HEMA_CVMDV
ID HEMA_CVMDV Reviewed; 431 AA.
AC O92367;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 02-JUN-2021, entry version 102.
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 DVIM) (MHV-DVIM) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=231423;
OH NCBI_TaxID=10088; Mus.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Compton S.R., Moore K.M.;
RT "Sequence of the hemagglutinin-esterase (HE) genes of two enterotropic MHV
RT strains.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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-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 host RER. {ECO:0000255|HAMAP-Rule:MF_04207}.
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; AF091734; AAC63044.1; -; mRNA.
DR PDB; 5JIF; X-ray; 2.00 A; A/B=24-395.
DR PDBsum; 5JIF; -.
DR SMR; O92367; -.
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: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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hemagglutinin;
KW Host cell membrane; Host membrane; Hydrolase; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CHAIN 22..431
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT /id="PRO_0000037146"
FT TOPO_DOM 22..399
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TOPO_DOM 421..431
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 11..131
FT /note="Esterase domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 132..274
FT /note="Receptor binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 275..387
FT /note="Esterase domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 337
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 48..69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 117..166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 205..284
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 213..257
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 315..320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 355..379
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5JIF"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:5JIF"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 204..218
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5JIF"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:5JIF"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:5JIF"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:5JIF"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:5JIF"
SQ SEQUENCE 431 AA; 48440 MW; DF4BE9EE0AE7301B CRC64;
MARTDAMAPR TLLLVLSLGY AFGFNEPLNV VSHLNDDWFL FGDSRSDCNH INNLSQQNYN
YMDINPELCK SGKISAKAGN SLFKSFHFTD FYNYTGEGSQ IIFYEGVNFT PYVGFKCLNN
GDNNRWMGNK ARFYTQLYQK MAHYRSLSVI NITYTYNGSA GPVSMCKHIA NGVTLTLNNP
TFIGKEVSKP DYYYESEANF TLQGCDEFIV PLCVFNGQYL SSKLYYDDSQ YYYNVDTGVL
YGFNSTLNIT SGLDLTCIYL ALTPGNYISI SNELLLTVPS KAICLRKPKA FTPVQVVDSR
WHSNRQSDNM TAIACQLPYC YFRNTTSDYN GVYDSHHGDA GFTSILAGLM YNVSCLAQQG
AFVYNNVSSS WPQYPYGHCP TAANIVFMAP VCMYDPLPVI LLGVLLGIAV LIIVFLMFYF
MTDSGVRLHE A
