ID   PG053_VACCC             Reviewed;         212 AA.
AC   P68452; P21018;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   02-SEP-2026, entry version 61.
DE   RecName: Full=EFC-associated protein OPG053;
DE   AltName: Full=Protein F9;
GN   Name=OPG053; ORFNames=F9L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: Component of the entry fusion complex (EFC), which consists
CC       of 11 proteins. During cell infection, this complex mediates entry of
CC       the virion core into the host cytoplasm by a two-step mechanism
CC       consisting of lipid mixing of the viral and cellular membranes and
CC       subsequent pore formation. {ECO:0000250|UniProtKB:P24361}.
CC   -!- SUBUNIT: Component of the entry fusion complex (EFC) composed of
CC       OPG053, OPG076, OPG086, OPG094, OPG095, OPG099, OPG107, OPG143, OPG104,
CC       OPG147 and OPG155. Except for OPG095 and OPG052, each of the EFC
CC       proteins is required for assembly or stability of the complex.
CC       {ECO:0000250|UniProtKB:P24361}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P24361};
CC       Single-pass membrane protein {ECO:0000250|UniProtKB:P24361}.
CC       Note=Component of the mature virion (MV) membrane.
CC       {ECO:0000250|UniProtKB:P24361}.
CC   -!- PTM: Disulfid bonds are oxidized in the cytoplasm by OPG088 protein.
CC       {ECO:0000250|UniProtKB:P24361}.
CC   -!- PTM: Unglycosylated because produced in viral factories instead of the
CC       classic ER -Golgi route. {ECO:0000250|UniProtKB:P24361}.
CC   -!- SIMILARITY: Belongs to the orthopoxvirus OPG053 family. {ECO:0000305}.
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DR   EMBL; M35027; AAA48025.1; -; Genomic_DNA.
DR   PIR; E42507; E42507.
DR   SMR; P68452; -.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; ISS:UniProtKB.
DR   InterPro; IPR003472; Virion_mem_poxvirus_L1.
DR   Pfam; PF02442; L1R_F9L; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Late protein; Membrane; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   CHAIN           1..212
FT                   /note="EFC-associated protein OPG053"
FT                   /id="PRO_0000099491"
FT   TOPO_DOM        1..175
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..212
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..55
FT                   /note="by OPG088"
FT                   /evidence="ECO:0000250|UniProtKB:P24361"
FT   DISULFID        47..127
FT                   /note="by OPG088"
FT                   /evidence="ECO:0000250|UniProtKB:P24361"
FT   DISULFID        107..149
FT                   /note="by OPG088"
FT                   /evidence="ECO:0000250|UniProtKB:P24361"
SQ   SEQUENCE   212 AA;  23792 MW;  5C99777A4CFADD9B CRC64;
     MAETKEFKTL YNLFIDSYLQ KLAQHSIPTN VTCAIHIGEV IGQFKNCALR ITNKCMSNSR
     LSFTLMVESF IEVISLLPEK DRRAIAEEIG IDLDDVPSAV SKLEKNCNAY AEVNNIIDIQ
     KLDIGECSAP PGQHMLLQIV NTGSAEANCG LQTIVKSLNK IYVPPIIENR LPYYDPWFLV
     GVAIILVIFT VAICSIRRNL ALKYRYGTFL YV
//