ID   L1_FOWPN                Reviewed;         243 AA.
AC   P15910; Q9J595;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   02-DEC-2020, entry version 82.
DE   RecName: Full=Protein L1 homolog;
DE   AltName: Full=Virion membrane protein M25;
GN   OrderedLocusNames=FPV128; ORFNames=FP2;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-444;
RX   PubMed=2838574; DOI=10.1099/0022-1317-69-6-1275;
RA   Binns M.M., Tomley F.M., Campbell J., Boursnell M.E.G.;
RT   "Comparison of a conserved region in fowlpox virus and vaccinia virus
RT   genomes and the translocation of the fowlpox virus thymidine kinase gene.";
RL   J. Gen. Virol. 69:1275-1283(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; D00320; BAA00225.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44472.1; -; Genomic_DNA.
DR   PIR; JS0222; WMVZP2.
DR   RefSeq; NP_039091.1; NC_002188.1.
DR   SMR; P15910; -.
DR   GeneID; 1486676; -.
DR   KEGG; vg:1486676; -.
DR   Proteomes; UP000008597; 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   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                   /evidence="ECO:0000250"
FT   CHAIN           2..243
FT                   /note="Protein L1 homolog"
FT                   /id="PRO_0000099615"
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..243
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"
FT   CONFLICT        19
FT                   /note="S -> C (in Ref. 1; BAA00225)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="A -> R (in Ref. 1; BAA00225)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  26519 MW;  36B7CD3E8E3284B8 CRC64;
     MGAAASIQTT VTTINKKISE KLEQTASASA TANCDINIGN IIFKKNKGCN VLVKNMCSAN
     ASAQLDAIVS AVREVYDQLT EQQKAYAPSL LTAALNIQTN VSTITQDFET YIKQKCNSDA
     VINNIINVQS LEVDECSAPP GQIMTFEFIN TGTATGNCAM KSVLDVLTKS SDRVSGNQST
     GNDFSKYLYI IGGIICFLIL LYYAKKLFFM STNDKVKVLL AKKPDVHWTT YIDTYFRSSP
     VLV