HEMA_PTV10
ID HEMA_PTV10 Reviewed; 430 AA.
AC Q70KP1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 10-FEB-2021, entry version 75.
DE RecName: Full=Hemagglutinin-esterase;
DE Short=HE protein;
DE EC=3.1.1.53;
DE AltName: Full=E3 glycoprotein;
DE Flags: Precursor;
GN Name=HE;
OS Porcine torovirus (strain P10) (PoTV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC Renitovirus.
OX NCBI_TaxID=360395;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12915570; DOI=10.1128/jvi.77.17.9567-9577.2003;
RA Smits S.L., Lavazza A., Matiz K., Horzinek M.C., Koopmans M.P.,
RA de Groot R.J.;
RT "Phylogenetic and evolutionary relationships among torovirus field
RT variants: evidence for multiple intertypic recombination events.";
RL J. Virol. 77:9567-9577(2003).
RN [2]
RP CHARACTERIZATION.
RX PubMed=15507445; DOI=10.1074/jbc.m409683200;
RA Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P.,
RA Kamerling J.P., Vlasak R., de Groot R.J.;
RT "Nidovirus sialate-O-acetylesterases: evolution and substrate specificity
RT of coronaviral and toroviral receptor-destroying enzymes.";
RL J. Biol. Chem. 280:6933-6941(2005).
CC -!- FUNCTION: Structural protein that makes short spikes at the surface of
CC the virus. Contains receptor binding and receptor-destroying
CC activities. Mediates de-O-acetylation of N-acetyl-9-O-acetylneuraminic
CC acid, which is probably the receptor determinant recognized by the
CC virus on the surface of erythrocytes and susceptible cells. This
CC receptor-destroying activity is important for virus release as it
CC probably helps preventing self-aggregation and ensures the efficient
CC spread of the progeny virus from cell to cell. May serve as a secondary
CC viral attachment protein for initiating infection, the spike protein
CC being the major one. Seems to be a 'luxury' protein that is not
CC absolutely necessary for virus infection in culture. However, its
CC presence in the virus may alter its pathogenicity. May become a target
CC for both the humoral and the cellular branches of the immune system.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=In infected
CC cells becomes incorporated into the envelope of virions during virus
CC assembly at the endoplasmic reticulum and cis Golgi. However, some may
CC escape incorporation into virions and subsequently migrate to the cell
CC surface (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ575366; CAE01332.1; -; Genomic_RNA.
DR SMR; Q70KP1; -.
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:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:CACAO.
DR GO; GO:0106331; F:sialate 4-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR007142; Hemagglutn-estrase_core.
DR InterPro; IPR003860; Hemagglutn-estrase_hemagglutn.
DR Pfam; PF03996; Hema_esterase; 1.
DR Pfam; PF02710; Hema_HEFG; 1.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Hydrolase; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..430
FT /note="Hemagglutinin-esterase"
FT /id="PRO_0000045401"
FT TOPO_DOM 28..404
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..430
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 16..133
FT /note="Esterase domain first part"
FT /evidence="ECO:0000250"
FT REGION 134..274
FT /note="Receptor binding"
FT /evidence="ECO:0000250"
FT REGION 275..390
FT /note="Esterase domain second part"
FT /evidence="ECO:0000250"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 53..69
FT /evidence="ECO:0000250"
FT DISULFID 120..168
FT /evidence="ECO:0000250"
FT DISULFID 207..284
FT /evidence="ECO:0000250"
FT DISULFID 215..257
FT /evidence="ECO:0000250"
FT DISULFID 315..320
FT /evidence="ECO:0000250"
FT DISULFID 357..382
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 48225 MW; 97A614A76EC44756 CRC64;
MLRMRVRPPS AIPVFLIFVL LPFVLTSKPI TPHYGPGHIT SDWCGFGDSR SDCGNQHTPK
SLDIPQELCP KFSSRTGSSM FISMHWNNDS DFNAFGYSNC GVEKVFYEGV NFSPYRNYTC
YQEGSFGWVS NKVGFYSKLY SMASTSRCIK LINLDPPTNF TNYRNGTCTG NGGTAKMPDN
PQLVIFNSVV KVSTQFVLPS SSDGFSCTKH LVPFCYIDGG CFEMSGVCYP FGYYYQSPSF
YHAFYTNGTA GLHRYICDYL EMKPGVYNAT TFGKFLIYPT KSYCMDTMNY TVPVQAVQSI
WSENRQSDDA IGQACKSPYC IFYNKTKPYL APNGADENHG DEEVRQMMQG LLVNSSCVSP
QGSTPLALYS SEMIYTPNYG SCPQYYKLFE TSSDENVDVT SSAYFVATWV LLVLVIILIF
ILISFCLSSY
