ID A8R4C8_9BETC Unreviewed; 423 AA.
AC A8R4C8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Hemagglutinin-esterase {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE Short=HE protein {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE EC=3.1.1.53 {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE AltName: Full=E3 glycoprotein {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
GN Name=HE {ECO:0000256|HAMAP-Rule:MF_04207,
GN ECO:0000256|RuleBase:RU361278, ECO:0000313|EMBL:ABP87989.1};
OS Equine coronavirus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Betacoronavirus 1.
OX NCBI_TaxID=136187 {ECO:0000313|EMBL:ABP87989.1, ECO:0000313|Proteomes:UP000103372};
RN [1] {ECO:0000313|EMBL:ABP87989.1, ECO:0000313|Proteomes:UP000103372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC99 {ECO:0000313|EMBL:ABP87989.1};
RX PubMed=17706262; DOI=10.1016/j.virol.2007.06.035;
RA Zhang J., Guy J.S., Snijder E.J., Denniston D.A., Timoney P.J.,
RA Balasuriya U.B.;
RT "Genomic characterization of equine coronavirus.";
RL Virology 369:92-104(2007).
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. {ECO:0000256|HAMAP-
CC Rule:MF_04207, 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, ECO:0000256|HAMAP-
CC Rule:MF_04207, 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, ECO:0000256|HAMAP-
CC Rule:MF_04207};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a complex with the M
CC protein in the pre-Golgi. Associates then with S-M complex to form a
CC ternary complex S-M-HE. {ECO:0000256|HAMAP-Rule:MF_04207}.
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, ECO:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}. Virion membrane
CC {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
CC Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04207,
CC 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|HAMAP-Rule:MF_04207,
CC ECO:0000256|RuleBase:RU361278}.
CC -!- PTM: N-glycosylated in the host RER. {ECO:0000256|HAMAP-Rule:MF_04207}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000256|ARBA:ARBA00010920,
CC ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04207}.
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DR EMBL; EF446615; ABP87989.1; -; Genomic_RNA.
DR SMR; A8R4C8; -.
DR Proteomes; UP000103372; Genome.
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-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR HAMAP; MF_04207; BETA_CORONA_HE; 1.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR042545; HEMA.
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 Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04207};
KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04207};
KW Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04207};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04207};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04207}.
FT CHAIN 16..423
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT /id="PRO_5023393264"
FT TRANSMEM 391..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361278"
FT TOPO_DOM 413..423
FT /note="Intravirion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DOMAIN 15..376
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 127..263
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 43..64
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 112..161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 306..311
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 346..370
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
SQ SEQUENCE 423 AA; 47812 MW; E0A5FAF40FD9AC85 CRC64;
MYLLPKFLAI LVAGSFGFEN PPVNIVSHIN EDWFLFGDSR SDCNHINTIN PRNYSYMDLN
PELCNSGKIS SKAGNSLFRS FHFTDFYNYT GEGQQIIFYE GVDFTPNHGF KCTASGDNAV
WMQNKARFYE IVYRSMAVYR SLTFKTVAYN YSGTAVATNL CKQSSLTMNN PTFIAKESGF
TDYYYTSIAN FSLQGCDEYI IPLCYFNGKF LSSSKYYDDS VYYFNIDTGE VFGFNSTRPT
ADGIDFNCFY YRVPSGLYQA ISYELMLTVP SKIICLSKPK DFTPVQVVDS RWNSARRSDN
MTAIACQLPY CYFRNSTSDY KGVYDINHGD AGFTSILSGL LYNSPCFSWQ GVYRFDNVST
VWPLYPFGKC PTAANLANVD GPICVYDPLP IILLGVLLGL AVIIIIALLF YFMVDNGTRL
HEA
//
