ID HEMA_CVHN1 Reviewed; 386 AA. AC Q5MQD1; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Hemagglutinin-esterase {ECO:0000255|HAMAP-Rule:MF_04207}; DE Short=HE protein {ECO:0000255|HAMAP-Rule:MF_04207}; DE EC=3.1.1.53 {ECO:0000255|HAMAP-Rule:MF_04207}; DE AltName: Full=E3 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04207}; DE Flags: Precursor; GN Name=HE {ECO:0000255|HAMAP-Rule:MF_04207}; ORFNames=2; OS Human coronavirus HKU1 (isolate N1) (HCoV-HKU1). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Embecovirus; Human coronavirus HKU1. OX NCBI_TaxID=443239; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=15613317; DOI=10.1128/jvi.79.2.884-895.2005; RA Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y., RA Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M., Wong S.S.Y., RA Guan Y., Peiris J.S.M., Yuen K.-Y.; RT "Characterization and complete genome sequence of a novel coronavirus, RT coronavirus HKU1, from patients with pneumonia."; RL J. Virol. 79:884-895(2005). 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:0000255|HAMAP- CC Rule:MF_04207}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04207}; 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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_04207}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP- CC Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP- CC Rule:MF_04207}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04207}; CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. CC Note=In infected cells becomes incorporated into the envelope of CC virions during virus assembly at the endoplasmic reticulum and cis CC Golgi. However, some may escape incorporation into virions and CC subsequently migrate to the cell surface. {ECO:0000255|HAMAP- CC Rule:MF_04207}. CC -!- PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-Rule:MF_04207}. CC -!- MISCELLANEOUS: Isolate N1 belongs to genotype A. CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses CC hemagglutinin-esterase family. {ECO:0000255|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; AY597011; AAT98579.1; -; Genomic_RNA. DR RefSeq; YP_173237.1; NC_006577.2. DR PDB; 6Y3Y; EM; 3.39 A; A/B=14-355. DR PDBsum; 6Y3Y; -. DR EMDB; EMD-10676; -. DR SMR; Q5MQD1; -. DR GlyCosmos; Q5MQD1; 6 sites, No reported glycans. DR DNASU; 3200425; -. DR GeneID; 3200425; -. DR KEGG; vg:3200425; -. DR Proteomes; UP000008170; Segment. 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:0001681; F:sialate O-acetylesterase activity; ISS:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hemagglutinin; KW Host cell membrane; Host membrane; Hydrolase; Membrane; Signal; KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion. FT SIGNAL 1..11 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CHAIN 12..386 FT /note="Hemagglutinin-esterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT /id="PRO_0000297761" FT TOPO_DOM 12..359 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TRANSMEM 360..380 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TOPO_DOM 381..386 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 1..121 FT /note="Esterase domain 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 122..236 FT /note="Receptor binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 237..349 FT /note="Esterase domain 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 34 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 296 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 299 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 145 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 286 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 328 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 38..59 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 107..154 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 180..246 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 188..219 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 277..282 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 317..341 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT STRAND 23..26 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 114..131 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 179..191 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 200..203 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 242..249 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 302..308 FT /evidence="ECO:0007829|PDB:6Y3Y" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:6Y3Y" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:6Y3Y" SQ SEQUENCE 386 AA; 44679 MW; 8A880856BCDE8818 CRC64; MLIIFLFFYF CYGFNEPLNV VSHLNHDWFL FGDSRSDCNH INNLKIKNFD YLDIHPSLCN NGKISSSAGD SIFKSFHFTR FYNYTGEGDQ IIFYEGVNFN PYHRFKCFPN GSNDVWLLNK VRFYRALYSN MAFFRYLTFV DIPYNVSLSK FNSCKSDILS LNNPIFINYS KEVYFTLLGC SLYLVPLCLF KSNFSQYYYN IDTGSVYGFS NVVYPDLDCI YISLKPGSYK VSTTAPFLSL PTKALCFDKS KQFVPVQVVD SRWNNERASD ISLSVACQLP YCYFRNSSAN YVGKYDINHG DSGFISILSG LLYNVSCISY YGVFLYDNFT SIWPYYSFGR CPTSSIIKHP ICVYDFLPII LQGILLCLAL LFVVFLLFLL YNDKSH //