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Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein)

 HEMA_CVBM               Reviewed;         424 AA.
P15776;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Hemagglutinin-esterase {ECO:0000255|HAMAP-Rule:MF_04207};
Short=HE protein {ECO:0000255|HAMAP-Rule:MF_04207};
EC=3.1.1.53 {ECO:0000255|HAMAP-Rule:MF_04207};
AltName: Full=E3 glycoprotein {ECO:0000255|HAMAP-Rule:MF_04207};
Flags: Precursor;
Name=HE {ECO:0000255|HAMAP-Rule:MF_04207}; ORFNames=2b;
Bovine coronavirus (strain Mebus) (BCoV) (BCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=11132;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SUBCELLULAR LOCATION.
PubMed=2319653;
Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.;
"Structure and orientation of expressed bovine coronavirus
hemagglutinin-esterase protein.";
J. Virol. 64:1834-1838(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2103108;
Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.;
"Structure and expression of the bovine coronavirus hemagglutinin
protein.";
Adv. Exp. Med. Biol. 276:95-102(1990).
[3]
PROTEIN SEQUENCE OF 19-27.
PubMed=2732694; DOI=10.1099/0022-1317-70-2-345;
Hogue B.G., Kienzle T.E., Brian D.A.;
"Synthesis and processing of the bovine enteric coronavirus
haemagglutinin protein.";
J. Gen. Virol. 70:345-352(1989).
[4]
CHARACTERIZATION.
PubMed=15507445; DOI=10.1074/jbc.M409683200;
Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P.,
Kamerling J.P., Vlasak R., de Groot R.J.;
"Nidovirus sialate-O-acetylesterases: evolution and substrate
specificity of coronaviral and toroviral receptor-destroying
enzymes.";
J. Biol. Chem. 280:6933-6941(2005).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-388 OF APOPROTEIN AND
MUTANT ALA-40 IN COMPLEX WITH RECEPTOR, FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, ACTIVE SITES, GLYCOSYLATION AT ASN-54; ASN-89; ASN-236;
ASN-301; ASN-316 AND ASN-358, DISULFIDE BONDS, AND MUTAGENESIS OF
SER-40; TYR-184; PHE-211; LEU-266 AND LEU-267.
PubMed=18550812; DOI=10.1073/pnas.0800502105;
Zeng Q., Langereis M.A., van Vliet A.L., Huizinga E.G., de Groot R.J.;
"Structure of coronavirus hemagglutinin-esterase offers insight into
corona and influenza virus evolution.";
Proc. Natl. Acad. Sci. U.S.A. 105:9065-9069(2008).
-!- FUNCTION: Structural protein that makes short spikes at the
surface of the virus. Contains receptor binding and receptor-
destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-
acetylneuraminic acid, which is probably the receptor determinant
recognized by the virus on the surface of erythrocytes and
susceptible cells. This receptor-destroying activity is important
for virus release as it probably helps preventing self-aggregation
and ensures the efficient spread of the progeny virus from cell to
cell. May serve as a secondary viral attachment protein for
initiating infection, the spike protein being the major one. May
become a target for both the humoral and the cellular branches of
the immune system. {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
-!- CATALYTIC ACTIVITY: N-acetyl-O-acetylneuraminate + H(2)O = N-
acetylneuraminate + acetate. {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms a complex with the M
protein in the pre-Golgi. Associates then with S-M complex to form
a ternary complex S-M-HE. {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04207}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04207}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04207}. Note=In infected cells
becomes incorporated into the envelope of virions during virus
assembly at the endoplasmic reticulum and cis Golgi. However, some
may escape incorporation into virions and subsequently migrate to
the cell surface. {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:2319653}.
-!- PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-
Rule:MF_04207, ECO:0000269|PubMed:18550812}.
-!- SIMILARITY: Belongs to the influenza type C/coronaviruses
hemagglutinin-esterase family. {ECO:0000255|HAMAP-Rule:MF_04207}.
-----------------------------------------------------------------------
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EMBL; U00735; AAA66393.1; -; Genomic_RNA.
EMBL; S50936; AAB19562.1; -; Genomic_RNA.
PIR; A34666; HMIHBC.
PDB; 3CL4; X-ray; 2.10 A; A=19-388.
PDB; 3CL5; X-ray; 1.80 A; A=19-388.
PDBsum; 3CL4; -.
PDBsum; 3CL5; -.
ProteinModelPortal; P15776; -.
SMR; P15776; -.
iPTMnet; P15776; -.
OrthoDB; VOG0900009Y; -.
BRENDA; 3.1.1.53; 8724.
EvolutionaryTrace; P15776; -.
Proteomes; UP000007554; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046789; F:host cell surface receptor binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0001681; F:sialate O-acetylesterase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
GO; GO:0002683; P:negative regulation of immune system process; IDA:UniProtKB.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
HAMAP; MF_04207; BETA_CORONA_HE; 1.
InterPro; IPR008980; Capsid_hemagglutn.
InterPro; IPR007142; Hemagglutn-estrase_core.
InterPro; IPR003860; Hemagglutn-estrase_hemagglutn.
Pfam; PF03996; Hema_esterase; 1.
