ID A0A096XNG5_9BETC Unreviewed; 426 AA. AC A0A096XNG5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 18-SEP-2019, entry version 17. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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-UniRule. 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:0001681; F:sialate O-acetylesterase activity; IEA:UniProtKB-UniRule. 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; 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 //