ID   L5_VACCA                Reviewed;         128 AA.
AC   O57201;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Protein L5;
GN   OrderedLocusNames=MVA084R, ACAM3000_MVA_084;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Envelope protein part of the entry-fusion complex responsible
CC       for the virus membrane fusion with host cell membrane during virus
CC       entry. Also plays a role in cell-cell fusion (syncytium formation) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at least
CC       composed of proteins A16, A21, A28, G3, G9, H2, J5, and L5. Formation
CC       of the viral membrane is necessary for the assembly of the complex.
CC       Interacts with G3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type
CC       III membrane protein {ECO:0000305}. Note=Component of the mature virion
CC       (MV) membrane (By similarity). The mature virion is located in the
CC       cytoplasm of infected cells and is probably released by cell lysis.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Most cysteines are linked by disulfide bonds. They are created by
CC       the viral disulfide bond formation pathway, a poxvirus-specific redox
CC       pathway that operates on the cytoplasmic side of the MV membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae L5 family. {ECO:0000305}.
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DR   EMBL; U94848; AAB96501.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10482.1; -; Genomic_DNA.
DR   PIR; T37360; T37360.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; Genome.
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:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR006956; Poxvirus_L5.
DR   Pfam; PF04872; Pox_L5; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Fusion of virus membrane with host cell membrane;
KW   Fusion of virus membrane with host membrane; Late protein; Membrane;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..128
FT                   /note="Protein L5"
FT                   /id="PRO_0000099625"
FT   TOPO_DOM        1..30
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..107
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  15058 MW;  B4BD848FB6C503FB CRC64;
     MENVPNVYFN PVFIEPTFKH SLLSVYKHRL IVLFEVFIVF ILIYVFFRSE LNMFFMPKRK
     IPDPIDRLRR ANLACEDDKL MIYGLPWMTT QTSALSINSK PIVYKDCAKL LRSINGSQPV
     SLNDVLRR