ID HEMA_BRV2 Reviewed; 416 AA. AC P0C0W0; O39517; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Hemagglutinin-esterase; DE Short=HE protein; DE EC=3.1.1.53; DE AltName: Full=E3 glycoprotein; DE Flags: Precursor; GN Name=HE; OS Breda virus 2 (BRV-2). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus; OC Renitovirus; Bovine torovirus. OX NCBI_TaxID=360394; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], CHARACTERIZATION, AND SUBCELLULAR RP LOCATION. RX PubMed=9188596; DOI=10.1128/jvi.71.7.5277-5286.1997; RA Cornelissen L.A.H.M., Wierda C.M.H., van der Meer F.J., Herrewegh A.A.P.M., RA Horzinek M.C., Egberink H.F., de Groot R.J.; RT "Hemagglutinin-esterase, a novel structural protein of torovirus."; RL Virology 71:5277-5286(1997). RN [2] RP CHARACTERIZATION. RX PubMed=15507445; DOI=10.1074/jbc.m409683200; RA Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P., RA Kamerling J.P., Vlasak R., de Groot R.J.; RT "Nidovirus sialate-O-acetylesterases: evolution and substrate specificity RT of coronaviral and toroviral receptor-destroying enzymes."; RL J. Biol. Chem. 280:6933-6941(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-9-di-O- CC acetylneuraminic acid, which is probably the receptor determinant CC recognized by the virus on the surface of erythrocytes and susceptible CC cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N- CC acetyl-9-O-acetylneuraminic acid, but displays a substrate preference CC for N-acetyl-9-di-O-acetylneuraminic acid. This receptor-destroying CC activity is important for virus release as it probably helps preventing CC self-aggregation and ensures the efficient spread of the progeny virus CC from cell to cell. May serve as a secondary viral attachment protein CC for initiating infection, the spike protein being the major one. Seems CC to be a 'luxury' protein that is not absolutely necessary for virus CC infection in culture. However, its presence in the virus may alter its CC pathogenicity. May become a target for both the humoral and the CC cellular branches of the immune system. 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 -!- 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 -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; CC Single-pass type I membrane protein {ECO:0000305}. Note=In infected CC cells becomes incorporated into the envelope of virions during virus CC assembly at the endoplasmic reticulum and cis Golgi. However, some may CC escape incorporation into virions and subsequently migrate to the cell CC surface (By similarity). {ECO:0000250}. CC -!- PTM: N-glycosylated. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses CC hemagglutinin-esterase family. {ECO:0000305}. 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; Y10866; CAA71819.1; -; Genomic_RNA. DR SMR; P0C0W0; -. DR GlyCosmos; P0C0W0; 6 sites, No reported glycans. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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: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: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; SSF52266; SGNH hydrolase; 1. DR SUPFAM; SSF49818; Viral protein domain; 1. PE 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane; KW Host membrane; Hydrolase; Membrane; Signal; Transmembrane; KW Transmembrane helix; Viral envelope protein; Virion. FT SIGNAL 1..14 FT /evidence="ECO:0000255" FT CHAIN 15..416 FT /note="Hemagglutinin-esterase" FT /id="PRO_0000045399" FT TOPO_DOM 15..393 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 394..414 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 415..416 FT /note="Intravirion" FT /evidence="ECO:0000255" FT REGION 4..121 FT /note="Esterase domain first part" FT /evidence="ECO:0000250" FT REGION 122..263 FT /note="Receptor binding" FT /evidence="ECO:0000250" FT REGION 264..379 FT /note="Esterase domain second part" FT /evidence="ECO:0000250" FT ACT_SITE 37 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 325 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 328 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 257 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 313 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 322 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 343 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 41..57 FT /evidence="ECO:0000250" FT DISULFID 108..156 FT /evidence="ECO:0000250" FT DISULFID 192..273 FT /evidence="ECO:0000250" FT DISULFID 200..246 FT /evidence="ECO:0000250" FT DISULFID 304..309 FT /evidence="ECO:0000250" FT DISULFID 346..371 FT /evidence="ECO:0000250" SQ SEQUENCE 416 AA; 46440 MW; 384C406385439054 CRC64; MLSLILFFPS FAFAATPVTP YYGPGHITFD WCGFGDSRSD CTNPQSPMSL DIPQQLCPKF SSKSSSSMFL SLHWNNHSSF VSYDYFNCGV EKVFYEGVNF SPRKQYSCWD EGVDGWIELK TRFYTKLYQM ATTSRCIKLI QLQAPSSLPT LQAGVCRTNK QLPDNPRLAL LSDTVPTSVQ FVLPGSSGTT ICTKHLVPFC YLNHGCFTTG GSCLPFGVSY VSDSFYYGYY DATPQIGSTE SHDYVCDYLF MEPGTYNAST VGKFLVYPTK SYCMDTMNIT VPVQAVQSIW SEQYASDDAI GQACKAPYCI FYNKTTPYTV TNGSDANHGD DEVRMMMQGL LRNSSCISPQ GSTPLALYST EMIYEPNYGS CPQFYKLFDT SGNENIDVIS SSYFVATWVL LVVVVILIFV IISFFC //