HEMA_CVBQ
ID HEMA_CVBQ Reviewed; 424 AA.
AC P59709; P24351; Q66166; Q66167; Q66168; Q77NC5; Q98VL2; Q9DGT1; Q9DGT9;
AC Q9DR84; Q9DRF4; Q9DRF5;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 10-FEB-2021, entry version 96.
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 Quebec) (BCoV) (BCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11133;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732684; DOI=10.1099/0022-1317-70-1-155;
RA Parker M.D., Cox G.J., Deregt D., Fitzpatrick D.R., Babiuk L.A.;
RT "Cloning and in vitro expression of the gene for the E3 haemagglutinin
RT glycoprotein of bovine coronavirus.";
RL J. Gen. Virol. 70:155-164(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BCQ.2590, Isolate BCQ.3, and Isolate BCQ.571;
RX PubMed=7730812; DOI=10.1099/0022-1317-76-5-1263;
RA Dea S., Michaud L., Milane G.;
RT "Comparison of bovine coronavirus isolates associated with neonatal calf
RT diarrhoea and winter dysentery in adult dairy cattle in Quebec.";
RL J. Gen. Virol. 76:1263-1270(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BCQ.1523, Isolate BCQ.2590, Isolate BCQ.3994,
RC Isolate BCQ.571, and Isolate BCQ.7373;
RX PubMed=11774537; DOI=10.1007/978-1-4615-1325-4_9;
RA Gelinas A.-M., Sasseville A.M.-J., Dea S.;
RT "Identification of specific variations within the HE, S1, and ORF4 genes of
RT bovine coronaviruses associated with enteric and respiratory diseases in
RT dairy cattle.";
RL Adv. Exp. Med. Biol. 494:63-67(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BCQ.1523, Isolate BCQ.2439, Isolate BCQ.2442,
RC Isolate BCQ.2508, Isolate BCQ.3708, Isolate BCQ.376, Isolate BCQ.701, and
RC Isolate BCQ.7373;
RX PubMed=11504427; DOI=10.1007/s007050170117;
RA Kourtesis A.B., Gelinas A.-M., Dea S.;
RT "Genomic and antigenic variations of the HE glycoprotein of bovine
RT coronaviruses associated with neonatal calf diarrhea and winter
RT dysentery.";
RL Arch. Virol. 146:1219-1230(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BCQ.3994;
RX PubMed=11376845; DOI=10.1016/s0168-1702(01)00243-x;
RA Gelinas A.-M., Boutin M., Sasseville A.M.-J., Dea S.;
RT "Bovine coronaviruses associated with enteric and respiratory diseases in
RT Canadian dairy cattle display different reactivities to anti-HE monoclonal
RT antibodies and distinct amino acid changes in their HE, S and ns4.9
RT protein.";
RL Virus Res. 76:43-57(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11774548;
RA Yoo D., Pei Y.;
RT "Full-length genomic sequence of bovine coronavirus (31 kb). Completion of
RT the open reading frame 1a/1b sequences.";
RL Adv. Exp. Med. Biol. 494:73-76(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 -!- MISCELLANEOUS: The sequence shown is that of Quebec reference strain.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000255|HAMAP-Rule:MF_04207}.
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DR EMBL; L38962; AAA92989.1; -; Genomic_RNA.
DR EMBL; L38963; AAA92990.1; -; Genomic_RNA.
DR EMBL; U06093; AAA92991.1; -; Genomic_RNA.
DR EMBL; AF239306; AAG40594.1; -; Genomic_RNA.
DR EMBL; AF239307; AAG40600.1; -; Genomic_RNA.
DR EMBL; AF230523; AAG40588.1; -; Genomic_RNA.
DR EMBL; AF230524; AAG40589.1; -; Genomic_RNA.
DR EMBL; AF230525; AAG40590.1; -; Genomic_RNA.
DR EMBL; AF230526; AAG40591.1; -; Genomic_RNA.
DR EMBL; AF230527; AAG40592.1; -; Genomic_RNA.
