HN_PIV5
ID HN_PIV5 Reviewed; 565 AA.
AC P04850;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3973974; DOI=10.1128/jvi.54.1.1-6.1985;
RA Hiebert S.W., Paterson R.G., Lamb R.A.;
RT "Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5:
RT nucleotide sequence of the mRNA predicts an N-terminal membrane anchor.";
RL J. Virol. 54:1-6(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 37-565.
RX PubMed=15893670; DOI=10.1016/j.str.2005.02.019;
RA Yuan P., Thompson T.B., Wurzburg B.A., Paterson R.G., Lamb R.A.,
RA Jardetzky T.S.;
RT "Structural studies of the parainfluenza virus 5 hemagglutinin-
RT neuraminidase tetramer in complex with its receptor, sialyllactose.";
RL Structure 13:803-815(2005).
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 -!- INTERACTION:
CC P04850; P04850: HN; NbExp=4; IntAct=EBI-15552318, EBI-15552318;
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; S76876; AAB21114.1; -; mRNA.
DR EMBL; K02870; AAA47878.1; -; Genomic_RNA.
DR EMBL; AF052755; AAC95517.1; -; Genomic_RNA.
DR PIR; A00879; HNNZSV.
DR PDB; 1Z4V; X-ray; 2.30 A; A=37-565.
DR PDB; 1Z4W; X-ray; 2.70 A; A=37-565.
DR PDB; 1Z4X; X-ray; 2.50 A; A=37-565.
DR PDB; 1Z4Y; X-ray; 2.60 A; A=37-565.
DR PDB; 1Z4Z; X-ray; 2.50 A; A=37-565.
DR PDB; 1Z50; X-ray; 2.80 A; A=37-565.
DR PDB; 3TSI; X-ray; 2.65 A; A/B/C/D=56-117.
DR PDB; 4JF7; X-ray; 2.50 A; A/B/C/D=56-565.
DR PDBsum; 1Z4V; -.
DR PDBsum; 1Z4W; -.
DR PDBsum; 1Z4X; -.
DR PDBsum; 1Z4Y; -.
DR PDBsum; 1Z4Z; -.
DR PDBsum; 1Z50; -.
DR PDBsum; 3TSI; -.
DR PDBsum; 4JF7; -.
DR SMR; P04850; -.
DR DIP; DIP-48442N; -.
DR CAZy; GH83; Glycoside Hydrolase Family 83.
DR PRIDE; P04850; -.
DR EvolutionaryTrace; P04850; -.
DR Proteomes; UP000007232; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
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; Disulfide bond; Glycoprotein; Hemagglutinin;
KW Host cell membrane; Host membrane; Host-virus interaction; Hydrolase;
KW Membrane; Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..565
FT /note="Hemagglutinin-neuraminidase"
FT /id="PRO_0000142641"
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 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT DISULFID 161..185
FT DISULFID 175..236
FT DISULFID 227..240
FT DISULFID 365..375
FT DISULFID 448..458
FT DISULFID 528..539
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:4JF7"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:4JF7"
FT HELIX 82..99
FT /evidence="ECO:0007829|PDB:4JF7"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4JF7"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4JF7"
FT TURN 121..125
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 206..218
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 351..355
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 356..367
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 414..434
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:1Z4V"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 498..506
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 520..531
FT /evidence="ECO:0007829|PDB:1Z4V"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 536..546
FT /evidence="ECO:0007829|PDB:1Z4V"
FT STRAND 548..564
FT /evidence="ECO:0007829|PDB:1Z4V"
SQ SEQUENCE 565 AA; 62205 MW; 30A4A7068A25B563 CRC64;
MVAEDAPVRA TCRVLFRTTT LIFLCTLLAL SISILYESLI TQKQIMSQAG STGSNSGLGS
ITDLLNNILS VANQIIYNSA VALPLQLDTL ESTLLTAIKS LQTSDKLEQN CSWSAALIND
NRYINGINQF YFSIAEGRNL TLGPLLNMPS FIPTATTPEG CTRIPSFSLT KTHWCYTHNV
ILNGCQDHVS SNQFVSMGII EPTSAGFPFF RTLKTLYLSD GVNRKSCSIS TVPGGCMMYC
FVSTQPERDD YFSAAPPEQR IIIMYYNDTI VERIINPPGV LDVWATLNPG TGSGVYYLGW
VLFPIYGGVI KGTSLWNNQA NKYFIPQMVA ALCSQNQATQ VQNAKSSYYS SWFGNRMIQS
GILACPLRQD LTNECLVLPF SNDQVLMGAE GRLYMYGDSV YYYQRSNSWW PMTMLYKVTI
TFTNGQPSAI SAQNVPTQQV PRPGTGDCSA TNRCPGFCLT GVYADAWLLT NPSSTSTFGS
EATFTGSYLN TATQRINPTM YIANNTQIIS SQQFGSSGQE AAYGHTTCFR DTGSVMVYCI
YIIELSSSLL GQFQIVPFIR QVTLS
