ID   A0A096XNG5_9BETC        Unreviewed;       426 AA.
AC   A0A096XNG5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   31-JUL-2019, entry version 16.
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};
OS   Longquan Rl rat coronavirus.
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; Betacoronavirus; unclassified Betacoronavirus.
OX   NCBI_TaxID=1508223 {ECO:0000313|EMBL:AID16648.1};
RN   [1] {ECO:0000313|EMBL:AID16648.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Longquan-189 {ECO:0000313|EMBL:AID16648.1};
RX   PubMed=25463600; DOI=10.1016/j.virol.2014.10.017;
RA   Wang W., Lin X.D., Guo W.P., Zhou R.H., Wang M.R., Wang C.Q., Ge S.,
RA   Mei S.H., Li M.H., Shi M., Holmes E.C., Zhang Y.Z.;
RT   "Discovery, diversity and evolution of novel coronaviruses sampled
RT   from rodents in China.";
RL   Virology 474:19-27(2015).
CC   -!- FUNCTION: Structural protein that makes short spikes at the
CC       surface of the virus. Contains receptor binding and receptor-
CC       destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-
CC       acetylneuraminic acid, which is probably the receptor determinant
CC       recognized by the virus on the surface of erythrocytes and
CC       susceptible cells. This receptor-destroying activity is important
CC       for virus release as it probably helps preventing self-aggregation
CC       and ensures the efficient spread of the progeny virus from cell to
CC       cell. May serve as a secondary viral attachment protein for
CC       initiating infection, the spike protein being the major one. May
CC       become a target for both the humoral and the cellular branches of
CC       the immune system. {ECO:0000256|HAMAP-Rule:MF_04207,
CC       ECO:0000256|RuleBase:RU361278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) +
CC         N-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) +
CC         N-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; Evidence={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
CC       a ternary complex S-M-HE. {ECO:0000256|HAMAP-Rule:MF_04207}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
CC       Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; Single-pass type I
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_04207,
CC       ECO:0000256|RuleBase:RU361278}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
CC       Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_04207, ECO:0000256|RuleBase:RU361278}. Note=In infected
CC       cells becomes incorporated into the envelope of virions during
CC       virus assembly at the endoplasmic reticulum and cis Golgi.
CC       However, some may escape incorporation into virions and
CC       subsequently migrate to the cell surface. {ECO:0000256|HAMAP-
CC       Rule:MF_04207, ECO:0000256|RuleBase:RU361278}.
CC   -!- PTM: N-glycosylated in the host RER. {ECO:0000256|HAMAP-
CC       Rule:MF_04207}.
CC   -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC       hemagglutinin-esterase family. {ECO:0000256|HAMAP-Rule:MF_04207,
CC       ECO:0000256|RuleBase:RU361278}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04207}.
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DR   EMBL; KF294370; AID16648.1; -; Genomic_RNA.
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:0001681; F:sialate O-acetylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
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; SSF49818; SSF49818; 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|HAMAP-Rule:MF_04207,
KW   ECO:0000256|RuleBase:RU361278};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW   ECO:0000256|RuleBase:RU361278};
KW   Signal {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|HAMAP-Rule:MF_04207,
KW   ECO:0000256|RuleBase:RU361278}.
FT   TRANSMEM    394    417       Helical. {ECO:0000256|RuleBase:RU361278}.
FT   TOPO_DOM    416    426       Intravirion. {ECO:0000256|HAMAP-Rule:
FT                                MF_04207}.
FT   DOMAIN       17    380       Hema_esterase. {ECO:0000259|Pfam:
FT                                PF03996}.
FT   DOMAIN      132    267       Hema_HEFG. {ECO:0000259|Pfam:PF02710}.
FT   ACT_SITE     47     47       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_04207}.
FT   ACT_SITE    329    329       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_04207}.
FT   ACT_SITE    332    332       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_04207}.
FT   DISULFID    116    165       {ECO:0000256|HAMAP-Rule:MF_04207}.
FT   DISULFID    310    315       {ECO:0000256|HAMAP-Rule:MF_04207}.
FT   DISULFID    350    374       {ECO:0000256|HAMAP-Rule:MF_04207}.
SQ   SEQUENCE   426 AA;  47667 MW;  A36DEC6318C2E119 CRC64;
     MCKNLITLYY LDNMWKLLLL CSVCYGFNDP LNVVSHFNDD WFLFGDSRSD CNHLPNNRSY
     MDLDPSLCDS GKISSKAGNS IFRSFHFTDF YNYTGEGNQI IFYEGVNFTP HHAFKCTASG
     SNVVWIQNKG SFYHKLYNSM SHYRTLTIVN VPYSYGGQAK PTTMCKSGSL TLNNPAFIAK
     EVGVNDYYYK SEANFTLTGC DEYIVPLCIF NGKFLSTGNY YDDSQYYYNM DTGVIYGFNS
     TSSASVGLDL ECKYLNLKSG SYKAISNELL LTIPIKAICL NKAKAFVPVQ VVDSRWNSGR
     VSDNKTAEAC KLPFCYFRNS TGNYLGRYDI NHGDAGFTSI LSGLLYNVPC IAFQGAFYYD
     NVTTVWPSSG SGHCPTASNI IVNIPVCAYD PLPIILLGIL LGIAVLIIVF LMFYFLVDNG
     VRLHEA
//