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 27-MAR-2024, entry version 85. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF159585; AAF00614.1; -; mRNA. DR SMR; Q9Q9G3; -. DR GlyCosmos; Q9Q9G3; 7 sites, No reported glycans. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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:RHEA. DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:RHEA. 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; SSF52266; SGNH hydrolase; 1. DR SUPFAM; SSF49818; Viral protein domain; 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 //