ID A0A096XNG5_9BETC Unreviewed; 426 AA. AC A0A096XNG5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-FEB-2025, entry version 37. 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=N-acetyl-4-O-acetylneuraminate + H2O = N-acetylneuraminate + CC acetate + H(+); 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:ARBA00049566, ECO:0000256|HAMAP- CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-9-O-acetylneuraminate + H2O = N-acetylneuraminate + CC acetate + H(+); 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:ARBA00047704, 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: Host cell membrane CC {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-Rule:MF_04207, CC ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-Rule:MF_04207, CC ECO:0000256|RuleBase:RU361278}. 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}. 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}. 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:0016020; C: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: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|ARBA:ARBA00022546, ECO:0000256|HAMAP- KW Rule:MF_04207}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04207}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04207}; 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|ARBA:ARBA00022879, ECO:0000256|HAMAP- KW Rule:MF_04207}; 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 //