ID Q06BD8_9BETC Unreviewed; 424 AA.
AC Q06BD8;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 59.
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, ECO:0000313|EMBL:ABI94000.1};
OS Bovine coronavirus isolate Alpaca.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Betacoronavirus 1.
OX NCBI_TaxID=404135 {ECO:0000313|EMBL:ABI94000.1, ECO:0000313|Proteomes:UP000154814};
RN [1] {ECO:0000313|EMBL:ABI94000.1, ECO:0000313|Proteomes:UP000154814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17459444; DOI=10.1016/j.virol.2007.03.035;
RA Jin L., Cebra C.K., Baker R.J., Mattson D.E., Cohen S.A., Alvarado D.E.,
RA Rohrmann G.F.;
RT "Analysis of the genome sequence of an alpaca coronavirus.";
RL Virology 365:198-203(2007).
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; DQ915164; ABI94000.1; -; Genomic_RNA.
DR Proteomes; UP000154814; 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 17..424
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT /id="PRO_5023307032"
FT TRANSMEM 392..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361278"
FT TOPO_DOM 414..424
FT /note="Intravirion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DOMAIN 22..377
FT /note="Haemagglutinin-esterase glycoprotein core"
FT /evidence="ECO:0000259|Pfam:PF03996"
FT DOMAIN 129..263
FT /note="Haemagglutinin-esterase glycoprotein haemagglutinin"
FT /evidence="ECO:0000259|Pfam:PF02710"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT ACT_SITE 329
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 44..65
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 113..162
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 307..312
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
FT DISULFID 347..371
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04207"
SQ SEQUENCE 424 AA; 47563 MW; 9772F2B9FCA79B19 CRC64;
MFLLPRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVTT NPRNYSYMDL
NPALCGSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY EGVNFTPYHA FKCTTSGSND
IWMQNKGLFY TQVYKNMAVY RSLTFVNVPY VYNGSAQSTA LCKSGSLVLN NPAYIAREAN
FGDYYYKVEA DFYLSGCDEY IVPLCIFNGK FLSNTKYYDD SQYYFNKDTG VIYGLNSTET
ITTGFDFNCH YLVLPSGNYL AISNELLLTV PTKAICLNKR KDFTPVQVVD SRWNNATQSD
NMTAVACQPP YCYFRNSTTN YVGVYDINHG DAGFTSILSG LLYDSPCFSQ QGVFRYDNVS
SVWPLYPYGR CPTAADINTP DVPICVYDPL PIILLGILLG VAVIIIVVLL LYFMVDNGTR
LHDA
//
