HEMA_HUTV
ID HEMA_HUTV Reviewed; 416 AA.
AC Q9Q9G3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 82.
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 Human torovirus (HuTV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus.
OX NCBI_TaxID=67605;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RETRACTED PAPER.
RX PubMed=10518710; DOI=10.1016/s0168-1702(99)00088-x;
RA Duckmanton L., Tellier R., Richardson C., Petric M.;
RT "The novel hemagglutinin-esterase genes of human torovirus and Breda
RT virus.";
RL Virus Res. 64:137-149(1999).
RN [2]
RP RETRACTION NOTICE OF PUBMED:10518710.
RX PubMed=11682139; DOI=10.1016/s0168-1702(01)00372-0;
RA Duckmanton L., Tellier R., Richardson C., Petric M.;
RL Virus Res. 81:167-167(2001).
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-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. Seems to be a 'luxury' protein that is not
CC absolutely necessary for virus infection in culture. However, its
CC presence in the virus may alter its pathogenicity. May become a target
CC for both the humoral and the cellular branches of the immune system (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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 -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the influenza type C/coronaviruses
CC hemagglutinin-esterase family. {ECO:0000305}.
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DR EMBL; AF159585; AAF00614.1; -; mRNA.
DR SMR; Q9Q9G3; -.
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: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: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 2: Evidence at transcript 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..14
FT /evidence="ECO:0000255"
FT CHAIN 15..416
FT /note="Hemagglutinin-esterase"
FT /id="PRO_0000045400"
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 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 41..57
FT /evidence="ECO:0000250"
FT DISULFID 88..136
FT /evidence="ECO:0000250"
FT DISULFID 108..156
FT /evidence="ECO:0000250"
FT DISULFID 192..273
FT /evidence="ECO:0000250"
FT DISULFID 200..246
FT /evidence="ECO:0000250"
FT DISULFID 206..213
FT /evidence="ECO:0000250"
FT DISULFID 304..309
FT /evidence="ECO:0000250"
FT DISULFID 346..371
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 46534 MW; 13607F00B989ACD8 CRC64;
MLSLILFFPS FAFAVTPVTP YFGPLYITFN CCLFGDSRSD CTKVQSPMSL DNPQNFCPNF
SLKSSSSMFF SIHYNNHSSL VLFDNFNCRI EKVYYNGVNL SPRNQYSCYD EGVDSYMELK
TSFNIKLNQM ATILRCIKLI QLKARSSFTT LQDVVCRTNK YLPNNPTFAL LSDTVPTWVQ
FVLPDLSGKT ICIKYLVPFC HLNHGCFTAG SSCPPFGVSY VSDSFNYGFN DATPYIGLAE
SHDNVCDYLF VEAGTHNASI VGNFLFYPTK SYCFNTMNFT VPVQAIQSIW SEGNESDDAI
AEACKPPFCI YYSKTTPYTV TNGSNADHRD DEVRMMVRGL LYNSSCISAQ GSTPLALYST
AMLYAPIYGS CPQYVKLFDT SGSESVDVIS SSYFVATWVL LVVVVILIFV IISFFC
