L1_VACCW
ID L1_VACCW Reviewed; 250 AA.
AC P07612; Q76ZT7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein L1;
DE AltName: Full=Virion membrane protein M25;
GN OrderedLocusNames=VACWR088; ORFNames=L1R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2987815; DOI=10.1093/nar/13.3.985;
RA Plucienniczak A., Schroeder E., Zettlmeissl G., Streeck R.E.;
RT "Nucleotide sequence of a cluster of early and late genes in a conserved
RT segment of the vaccinia virus genome.";
RL Nucleic Acids Res. 13:985-998(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=2243383; DOI=10.1128/jvi.64.12.5988-5996.1990;
RA Franke C.A., Wilson E.M., Hruby D.E.;
RT "Use of a cell-free system to identify the vaccinia virus L1R gene product
RT as the major late myristylated virion protein M25.";
RL J. Virol. 64:5988-5996(1990).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8463289; DOI=10.1016/s0021-9258(18)53215-4;
RA Ravanello M.P., Franke C.A., Hruby D.E.;
RT "An NH2-terminal peptide from the vaccinia virus L1R protein directs the
RT myristylation and virion envelope localization of a heterologous fusion
RT protein.";
RL J. Biol. Chem. 268:7585-7593(1993).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-2.
RX PubMed=8083978; DOI=10.1128/jvi.68.10.6401-6410.1994;
RA Ravanello M.P., Hruby D.E.;
RT "Conditional lethal expression of the vaccinia virus L1R myristylated
RT protein reveals a role in virion assembly.";
RL J. Virol. 68:6401-6410(1994).
RN [6]
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).
RN [7]
RP INTERACTION WITH G4.
RX PubMed=11983854; DOI=10.1073/pnas.062163799;
RA Senkevich T.G., White C.L., Koonin E.V., Moss B.;
RT "Complete pathway for protein disulfide bond formation encoded by
RT poxviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002).
RN [8]
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-34; CYS-49; CYS-57; CYS-116;
RP CYS-136 AND CYS-158.
RX PubMed=16336686; DOI=10.1186/1743-422x-2-91;
RA Blouch R.E., Byrd C.M., Hruby D.E.;
RT "Importance of disulphide bonds for vaccinia virus L1R protein function.";
RL Virol. J. 2:91-91(2005).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=18596103; DOI=10.1128/jvi.00852-08;
RA Bisht H., Weisberg A.S., Moss B.;
RT "Vaccinia virus l1 protein is required for cell entry and membrane
RT fusion.";
RL J. Virol. 82:8687-8694(2008).
RN [10]
RP FUNCTION.
RX PubMed=19162289; DOI=10.1016/j.virol.2008.12.019;
RA Foo C.H., Lou H., Whitbeck J.C., Ponce-de-Leon M., Atanasiu D.,
RA Eisenberg R.J., Cohen G.H.;
RT "Vaccinia virus L1 binds to cell surfaces and blocks virus entry
RT independently of glycosaminoglycans.";
RL Virology 385:368-382(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 1-185.
RX PubMed=15761054; DOI=10.1073/pnas.0501103102;
RA Su H.P., Garman S.C., Allison T.J., Fogg C., Moss B., Garboczi D.N.;
RT "The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent
RT neutralizing antibodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4240-4245(2005).
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.
CC {ECO:0000269|PubMed:18596103, ECO:0000269|PubMed:19162289,
CC ECO:0000269|PubMed:8083978}.
CC -!- SUBUNIT: Interacts with G4; this interaction involves formation of a
CC transient disulfide-bonded intermediate, allowing disulfide bond
CC transfer. {ECO:0000269|PubMed:11983854}.
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).
CC {ECO:0000269|PubMed:9188589}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:18596103}.
CC -!- PTM: Myristoylated. {ECO:0000269|PubMed:2243383,
CC ECO:0000269|PubMed:9188589}.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae L1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X01978; CAA26010.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89367.1; -; Genomic_DNA.
DR PIR; B23092; QQVZF2.
DR RefSeq; YP_232970.1; NC_006998.1.
DR PDB; 1YPY; X-ray; 1.51 A; A/B=2-185.
DR PDB; 2I9L; X-ray; 3.10 A; I/J/K/L=2-185.
DR PDB; 4U6H; X-ray; 3.10 A; E/J=1-184.
DR PDBsum; 1YPY; -.
DR PDBsum; 2I9L; -.
DR PDBsum; 4U6H; -.
DR SMR; P07612; -.
DR TCDB; 1.G.11.1.1; the poxvirus cell entry protein complex (pep-c) family.
DR iPTMnet; P07612; -.
DR ABCD; P07612; 5 sequenced antibodies.
DR DNASU; 3707544; -.
DR GeneID; 3707544; -.
DR KEGG; vg:3707544; -.
DR EvolutionaryTrace; P07612; -.
DR Proteomes; UP000000344; 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 3D-structure; Disulfide bond; Host-virus interaction; Lipoprotein;
KW Membrane; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; 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_0000099613"
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 LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:2243383,
FT ECO:0000269|PubMed:9188589"
FT DISULFID 34..57
FT /evidence="ECO:0000269|PubMed:16336686"
FT DISULFID 49..136
FT /evidence="ECO:0000269|PubMed:16336686"
FT DISULFID 116..158
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 2
FT /note="G->A: Complete loss of myristoylation. Blocks the
FT maturation of virus."
FT /evidence="ECO:0000269|PubMed:8083978,
FT ECO:0000269|PubMed:9188589"
FT MUTAGEN 34
FT /note="C->S: 75% loss in virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 49
FT /note="C->S: 75% loss in virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 57
FT /note="C->S: Almost no effect on virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 116
FT /note="C->S: 50% loss in virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 136
FT /note="C->S: 70% loss in virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT MUTAGEN 158
FT /note="C->S: 60% loss in virus production."
FT /evidence="ECO:0000269|PubMed:16336686"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:1YPY"
FT STRAND 35..55
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1YPY"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1YPY"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1YPY"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1YPY"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2I9L"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1YPY"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:1YPY"
SQ SEQUENCE 250 AA; 27279 MW; 28FE89850863372D CRC64;
MGAAASIQTT VNTLSERISS KLEQEANASA QTKCDIEIGN FYIRQNHGCN LTVKNMCSAD
ADAQLDAVLS AATETYSGLT PEQKAYVPAM FTAALNIQTS VNTVVRDFEN YVKQTCNSSA
VVDNKLKIQN VIIDECYGAP GSPTNLEFIN TGSSKGNCAI KALMQLTTKA TTQIAPKQVA
GTGVQFYMIV IGVIILAALF MYYAKRMLFT STNDKIKLIL ANKENVHWTT YMDTFFRTSP
MVIATTDMQN
