ID   L1_VACCC                Reviewed;         250 AA.
AC   P20540;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-SEP-2021, entry version 87.
DE   RecName: Full=Protein L1;
DE   AltName: Full=Virion membrane protein M25;
GN   ORFNames=L1R;
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).
RN   [3]
RP   MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX   PubMed=9188589; DOI=10.1128/jvi.71.7.5218-5226.1997;
RA   Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E.;
RT   "Identification and analysis of three myristylated vaccinia virus late
RT   proteins.";
RL   J. Virol. 71:5218-5226(1997).
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; M35027; AAA48076.1; -; Genomic_DNA.
DR   PIR; H42512; H42512.
DR   SMR; P20540; -.
DR   ELM; P20540; -.
DR   iPTMnet; P20540; -.
DR   Proteomes; UP000008269; 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   1: Evidence at protein level;
KW   Disulfide bond; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   CHAIN           2..250
FT                   /note="Protein L1"
FT                   /id="PRO_0000099612"
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:0000269|PubMed:9188589"
FT   DISULFID        34..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..158
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         2
FT                   /note="G->A: Complete loss of myristoylation."
FT                   /evidence="ECO:0000269|PubMed:9188589"
SQ   SEQUENCE   250 AA;  27307 MW;  28E1ABB817410A2D 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
     MVIATTDMQN