HEMA_BRV1
ID HEMA_BRV1 Reviewed; 416 AA.
AC P0C0V9; O39517; Q3T8I8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 02-JUN-2021, entry version 78.
DE RecName: Full=Hemagglutinin-esterase;
DE Short=HE protein;
DE EC=3.1.1.53;
DE AltName: Full=E3 glycoprotein;
DE Flags: Precursor;
GN Name=HE;
OS Breda virus 1 (BRV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC Renitovirus.
OX NCBI_TaxID=360393;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9879765; DOI=10.1016/s0168-1702(98)00104-x;
RA Duckmanton L.M., Tellier R., Liu P., Petric M.;
RT "Bovine torovirus: sequencing of the structural genes and expression of the
RT nucleocapsid protein of Breda virus.";
RL Virus Res. 58:83-96(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16137782; DOI=10.1016/j.virusres.2005.07.005;
RA Draker R., Roper R.L., Petric M., Tellier R.;
RT "The complete sequence of the bovine torovirus genome.";
RL Virus Res. 115:56-68(2006).
RN [3]
RP CHARACTERIZATION.
RX PubMed=15507445; DOI=10.1074/jbc.m409683200;
RA Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P.,
RA Kamerling J.P., Vlasak R., de Groot R.J.;
RT "Nidovirus sialate-O-acetylesterases: evolution and substrate specificity
RT of coronaviral and toroviral receptor-destroying enzymes.";
RL J. Biol. Chem. 280:6933-6941(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-392 OF APOPROTEIN AND IN
RP COMPLEX WITH RECEPTOR ANALOG, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION
RP AT ASN-76; ASN-257; ASN-278; ASN-313; ASN-322 AND ASN-343, DISULFIDE BONDS,
RP AND MUTAGENESIS OF SER-64; ARG-103; TRP-109; LEU-168; LEU-170 AND PHE-207.
RX PubMed=19721004; DOI=10.1073/pnas.0904266106;
RA Langereis M.A., Zeng Q., Gerwig G.J., Frey B., von Itzstein M.,
RA Kamerling J.P., de Groot R.J., Huizinga E.G.;
RT "Structural basis for ligand and substrate recognition by torovirus
RT hemagglutinin esterases.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15897-15902(2009).
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-9-di-O-
CC acetylneuraminic acid, which is probably the receptor determinant
CC recognized by the virus on the surface of erythrocytes and susceptible
CC cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-
CC acetyl-9-O-acetylneuraminic acid, but displays a substrate preference
CC for N-acetyl-9-di-O-acetylneuraminic acid. This receptor-destroying
CC activity is important for virus release as it probably helps preventing
CC self-aggregation and ensures the efficient spread of the progeny virus
CC from cell to cell. May serve as a secondary viral attachment protein
CC for initiating infection, the spike protein being the major one. Seems
CC to be a 'luxury' protein that is not absolutely necessary for virus
CC infection in culture. However, its presence in the virus may alter its
CC pathogenicity. May become a target for both the humoral and the
CC cellular branches of the immune system. {ECO:0000269|PubMed:19721004}.
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:0000269|PubMed:19721004};
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:0000269|PubMed:19721004};
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=In infected
CC cells becomes incorporated into the envelope of virions during virus
CC assembly at the endoplasmic reticulum and cis Golgi. However, some may
CC escape incorporation into virions and subsequently migrate to the cell
CC surface (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000305}.
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DR EMBL; AF076621; AAD03842.1; -; Genomic_RNA.
DR EMBL; AY427798; AAS17961.1; -; Genomic_RNA.
DR RefSeq; YP_337909.1; NC_007447.1.
DR PDB; 3I26; X-ray; 1.80 A; A/B/C/D=15-392.
DR PDB; 3I27; X-ray; 2.00 A; A/B/C/D=15-392.
DR PDBsum; 3I26; -.
DR PDBsum; 3I27; -.
DR SMR; P0C0V9; -.
DR DIP; DIP-48962N; -.