DR EMBL; AF230528; AAG40593.1; -; Genomic_RNA.
DR EMBL; AF339836; AAK14397.1; -; Genomic_RNA.
DR EMBL; AF220295; AAL40399.1; -; Genomic_RNA.
DR PIR; A31684; HMIHBQ.
DR RefSeq; NP_150076.1; NC_003045.1.
DR SMR; P59709; -.
DR GeneID; 921684; -.
DR KEGG; vg:921684; -.
DR Proteomes; UP000008572; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
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; SSF49818; SSF49818; 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_0000037143"
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"
FT VARIANT 5
FT /note="L -> P (in strain: Isolate BCQ.3, Isolate BCQ.1523,
FT Isolate BCQ.2439, Isolate BCQ.2442, Isolate BCQ.2508,
FT Isolate BCQ.2590, Isolate BCQ.3708, Isolate BCQ.3994 and
FT Isolate BCQ.7373)"
FT VARIANT 8
FT /note="V -> A (in strain: Isolate BCQ.2590)"
FT VARIANT 11
FT /note="S -> C (in strain: Isolate BCQ.1523, Isolate
FT BCQ.2442 and Isolate BCQ.2508)"
FT VARIANT 49
FT /note="N -> T (in strain: Isolate BCQ.376, Isolate BCQ.701,
FT Isolate BCQ.1523, Isolate BCQ.2442, Isolate BCQ.2508,
FT Isolate BCQ.3708, Isolate BCQ.3994 and Isolate BCQ.7373)"
FT VARIANT 53
FT /note="R -> P (in strain: Isolate BCQ.2590)"
FT VARIANT 66
FT /note="D -> G (in strain: Isolate BCQ.376, Isolate BCQ.701,
FT Isolate BCQ.3708 and Isolate BCQ.3994)"
FT VARIANT 103
FT /note="L -> I (in strain: Isolate BCQ.2439)"
FT VARIANT 103
FT /note="L -> V (in strain: Isolate BCQ.3, Isolate BCQ.376,
FT Isolate BCQ.701, Isolate BCQ.1523, Isolate BCQ.2442,
FT Isolate BCQ.2508, Isolate BCQ.2590, Isolate BCQ.3708,
FT Isolate BCQ.3994 and Isolate BCQ.7373)"
FT VARIANT 114
FT /note="T -> I (in strain: Isolate BCQ.3708)"
FT VARIANT 182
FT /note="G -> R (in strain: Isolate BCQ.7373)"
FT VARIANT 245
FT /note="F -> L (in strain: Isolate BCQ.7373)"
FT VARIANT 282
FT /note="D -> G (in strain: Isolate BCQ.7373)"
FT VARIANT 344
FT /note="D -> A (in strain: Isolate BCQ.2590)"
FT VARIANT 350
FT /note="Q -> R (in strain: Isolate BCQ.2590)"
FT VARIANT 367
FT /note="S -> P (in strain: Isolate BCQ.376, Isolate BCQ.701,
FT Isolate BCQ.1523, Isolate BCQ.2439, Isolate BCQ.2442,
FT Isolate BCQ.2508, Isolate BCQ.2590, Isolate BCQ.3708,
FT Isolate BCQ.3994 and Isolate BCQ.7373)"
FT VARIANT 392
FT /note="L -> I (in strain: Isolate BCQ.3, Isolate BCQ.376,
FT Isolate BCQ.571, Isolate BCQ.701, Isolate BCQ.1523, Isolate
FT BCQ.2439, Isolate BCQ.2442, Isolate BCQ.2508, Isolate
FT BCQ.3708, Isolate BCQ.3994 and Isolate BCQ.7373)"
SQ SEQUENCE 424 AA; 47709 MW; F1CE076E4AA7B277 CRC64;
MFLLLRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVNT NPRNYSYMDL
NPALCDSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY EGLNFTPYHA 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
SVWPLYSYGR CPTAADINTP DVPICVYDPL PLILLGILLG VAVIIIVVLL LYFMVDNGTR
LHDA
