ID   A0A096XNG5_9BETC        Unreviewed;       426 AA.
AC   A0A096XNG5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   10-APR-2019, entry version 14.
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};
GN   Name=HE {ECO:0000256|RuleBase:RU361278};
OS   Longquan Rl rat coronavirus.
OC   Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   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|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;
CC         Evidence={ECO:0000256|RuleBase:RU361278};
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU361278}. Host cell membrane
CC       {ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU361278}. Note=In infected cells
CC       becomes incorporated into the envelope of virions during virus
CC       assembly at the endoplasmic reticulum and cis Golgi. However, some
CC       may escape incorporation into virions and subsequently migrate to
CC       the cell surface. {ECO:0000256|RuleBase:RU361278}.
CC   -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC       hemagglutinin-esterase family. {ECO:0000256|RuleBase:RU361278}.
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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   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   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|RuleBase:RU361278};
KW   Membrane {ECO:0000256|RuleBase:RU361278};
KW   Transmembrane {ECO:0000256|RuleBase:RU361278};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361278};
KW   Viral envelope protein {ECO:0000256|RuleBase:RU361278};
KW   Virion {ECO:0000256|RuleBase:RU361278}.
FT   TRANSMEM    394    417       Helical. {ECO:0000256|RuleBase:RU361278}.
FT   DOMAIN       17    380       Hema_esterase. {ECO:0000259|Pfam:
FT                                PF03996}.
FT   DOMAIN      132    267       Hema_HEFG. {ECO:0000259|Pfam:PF02710}.
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
//