27:69-80(1987).
RN [4]
RP VARIANT NEURAMINIDASE-DEFICIENT ASN-216.
RC STRAIN=Isolate C28;
RX PubMed=8525632; DOI=10.1006/viro.1995.9925;
RA Huberman K., Peluso R.W., Moscona A.;
RT "Hemagglutinin-neuraminidase of human parainfluenza 3: role of the
RT neuraminidase in the viral life cycle.";
RL Virology 214:294-300(1995).
RN [5]
RP VARIANT 4-GU-DANA-RESISTANT ILE-193.
RC STRAIN=Isolate ZM1;
RX PubMed=12477836; DOI=10.1128/jvi.77.1.309-317.2003;
RA Murrell M., Porotto M., Weber T., Greengard O., Moscona A.;
RT "Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase
RT causing increased receptor binding activity and resistance to the
RT transition state sialic acid analog 4-GU-DANA (Zanamivir).";
RL J. Virol. 77:309-317(2003).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.7.;
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; M17641; AAA46846.1; -; mRNA.
DR EMBL; M21649; AAA46853.1; -; Genomic_RNA.
DR EMBL; M20402; AAA46856.1; -; mRNA.
DR PIR; A27765; HNNZP3.
DR PDB; 4MZA; X-ray; 1.65 A; A/B=136-572.
DR PDB; 4MZE; X-ray; 1.80 A; A/B=136-572.
DR PDB; 4XJR; X-ray; 3.00 A; A/B=125-572.
DR PDBsum; 4MZA; -.
DR PDBsum; 4MZE; -.
DR PDBsum; 4XJR; -.
DR SMR; P08492; -.
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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Host-virus interaction; Hydrolase; Membrane; Signal-anchor;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT CHAIN 1..572
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142625"
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"
FT VARIANT 193
FT /note="T -> I (in strain: Isolate ZM1; 4-GU-DANA antiviral
FT drug resistant and increased receptor binding avidity)"
FT /evidence="ECO:0000269|PubMed:12477836"
FT VARIANT 216
FT /note="D -> N (in strain: Isolate C28; 50% loss of
FT neuraminidase activity)"
FT /evidence="ECO:0000269|PubMed:8525632"
FT VARIANT 567
FT /note="I -> V (in strain: Isolate ZM1)"
FT CONFLICT 135
FT /note="Q -> R (in Ref. 2; AAA46853)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="V -> A (in Ref. 2; AAA46853)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="S -> G (in Ref. 3; AAA46856)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="S -> A (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4MZE"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 203..215
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 235..247
FT /evidence="ECO:0007829|PDB:4MZA"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 331..342
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:4MZA"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:4MZA"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4XJR"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 488..496
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 505..513
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 515..522
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 526..538
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 541..552
FT /evidence="ECO:0007829|PDB:4MZA"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 557..566
FT /evidence="ECO:0007829|PDB:4MZA"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:4MZA"
SQ SEQUENCE 572 AA; 64247 MW; BDCA6F9A41E20369 CRC64;
MEYWKHTNHG KDAGNELETS MATHGNKITN KITYILWTII LVLLSIVFII VLINSIKSEK
AHESLLQDVN NEFMEVTEKI QMASDNINDL IQSGVNTRLL TIQSHVQNYI PISLTQQMSD
LRKFISEITI RNDNQEVPPQ RITHDVGIKP LNPDDFWRCT SGLPSLMKTP KIRLMPGPGL
LAMPTTVDGC VRTPSLVIND LIYAYTSNLI TRGCQDIGKS YQVLQIGIIT VNSDLVPDLN
PRISHTFNIN DNRKSCSLAL LNTDVYQLCS TPKVDERSDY ASSGIEDIVL DIVNHDGSIS
TTRFKNNNIS FDQPYAALYP SVGPGIYYKG KIIFLGYGGL EHPINENAIC NTTGCPGKTQ
RDCNQASHSP WFSDRRMVNS IIVVDKGLNS IPKLKVWTIS MRQNYWGSEG RLLLLGNKIY
IYTRSTSWHS KLQLGIIDIT DYSDIRIKWT WHNVLSRPGN NECPWGHSCP DGCITGVYTD
AYPLNPTGSI VSSVILDSQK SRVNPVITYS TSTERVNELA IRNKTLSAGY TTTSCITHYN
KGYCFHIVEI NHKSLDTFQP MLFKTEIPKS CS
