L1_VACCA
ID L1_VACCA Reviewed; 250 AA.
AC Q76RD2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 07-APR-2021, entry version 65.
DE RecName: Full=Protein L1;
DE AltName: Full=Virion membrane protein M25;
GN OrderedLocusNames=MVA080R, ACAM3000_MVA_080; ORFNames=L1R;
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 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 late in 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; U94848; AAB96498.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10478.1; -; Genomic_DNA.
DR SMR; Q76RD2; -.
DR PRIDE; Q76RD2; -.
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: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_0000099611"
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; 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