HN_PIV5C
ID HN_PIV5C Reviewed; 565 AA.
AC P28883;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 07-APR-2021, entry version 107.
DE RecName: Full=Hemagglutinin-neuraminidase;
DE EC=3.2.1.18;
GN Name=HN;
OS Parainfluenza virus 5 (isolate Canine/CPI-) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=31609;
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; JQ1305; HNNZC1.
DR SMR; P28883; -.
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 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_0000142642"
FT TOPO_DOM 1..20
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..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; 62279 MW; 4DA94276001FBD3C CRC64;
MVAEDAPVRG TCRVLFRTTT LIFLCTLLAL SISILYESLI IQKQIMSQAG STGSNFRLGS
ITDLLNNILS VANQIIYNSA VALPLQLDTL ESTLLTAIKS LQTSDKLEQN CSWGAALIND
NRYINGINQF YFSIAEGRNL TLGPLLNIPS FIPTATTPEG CTRIPSFSLT KTHWCYTHNV
ILNGCQDHVS SNQFVSMGII EPTSAGFPSF RTLKTLYLSD GVNRKSCSIS TVPGGCMMYC
FVSTQPERDD YLSTAPPEQR IIIMYYNDTI VERIINPPGV LDVWATLNPG TGSGVYYLGW
VLFPTYGGVI KDTSLWNNQA NKYFIPQMVA ALCSQNQATQ VQNAKSSYYS SWFGNRMIQS
GILACPLQQD LTNECLILPF SNDQVLMGAE GRLYMYGDSV YYYQRSNSWW PMTMLYKVTI
TFTNGQPSAI SAQNVPTQQV PRPGTGDCSA TNRCPGFCLK GVYADAWLLT NPSSTSTFGS
EATFTGSYLN AATQRINPTM YIANNTQIIS SQQFGSSGQE AAYGHTTCFR DTGSVMVYCI
YIIELSSSLL GQFQIVPFIR QVTLS
