ID   L1_VARV                 Reviewed;         250 AA.
AC   P0DOT8; P33040;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   29-SEP-2021, entry version 10.
DE   RecName: Full=Protein L1;
DE   AltName: Full=Virion membrane protein M25;
GN   ORFNames=L1R;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: Envelope protein which probably plays a role in virus entry
CC       into the host cell. Is probably involved in the virus attachment to the
CC       host cell surface and associates with the entry/fusion complex (EFC).
CC       Needed for fusion and penetration of the virus core into host cell (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G4; this interaction involves formation of a
CC       transient disulfide-bonded intermediate, allowing disulfide bond
CC       transfer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Note=Localizes to the membrane
CC       surrounding the core of mature virus particles (MV). {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Myristoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae L1 family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60821.1; -; Genomic_DNA.
DR   PIR; T28511; T28511.
DR   RefSeq; NP_042117.1; NC_001611.1.
DR   SMR; P0DOT8; -.
DR   GeneID; 1486470; -.
DR   KEGG; vg:1486470; -.
DR   Proteomes; UP000119805; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR003472; Virion_mem_poxvirus_L1.
DR   Pfam; PF02442; L1R_F9L; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW   Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..250
FT                   /note="Protein L1"
FT                   /id="PRO_0000448204"
FT   TOPO_DOM        2..183
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..250
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          2..12
FT                   /note="Targeting to MV membrane"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..158
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  27289 MW;  28E1AD7817410A2D CRC64;
     MGAAASIQTT VNTLSERISS KLEQEANASA QTKCDIEIGN FYIRQNHGCN LTVKNMCSAD
     ADAQLDAVLS AATETYSGLT PEQKAYVPAM FTAALNIQTS VNTVVRDFEN YVKQTCNSSA
     VVDNKLKIQN VIIDECYGAP GSPTNLEFIN TGSSKGNCAI KALMQLTTKA TTQIAPRQVA
     GTGVQFYMIV IGVIILAALF MYYAKRMLFT STNDKIKLIL ANKENVHWTT YMDTFFRTSP
     MVIATTDIQN