DR UniLectin; P0C0V9; -.
DR iPTMnet; P0C0V9; -.
DR GeneID; 3707767; -.
DR KEGG; vg:3707767; -.
DR EvolutionaryTrace; P0C0V9; -.
DR Proteomes; UP000000355; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IMP:UniProtKB.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
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; IDA:UniProtKB.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR InterPro; IPR008980; Capsid_hemagglutn.
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; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..416
FT /note="Hemagglutinin-esterase"
FT /id="PRO_0000045398"
FT TOPO_DOM 15..393
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..416
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 4..121
FT /note="Esterase domain first part"
FT /evidence="ECO:0000250"
FT REGION 122..263
FT /note="Receptor binding"
FT /evidence="ECO:0000250"
FT REGION 264..379
FT /note="Esterase domain second part"
FT /evidence="ECO:0000250"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 41..57
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 88..136
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 200..246
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 206..213
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 304..309
FT /evidence="ECO:0000269|PubMed:19721004"
FT DISULFID 346..371
FT /evidence="ECO:0000269|PubMed:19721004"
FT VARIANT 29
FT /note="F -> S"
FT VARIANT 114
FT /note="D -> G"
FT VARIANT 133
FT /note="T -> I"
FT VARIANT 152
FT /note="Q -> K"
FT VARIANT 155
FT /note="V -> E"
FT VARIANT 159
FT /note="N -> K"
FT VARIANT 214
FT /note="L -> R"
FT VARIANT 234
FT /note="P -> S"
FT VARIANT 238
FT /note="S -> L"
FT VARIANT 416
FT /note="C -> V"
FT MUTAGEN 64
FT /note="S->T: Strongly reduced activity toward 7,9-di-O-
FT acetylated sialic acids and strongly increased activity
FT toward 9-mono-O-acetylated sialic acids."
FT /evidence="ECO:0000269|PubMed:19721004"
FT MUTAGEN 103
FT /note="R->H: Strongly reduced activity toward both 7,9-di
FT and 9-mono-O-acetylated sialic acids. Increased activity
FT toward synthetic substrate (4-nitrophenyl)acetate."
FT /evidence="ECO:0000269|PubMed:19721004"
FT MUTAGEN 109
FT /note="W->A: Reduced lectin activity."
FT /evidence="ECO:0000269|PubMed:19721004"
FT MUTAGEN 168
FT /note="L->A: Reduced lectin activity."
FT /evidence="ECO:0000269|PubMed:19721004"
FT MUTAGEN 170
FT /note="L->A: Reduced lectin activity."
FT /evidence="ECO:0000269|PubMed:19721004"
FT MUTAGEN 207
FT /note="F->A: Loss of lectin activity."
FT /evidence="ECO:0000269|PubMed:19721004"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3I26"
FT TURN 44..49
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 112..131
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 253..267
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:3I26"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:3I26"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3I26"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3I26"
SQ SEQUENCE 416 AA; 46440 MW; 384C406385439054 CRC64;
MLSLILFFPS FAFAATPVTP YYGPGHITFD WCGFGDSRSD CTNPQSPMSL DIPQQLCPKF
SSKSSSSMFL SLHWNNHSSF VSYDYFNCGV EKVFYEGVNF SPRKQYSCWD EGVDGWIELK
TRFYTKLYQM ATTSRCIKLI QLQAPSSLPT LQAGVCRTNK QLPDNPRLAL LSDTVPTSVQ
FVLPGSSGTT ICTKHLVPFC YLNHGCFTTG GSCLPFGVSY VSDSFYYGYY DATPQIGSTE
SHDYVCDYLF MEPGTYNAST VGKFLVYPTK SYCMDTMNIT VPVQAVQSIW SEQYASDDAI
GQACKAPYCI FYNKTTPYTV TNGSDANHGD DEVRMMMQGL LRNSSCISPQ GSTPLALYST
EMIYEPNYGS CPQFYKLFDT SGNENIDVIS SSYFVATWVL LVVVVILIFV IISFFC
