ID HEMA_CVMA5 Reviewed; 428 AA. AC P31615; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 120. 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 Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Embecovirus; Murine coronavirus. OX NCBI_TaxID=11142; OH NCBI_TaxID=10090; Mus musculus (Mouse). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2845655; DOI=10.1016/0042-6822(88)90512-0; RA Luytjes W., Bredenbeek P.J., Noten A.F.H., Horzinek M.C., Spaan W.J.M.; RT "Sequence of mouse hepatitis virus A59 mRNA 2: indications for RNA RT recombination between coronaviruses and influenza C virus."; RL Virology 166:415-422(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate C12 mutant; RX PubMed=9426441; DOI=10.1006/viro.1997.8877; RA Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.; RT "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is RT associated with a Q159L amino acid substitution in the spike protein."; RL Virology 239:1-10(1997). 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 -!- MISCELLANEOUS: Readthrough of the terminator UGA may occur between the CC codons for Ile-14 and Cys-16. CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses CC hemagglutinin-esterase family. {ECO:0000255|HAMAP-Rule:MF_04207}. CC -!- SEQUENCE CAUTION: CC Sequence=AF029248; Type=Frameshift; 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; M23256; AAA46449.1; ALT_SEQ; Genomic_RNA. DR EMBL; AF029248; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR PIR; B31165; HMIHMH. DR GlyCosmos; P31615; 9 sites, No reported glycans. DR Proteomes; UP000007192; 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; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion. FT SIGNAL 1..19 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CHAIN 20..428 FT /note="Hemagglutinin-esterase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT /id="PRO_0000037145" FT TOPO_DOM 20..404 FT /note="Virion surface" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TRANSMEM 405..425 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT TOPO_DOM 426..428 FT /note="Intravirion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 9..129 FT /note="Esterase domain 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 130..278 FT /note="Receptor binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT REGION 279..392 FT /note="Esterase domain 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 42 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 339 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT ACT_SITE 342 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 91 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 149 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 193 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 313 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 CARBOHYD 332 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 357 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT CARBOHYD 371 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 46..67 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 115..164 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 199..288 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 207..261 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 319..324 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" FT DISULFID 360..384 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207" SQ SEQUENCE 428 AA; 47808 MW; 0CB408413DFB20EC CRC64; MCIAMAPRTL LLLIXCQLVF GFNEPLNIVS HLNDDWFLFG DSRSDCTYVE NNGHPKLDWL DLDPKLCNSG KISAKSGNSL FRSFHFTDFY NYTGEGDQIV FYEGVNFSPS HGFKCLAHGD NKRWMGNKAR FYARVYEKMA QYRSLSFVNV SYAYGGNAKP ASICKDNTLT LNNPTFISKE SNYVDYYYES EANFTLEGCD EFIVPLCGFN GHSKGSSSDA ANKYYTDSQS YYNMDIGVLY GFNSTLDVGN TAKDPGLDLT CRYLALTPGN YKAVSLEYLL SLPSKAICLH KTKRFMPVQV VDSRWSSIRQ SDNMTAAACQ LPYCFFRNTS ANYSGGTHDA HHGDFHFRQL LSGLLYNVSC IAQQGAFLYN NVSSSWPAYG YGHCPTAANI GYMAPVCIYD PLPVILLGVL LGIAVLIIVF LNVLFYDG //