ID HEMA_CVBEN Reviewed; 424 AA. AC P59711; Q98VL2; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 99. 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=2b; OS Bovine coronavirus (strain 98TXSF-110-ENT) (BCoV-ENT) (BCV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Embecovirus; Betacoronavirus 1. OX NCBI_TaxID=233262; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=11714968; DOI=10.1099/0022-1317-82-12-2927; RA Chouljenko V.N., Lin X.Q., Storz J., Kousoulas K.G., Gorbalenya A.E.; RT "Comparison of genomic and predicted amino acid sequences of respiratory RT and enteric bovine coronaviruses isolated from the same animal with fatal RT shipping pneumonia."; RL J. Gen. Virol. 82:2927-2933(2001). 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 RER. CC -!- PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-Rule:MF_04207}. 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; AF391541; AAK83355.1; -; Genomic_RNA. DR RefSeq; NP_150076.1; NC_003045.1. DR SMR; P59711; -. DR GlyCosmos; P59711; 8 sites, No reported glycans. DR GeneID; 921684; -. DR KEGG; vg:921684; -. DR Proteomes; UP000008570; 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 3: Inferred from homology; 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..16 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CHAIN 17..424 FT /note="Hemagglutinin-esterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT /id="PRO_0000037133" FT TOPO_DOM 17..392 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TRANSMEM 393..413 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TOPO_DOM 414..424 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 7..127 FT /note="Esterase domain 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 128..266 FT /note="Receptor binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 267..379 FT /note="Esterase domain 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 40 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 326 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 329 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 153 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 236 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 316 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 358 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 417 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 44..65 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 113..162 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 197..276 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 205..249 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 307..312 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 347..371 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" SQ SEQUENCE 424 AA; 47618 MW; 797752B9FCA23B1A CRC64; MFLLPRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVTT NPRNYSYMDL NPALCGSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY EGVNFTPYHA FKCTTSGSND IWMQNKGLFY TQVYKNMAVY RSLTFVNVPY VYNGSAQSTA LCKSGSLVLN NPAYIAREAN FGDYYYKVEA DFYLSGCDEY IVPLCIFNGK FLSNTKYYDD SQYYFNKDTG VIYGLNSTET ITTGFDFNCH YLVLPSGNYL AISNELLLTV PTKAICLNKR KDFTPVQVVD SRWNNARQSD NMTAVACQPP YCYFRNSTTN YVGVYDINHG DAGFTSILSG LLYDSPCFSQ QGVFRYDNVS SVWPLYPYGR CPTAADINTP DVPICVYDPL PIILLGILLG VAVIIIVVLL LYFMVDNGTR LHDA //