HEMA_CVMJH
ID HEMA_CVMJH Reviewed; 439 AA.
AC Q83356; Q83353;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 JHM) (MHV-JHM) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11144;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1646274; DOI=10.1099/0022-1317-72-6-1309;
RA Pfleiderer M., Routledge E., Herrler G., Siddell S.G.;
RT "High level transient expression of the murine coronavirus haemagglutinin-
RT esterase.";
RL J. Gen. Virol. 72:1309-1315(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2547994; DOI=10.1128/jvi.63.9.3729-3736.1989;
RA Shieh C.-K., Lee H.-J., Yokomori K., la Monica N., Makino S., Lai M.M.C.;
RT "Identification of a new transcriptional initiation site and the
RT corresponding functional gene 2b in the murine coronavirus RNA genome.";
RL J. Virol. 63:3729-3736(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2103098; DOI=10.1007/978-1-4684-5823-7_4;
RA Pfleiderer M., Routledge E., Siddell S.G.;
RT "Functional analysis of the coronavirus MHV-JHM surface glycoproteins in
RT vaccinia virus recombinants.";
RL Adv. Exp. Med. Biol. 276:21-31(1990).
RN [4]
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; D00764; BAA00661.1; -; Genomic_RNA.
DR EMBL; M28348; AAA46442.1; -; Genomic_RNA.
DR PIR; JQ0997; JQ0997.
DR SMR; Q83356; -.
DR Proteomes; UP000007193; Genome.
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_0000037147"
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 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 309
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 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"
FT CONFLICT 133
FT /note="R -> A (in Ref. 2; AAA46442)"
FT CONFLICT 245
FT /note="F -> L (in Ref. 2)"
FT CONFLICT 247
FT /note="S -> C (in Ref. 2)"
SQ SEQUENCE 439 AA; 49110 MW; 3E4E70E58D2FB762 CRC64;
MGSTCIAMAP RTLLLLIGCQ LVFGFNEPLN IVSHLNDDWF LFGDSRSDCT YVENNGHPKL
DWLDLDPKLC NSGKISAKSG NSLFRSFHFT DFYNYTGEGD QIVFYEGVNF SPNHGFKCLA
YGDNKRWMGN KARFYARVYE KMAQYRSLSF VNVPYAYGGK AKPTSICKHK TLTLNNPTFI
SKESNYVDYY YESEANFTLA GCDEFIVPLC VFNGHSKGSS SDPANKYYMD SQSYYNMDTG
VLYGFNSTLD VGNTAKDPGL DLTCRYLALT PGNYKAVSLE YLLSLPSKAI CLRKPKRFMP
VQVVDSRWNS TRQSDNMTAV ACQLPYCFFR NTSADYSGGT HDVHHGDFHF RQLLSGLLLN
VSCIAQQGAF LYNNVSSSWP AYGYGQCPTA ANIGYMAPVC IYDPLPVVLL GVLLGIAVLI
IVFLILYFMT DSGVRLHEA
