ID   A0A096XNG5_9BETC        Unreviewed;       426 AA.
AC   A0A096XNG5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
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 from
RT   rodents in China.";
RL   Virology 474:19-27(2015).
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; KF294370; AID16648.1; -; 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-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: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: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|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_04207};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_04207};
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           25..426
FT                   /note="Hemagglutinin-esterase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT                   /id="PRO_5023342294"
FT   TRANSMEM        394..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361278"
FT   TOPO_DOM        416..426
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   DOMAIN          17..380
FT                   /note="Haemagglutinin-esterase glycoprotein core"
FT                   /evidence="ECO:0000259|Pfam:PF03996"
FT   DOMAIN          132..267
FT                   /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT                   /evidence="ECO:0000259|Pfam:PF02710"
FT   ACT_SITE        47
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   ACT_SITE        329
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   ACT_SITE        332
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   DISULFID        116..165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   DISULFID        310..315
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT   DISULFID        350..374
FT                   /evidence="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
//