HEMA_BRV2
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 02-JUN-2021, entry version 66.
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.
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}.
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DR EMBL; Y10866; CAA71819.1; -; Genomic_RNA.
DR SMR; P0C0W0; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
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; SSF49818; SSF49818; 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
