ID H9BZX8_9BETC Unreviewed; 439 AA.
AC H9BZX8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Hemagglutinin-esterase {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE Short=HE protein {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE EC=3.1.1.53 {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
DE AltName: Full=E3 glycoprotein {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
GN Name=HE {ECO:0000256|HAMAP-Rule:MF_04207,
GN ECO:0000256|RuleBase:RU361278};
OS Murine hepatitis virus strain S/3239-17.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Murine coronavirus.
OX NCBI_TaxID=1163669 {ECO:0000313|EMBL:AFD97612.1, ECO:0000313|Proteomes:UP000118088};
RN [1] {ECO:0000313|EMBL:AFD97612.1, ECO:0000313|Proteomes:UP000118088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHV/S/3239-17 {ECO:0000313|EMBL:AFD97612.1};
RA Thor S.W., Hilt D.A., Kissinger J.C., Robertson J.S., Lemke C.,
RA Paterson A.H., Jackwood M.W.;
RT "Genomic, phylogenetic and recombinational analysis of alpha- and
RT betacoronaviruses.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}.
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 Evidence={ECO:0000256|ARBA:ARBA00000954, ECO:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
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 Evidence={ECO:0000256|ARBA:ARBA00001221, ECO:0000256|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:0000256|HAMAP-Rule:MF_04207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Host cell membrane {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-
CC Rule:MF_04207, ECO:0000256|RuleBase:RU361278}. Virion membrane
CC {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
CC Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04207,
CC ECO:0000256|RuleBase:RU361278}. Note=In infected cells becomes
CC incorporated into the envelope of virions during virus assembly at the
CC endoplasmic reticulum and cis Golgi. However, some may escape
CC incorporation into virions and subsequently migrate to the cell
CC surface. {ECO:0000256|HAMAP-Rule:MF_04207,
CC ECO:0000256|RuleBase:RU361278}.
CC -!- PTM: N-glycosylated in the host RER. {ECO:0000256|HAMAP-Rule:MF_04207}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000256|ARBA:ARBA00010920,
CC ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04207}.
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DR EMBL; JQ173883; AFD97612.1; -; Genomic_RNA.
DR SMR; H9BZX8; -.
DR Proteomes; UP000118088; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:RHEA.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:RHEA.
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; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF49818; Viral protein domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04207};
KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04207};
KW Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04207};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04207};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04207,
KW ECO:0000256|RuleBase:RU361278};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04207}.
FT CHAIN 23..439
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT /id="PRO_5023308951"
FT TOPO_DOM 23..407
FT /note="Virion surface"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT TRANSMEM 405..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361278"
FT TOPO_DOM 429..439
FT /note="Intravirion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DOMAIN 13..393
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 133..279
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT REGION 133..281
FT /note="Receptor binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT REGION 282..395
FT /note="Esterase domain 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 45
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 49..70
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 118..167
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 202..291
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 210..264
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 322..327
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 363..387
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
SQ SEQUENCE 439 AA; 49205 MW; 68CC6EC9CD108FAA CRC64;
MGCMCIAMAP RTLLLLIGCQ LVFGFNEPLN IVSHLNDDWF LFGDSRSDCT YVENNGHPKL
DWLDLDPKLC NSGRISAKSG NSLFRSFHFI DFYNYSGEGD QVIFYEGVNF SPSHGFKCLA
YGDNKRWMGN KARFYARVYE KMAQYRSLSF VNVSYAYGGN AKPTSICKDK TLTLNNPTFI
SKESNYVDYY YESEANFTLQ GCDEFIVPLC VFNGHSKGSS SDPANKYYTD SQSYYNMDTG
VLYGFNSTLD VGNTVQNPGL DLTCRYLALT PGNYKAVSLE YLLSLPSKAI CLRKPKSFMP
VQVVDSRWNS TRQSDNMTAV ACQLPYCFFR NTSADYSGGT HDVHHGDFHF RQLLSGLLYN
VSCIAQQGAF VYNNVSSSWP AYGYGHCPTA ANIGYMAPVC IYDPLPVILL GVLLGIAVLI
IVFLMFYFMT DSGVRLHEA
//
