HEMA_CVHN1
ID HEMA_CVHN1 Reviewed; 386 AA.
AC Q5MQD1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 02-JUN-2021, entry version 95.
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=2;
OS Human coronavirus HKU1 (isolate N1) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=443239;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15613317; DOI=10.1128/jvi.79.2.884-895.2005;
RA Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y.,
RA Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M., Wong S.S.Y.,
RA Guan Y., Peiris J.S.M., Yuen K.-Y.;
RT "Characterization and complete genome sequence of a novel coronavirus,
RT coronavirus HKU1, from patients with pneumonia.";
RL J. Virol. 79:884-895(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 -!- MISCELLANEOUS: Isolate N1 belongs to genotype A.
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; AY597011; AAT98579.1; -; Genomic_RNA.
DR RefSeq; YP_173237.1; NC_006577.2.
DR PDB; 6Y3Y; EM; 3.39 A; A/B=14-355.
DR PDBsum; 6Y3Y; -.
DR SMR; Q5MQD1; -.
DR DNASU; 3200425; -.
DR GeneID; 3200425; -.
DR KEGG; vg:3200425; -.
DR Proteomes; UP000008170; 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:0001681; F:sialate O-acetylesterase activity; ISS:UniProtKB.
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..11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CHAIN 12..386
FT /note="Hemagglutinin-esterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT /id="PRO_0000297761"
FT TOPO_DOM 12..359
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT TOPO_DOM 381..386
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 1..121
FT /note="Esterase domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 122..236
FT /note="Receptor binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT REGION 237..349
FT /note="Esterase domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 38..59
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 107..154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 180..246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 188..219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 277..282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT DISULFID 317..341
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04207"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6Y3Y"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6Y3Y"
SQ SEQUENCE 386 AA; 44679 MW; 8A880856BCDE8818 CRC64;
MLIIFLFFYF CYGFNEPLNV VSHLNHDWFL FGDSRSDCNH INNLKIKNFD YLDIHPSLCN
NGKISSSAGD SIFKSFHFTR FYNYTGEGDQ IIFYEGVNFN PYHRFKCFPN GSNDVWLLNK
VRFYRALYSN MAFFRYLTFV DIPYNVSLSK FNSCKSDILS LNNPIFINYS KEVYFTLLGC
SLYLVPLCLF KSNFSQYYYN IDTGSVYGFS NVVYPDLDCI YISLKPGSYK VSTTAPFLSL
PTKALCFDKS KQFVPVQVVD SRWNNERASD ISLSVACQLP YCYFRNSSAN YVGKYDINHG
DSGFISILSG LLYNVSCISY YGVFLYDNFT SIWPYYSFGR CPTSSIIKHP ICVYDFLPII
LQGILLCLAL LFVVFLLFLL YNDKSH
