HEMA_CVBM
ID HEMA_CVBM Reviewed; 424 AA.
AC P15776;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 02-JUN-2021, entry version 130.
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 Mebus) (BCoV) (BCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11132;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SUBCELLULAR LOCATION.
RX PubMed=2319653; DOI=10.1128/jvi.64.4.1834-1838.1990;
RA Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.;
RT "Structure and orientation of expressed bovine coronavirus hemagglutinin-
RT esterase protein.";
RL J. Virol. 64:1834-1838(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2103108; DOI=10.1007/978-1-4684-5823-7_14;
RA Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.;
RT "Structure and expression of the bovine coronavirus hemagglutinin
RT protein.";
RL Adv. Exp. Med. Biol. 276:95-102(1990).
RN [3]
RP PROTEIN SEQUENCE OF 19-27.
RX PubMed=2732694; DOI=10.1099/0022-1317-70-2-345;
RA Hogue B.G., Kienzle T.E., Brian D.A.;
RT "Synthesis and processing of the bovine enteric coronavirus haemagglutinin
RT protein.";
RL J. Gen. Virol. 70:345-352(1989).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-388 OF APOPROTEIN AND MUTANT
RP ALA-40 IN COMPLEX WITH RECEPTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP ACTIVE SITES, GLYCOSYLATION AT ASN-54; ASN-89; ASN-236; ASN-301; ASN-316
RP AND ASN-358, DISULFIDE BONDS, AND MUTAGENESIS OF SER-40; TYR-184; PHE-211;
RP LEU-266 AND LEU-267.
RX PubMed=18550812; DOI=10.1073/pnas.0800502105;
RA Zeng Q., Langereis M.A., van Vliet A.L., Huizinga E.G., de Groot R.J.;
RT "Structure of coronavirus hemagglutinin-esterase offers insight into corona
RT and influenza virus evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9065-9069(2008).
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, ECO:0000269|PubMed:18550812}.
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, ECO:0000269|PubMed:18550812};
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, ECO:0000269|PubMed:18550812};
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 ECO:0000269|PubMed:18550812}.
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, ECO:0000269|PubMed:2319653}.
CC -!- PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-Rule:MF_04207,
CC ECO:0000269|PubMed:18550812}.
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; U00735; AAA66393.1; -; Genomic_RNA.
DR EMBL; S50936; AAB19562.1; -; Genomic_RNA.
DR PIR; A34666; HMIHBC.
DR PDB; 3CL4; X-ray; 2.10 A; A=19-388.
DR PDB; 3CL5; X-ray; 1.80 A; A=19-388.
DR PDBsum; 3CL4; -.
DR PDBsum; 3CL5; -.
DR SMR; P15776; -.
DR UniLectin; P15776; -.
DR iPTMnet; P15776; -.
DR BRENDA; 3.1.1.53; 8724.
DR EvolutionaryTrace; P15776; -.
DR Proteomes; UP000007554; 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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0002683; P:negative regulation of immune system process; IDA:UniProtKB.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemagglutinin; Host cell membrane; Host membrane; Hydrolase; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2732694"
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_0000037138"
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 ECO:0000269|PubMed:18550812"
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 ECO:0000269|PubMed:18550812"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
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 ECO:0000269|PubMed:18550812"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
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 ECO:0000269|PubMed:18550812"
FT DISULFID 113..162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT DISULFID 197..276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT DISULFID 205..249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT DISULFID 307..312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT DISULFID 347..371
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207,
FT ECO:0000269|PubMed:18550812"
FT MUTAGEN 40
FT /note="S->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18550812"
FT MUTAGEN 184
FT /note="Y->A: Decreased receptor binding."
FT /evidence="ECO:0000269|PubMed:18550812"
FT MUTAGEN 211
FT /note="F->A: Loss of receptor binding."
FT /evidence="ECO:0000269|PubMed:18550812"
FT MUTAGEN 266
FT /note="L->A: Loss of receptor binding; when associated with
FT A-267."
FT /evidence="ECO:0000269|PubMed:18550812"
FT MUTAGEN 267
FT /note="L->A: Loss of receptor binding; when associated with
FT A-266."
FT /evidence="ECO:0000269|PubMed:18550812"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3CL4"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3CL4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3CL4"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 188..207
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3CL5"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 247..270
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:3CL5"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:3CL5"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:3CL5"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3CL5"
SQ SEQUENCE 424 AA; 47695 MW; FDEF70542F91F305 CRC64;
MFLLLRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVNT NPRNYSYMDL
NPALCDSGKI 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
SVWPLYSYGR CPTAADINTP DVPICVYDPL PLILLGILLG VAVIIIVVLL LYFMVDNGTR
LHDA
