HEMA_CVPV
ID HEMA_CVPV Reviewed; 439 AA.
AC O91262;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 10-FEB-2021, entry version 101.
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};
OS Puffinosis coronavirus (PV) (Puffinosis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=76583;
OH NCBI_TaxID=48688; Puffinus puffinus (Manx shearwater).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10196267; DOI=10.1128/jvi.73.5.3737-3743.1999;
RA Klausegger A., Strobl B., Regl G., Kaser A., Luytjes W., Vlasak R.;
RT "Identification of a coronavirus hemagglutinin-esterase with a substrate
RT specificity different from those of influenza C virus and bovine
RT coronavirus.";
RL J. Virol. 73:3737-3743(1999).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11807232; DOI=10.1099/0022-1317-83-2-395;
RA Wurzer W.J., Obojes K., Vlasak R.;
RT "The sialate-4-O-acetylesterases of coronaviruses related to mouse
RT hepatitis virus: a proposal to reorganize group 2 Coronaviridae.";
RL J. Gen. Virol. 83:395-402(2002).
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; AJ005960; CAA06776.1; -; mRNA.
DR SMR; O91262; -.
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 Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Hydrolase; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CHAIN 23..439
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT /id="PRO_0000037151"
FT TOPO_DOM 23..407
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TOPO_DOM 429..439
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 12..132
FT /note="Esterase domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 133..281
FT /note="Receptor binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 282..395
FT /note="Esterase domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 45
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 49..70
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 118..167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 202..291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 210..264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 322..327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 363..387
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
SQ SEQUENCE 439 AA; 49180 MW; A578474DCBAAF7C0 CRC64;
MGSMCIAMAP RTLLLLIGCQ LALGFNEPLN VVSHLSDDWF LFGDSRSDCS YVENNGHPAF
DWLDLPQELC HSGKISAKSG NSLFKSFHFT DWYNYTGEGD QVIFYEGVNF SPSHGFKCLA
EGDNKRWMGN KARFYALVYK KMAYYRSLSF VNVSYSYGGK AKPTAICKDN TLTLNNPTFI
SKESNYVDYY YESDANFTLE GCDEFIVPLC VFNGHSRGSS SDPANKYYMD SQMYYNMDTG
VFYGFNSTLD VGNTAQNPGL DLTCIYYALT PGNYKAVSLE YLLTIPSKAI CLRKPKRFMP
VQVVDSRWNN AKHSDNMTAV ACQTPYCLFR NTSSGYNGST HDVHHGGFHF RKLLSGLLYN
VSCIAQQGAF FYNNVSSQWP VLGYGQCPTA ANIEFIAPVC LYDPLPVILL GVLLGIAVLI
IVFLLFYFMT DSGVRLHEA
