ID G0ZTD0_9BETC Unreviewed; 122 AA.
AC G0ZTD0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Hemagglutinin-esterase {ECO:0000256|RuleBase:RU361278};
DE Short=HE protein {ECO:0000256|RuleBase:RU361278};
DE EC=3.1.1.53 {ECO:0000256|RuleBase:RU361278};
DE AltName: Full=E3 glycoprotein {ECO:0000256|RuleBase:RU361278};
DE Flags: Fragment;
GN Name=HE {ECO:0000256|RuleBase:RU361278};
OS Betacoronavirus 1.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=694003 {ECO:0000313|EMBL:AEL88650.1};
RN [1] {ECO:0000313|EMBL:AEL88650.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Equine/Brazil/2009/E19 {ECO:0000313|EMBL:AEL88650.1};
RX PubMed=24348152; DOI=10.1155/2013/349702;
RA Barros I.N., Silva S.O.S., Nogueira Neto F.S., Asano K.M., Souza S.P.,
RA Richtzenhain L.J., Brandao P.E.;
RT "A multigene approach for comparing genealogy of betacoronavirus from
RT cattle and horses.";
RL ScientificWorldJournal 2013:349702-349702(2013).
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-4-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. May become a target for both the humoral and the
CC cellular branches of the immune system.
CC {ECO:0000256|RuleBase:RU361278}.
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 Evidence={ECO:0000256|ARBA:ARBA00000954,
CC ECO:0000256|RuleBase:RU361278};
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 Evidence={ECO:0000256|ARBA:ARBA00001221};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Host cell membrane {ECO:0000256|ARBA:ARBA00004402,
CC ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|RuleBase:RU361278}. Virion
CC membrane {ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU361278}. Note=In infected cells becomes
CC incorporated into the envelope of virions during virus assembly at the
CC endoplasmic reticulum and cis Golgi. However, some may escape
CC incorporation into virions and subsequently migrate to the cell
CC surface. {ECO:0000256|RuleBase:RU361278}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000256|ARBA:ARBA00010920,
CC ECO:0000256|RuleBase:RU361278}.
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DR EMBL; JF345128; AEL88650.1; -; Genomic_RNA.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0106331; F:sialate 4-O-acetylesterase activity; IEA:RHEA.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:RHEA.
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; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF49818; Viral protein domain; 1.
PE 3: Inferred from homology;
KW Hemagglutinin {ECO:0000256|RuleBase:RU361278};
KW Host cell membrane {ECO:0000256|RuleBase:RU361278};
KW Host membrane {ECO:0000256|RuleBase:RU361278};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361278};
KW Membrane {ECO:0000256|RuleBase:RU361278};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Viral envelope protein {ECO:0000256|RuleBase:RU361278};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU361278}.
FT DOMAIN 3..74
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 75..121
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEL88650.1"
FT NON_TER 122
FT /evidence="ECO:0000313|EMBL:AEL88650.1"
SQ SEQUENCE 122 AA; 13771 MW; 7C651C0C8B32D28F CRC64;
YSYMDLNPAL CDSGKISSKA GNSIFRSFHF TDFYNYTGEG QQIIFYEGVN FTPYYAFKCT
TSGSNDIWMH NKGLFYTQVY KNMAVYRSLT FVNVPYVYNG SAQSTALCKS GSLVLNNPAY
IA
//