Pfam; PF02710; Hema_HEFG; 1.
SUPFAM; SSF49818; SSF49818; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
Host membrane; Hydrolase; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein; Virion.
SIGNAL 1 18 {ECO:0000269|PubMed:2732694}.
SIGNAL 1 16 {ECO:0000255|HAMAP-Rule:MF_04207}.
CHAIN 17 424 Hemagglutinin-esterase.
{ECO:0000255|HAMAP-Rule:MF_04207}.
/FTId=PRO_0000037138.
TOPO_DOM 17 392 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04207}.
TRANSMEM 393 413 Helical. {ECO:0000255|HAMAP-
Rule:MF_04207}.
TOPO_DOM 414 424 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04207}.
REGION 7 127 Esterase domain 1. {ECO:0000255|HAMAP-
Rule:MF_04207}.
REGION 128 266 Receptor binding. {ECO:0000255|HAMAP-
Rule:MF_04207}.
REGION 267 379 Esterase domain 2. {ECO:0000255|HAMAP-
Rule:MF_04207}.
ACT_SITE 40 40 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
ACT_SITE 326 326 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_04207}.
ACT_SITE 329 329 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_04207}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04207}.
DISULFID 44 65 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
DISULFID 113 162 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
DISULFID 197 276 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
DISULFID 205 249 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
DISULFID 307 312 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
DISULFID 347 371 {ECO:0000255|HAMAP-Rule:MF_04207,
ECO:0000269|PubMed:18550812}.
MUTAGEN 40 40 S->A: Loss of enzyme activity.
{ECO:0000269|PubMed:18550812}.
MUTAGEN 184 184 Y->A: Decreased receptor binding.
{ECO:0000269|PubMed:18550812}.
MUTAGEN 211 211 F->A: Loss of receptor binding.
{ECO:0000269|PubMed:18550812}.
MUTAGEN 266 266 L->A: Loss of receptor binding; when
associated with A-267.
{ECO:0000269|PubMed:18550812}.
MUTAGEN 267 267 L->A: Loss of receptor binding; when
associated with A-266.
{ECO:0000269|PubMed:18550812}.
STRAND 23 25 {ECO:0000244|PDB:3CL4}.
STRAND 29 32 {ECO:0000244|PDB:3CL5}.
STRAND 34 39 {ECO:0000244|PDB:3CL5}.
HELIX 40 42 {ECO:0000244|PDB:3CL5}.
HELIX 44 49 {ECO:0000244|PDB:3CL5}.
STRAND 50 52 {ECO:0000244|PDB:3CL5}.
HELIX 55 57 {ECO:0000244|PDB:3CL4}.
HELIX 62 64 {ECO:0000244|PDB:3CL5}.
STRAND 70 73 {ECO:0000244|PDB:3CL5}.
HELIX 78 83 {ECO:0000244|PDB:3CL5}.
STRAND 84 86 {ECO:0000244|PDB:3CL5}.
STRAND 95 100 {ECO:0000244|PDB:3CL5}.
HELIX 107 109 {ECO:0000244|PDB:3CL5}.
HELIX 119 137 {ECO:0000244|PDB:3CL5}.
STRAND 140 147 {ECO:0000244|PDB:3CL5}.
STRAND 150 152 {ECO:0000244|PDB:3CL4}.
STRAND 162 164 {ECO:0000244|PDB:3CL5}.
STRAND 167 169 {ECO:0000244|PDB:3CL5}.
STRAND 171 175 {ECO:0000244|PDB:3CL5}.
STRAND 182 184 {ECO:0000244|PDB:3CL5}.
STRAND 188 207 {ECO:0000244|PDB:3CL5}.
STRAND 211 213 {ECO:0000244|PDB:3CL5}.
STRAND 216 218 {ECO:0000244|PDB:3CL5}.
STRAND 221 226 {ECO:0000244|PDB:3CL5}.
TURN 227 229 {ECO:0000244|PDB:3CL5}.
STRAND 232 236 {ECO:0000244|PDB:3CL5}.
STRAND 242 244 {ECO:0000244|PDB:3CL5}.
STRAND 247 270 {ECO:0000244|PDB:3CL5}.
STRAND 273 280 {ECO:0000244|PDB:3CL5}.
STRAND 286 289 {ECO:0000244|PDB:3CL5}.
HELIX 302 306 {ECO:0000244|PDB:3CL5}.
TURN 309 311 {ECO:0000244|PDB:3CL5}.
STRAND 312 315 {ECO:0000244|PDB:3CL5}.
STRAND 323 326 {ECO:0000244|PDB:3CL5}.
STRAND 329 331 {ECO:0000244|PDB:3CL5}.
HELIX 332 338 {ECO:0000244|PDB:3CL5}.
HELIX 339 342 {ECO:0000244|PDB:3CL5}.
STRAND 346 349 {ECO:0000244|PDB:3CL5}.
STRAND 352 355 {ECO:0000244|PDB:3CL5}.
STRAND 357 359 {ECO:0000244|PDB:3CL5}.
STRAND 368 370 {ECO:0000244|PDB:3CL5}.
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


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