ID   HEMA_BEV                Reviewed;         142 AA.
AC   P31964;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Truncated non-functional hemagglutinin-esterase homolog;
GN   Name=HE;
OS   Berne virus (BEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC   Renitovirus; Equine torovirus.
OX   NCBI_TaxID=11156;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate P138/72;
RX   PubMed=1984666; DOI=10.1016/0042-6822(91)90056-h;
RA   Snijder E.J., den Boon J.A., Horzinek M.C., Spaan W.J.M.;
RT   "Comparison of the genome organization of toro- and coronaviruses: evidence
RT   for two nonhomologous RNA recombination events during Berne virus
RT   evolution.";
RL   Virology 180:448-452(1991).
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   -!- MISCELLANEOUS: The truncated hemagglutinin-esterase of Berne virus is
CC       probably non-functional, since part of its active site is missing.
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; X52375; CAA36602.1; -; mRNA.
DR   PIR; A38524; HMWJBV.
DR   SMR; P31964; -.
DR   Proteomes; UP000006571; 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:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR   InterPro; IPR007142; Hemagglutn-estrase_core.
DR   Pfam; PF03996; Hema_esterase; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemagglutinin; Host cell membrane;
KW   Host membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..142
FT                   /note="Truncated non-functional hemagglutinin-esterase
FT                   homolog"
FT                   /id="PRO_0000106127"
FT   TOPO_DOM        1..117
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..142
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   142 AA;  15571 MW;  5421B9180E36116D CRC64;
     MNFTVPVQAI QSIWSVGKES DDAIAEACKP PFCIYFSKKT PYTVTNGSNA DHGDDEVRQM
     MRGLLYNSSC ISAQGHTPLA LYSTAMLYPP MYGSCPQYVK LFDGSGSESV DVISSSYFVA
     TWVLLVVVII LVFIIISFCI SN