F13_VACCW
ID F13_VACCW Reviewed; 372 AA.
AC P04021; Q76ZW5;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 23-FEB-2022, entry version 118.
DE RecName: Full=Envelope phospholipase F13;
DE EC=3.1.1.- {ECO:0000269|PubMed:9405398};
DE AltName: Full=37 kDa protein;
DE AltName: Full=Palmitoylated EV membrane protein;
DE AltName: Full=p37K;
GN OrderedLocusNames=VACWR052; ORFNames=F13L;
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=3701927; DOI=10.1128/jvi.58.3.757-764.1986;
RA Hirt P., Hiller G., Wittek R.;
RT "Localization and fine structure of a vaccinia virus gene encoding an
RT envelope antigen.";
RL J. Virol. 58:757-764(1986).
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 FUNCTION, AND PALMITOYLATION AT CYS-185 AND CYS-186.
RX PubMed=8999886; DOI=10.1074/jbc.272.3.1956;
RA Grosenbach D.W., Ulaeto D.O., Hruby D.E.;
RT "Palmitylation of the vaccinia virus 37-kDa major envelope antigen.
RT Identification of a conserved acceptor motif and biological relevance.";
RL J. Biol. Chem. 272:1956-1964(1997).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9405398; DOI=10.1074/jbc.272.51.32042;
RA Baek S.H., Kwak J.Y., Lee S.H., Lee T., Ryu S.H., Uhlinger D.J.,
RA Lambeth J.D.;
RT "Lipase activities of p37, the major envelope protein of vaccinia virus.";
RL J. Biol. Chem. 272:32042-32049(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12706074; DOI=10.1016/s0042-6822(03)00063-1;
RA Husain M., Weisberg A., Moss B.;
RT "Topology of epitope-tagged F13L protein, a major membrane component of
RT extracellular vaccinia virions.";
RL Virology 308:233-242(2003).
RN [6]
RP FUNCTION, AND DOMAIN LATE-BUDDING.
RX PubMed=17475658; DOI=10.1128/jvi.00034-07;
RA Honeychurch K.M., Yang G., Jordan R., Hruby D.E.;
RT "The vaccinia virus F13L YPPL motif is required for efficient release of
RT extracellular enveloped virus.";
RL J. Virol. 81:7310-7315(2007).
RN [7]
RP PALMITOYLATION.
RX PubMed=11017799; DOI=10.1006/viro.2000.0522;
RA Grosenbach D.W., Hansen S.G., Hruby D.E.;
RT "Identification and analysis of vaccinia virus palmitylproteins.";
RL Virology 275:193-206(2000).
RN [8]
RP INTERACTION WITH PROTEIN B5.
RX PubMed=22238237; DOI=10.1099/vir.0.039016-0;
RA Lorenzo M.M., Sanchez-Puig J.M., Blasco R.;
RT "Mutagenesis of the palmitoylation site in vaccinia virus envelope
RT glycoprotein B5.";
RL J. Gen. Virol. 93:733-743(2012).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27466413; DOI=10.1128/jvi.01114-16;
RA Sivan G., Weisberg A.S., Americo J.L., Moss B.;
RT "Retrograde Transport from Early Endosomes to the trans-Golgi Network
RT Enables Membrane Wrapping and Egress of Vaccinia Virus Virions.";
RL J. Virol. 90:8891-8905(2016).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29540596; DOI=10.1128/jvi.02154-17;
RA Bryk P., Brewer M.G., Ward B.M.;
RT "Vaccinia Virus Phospholipase Protein F13 Promotes Rapid Entry of
RT Extracellular Virions into Cells.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Major envelope protein that plays a role in the biogenesis of
CC the viral double membrane and in egress of virus from the host cell
CC (PubMed:8999886, PubMed:17475658, PubMed:27466413). Produces the
CC wrapped form of virus that is required for cell-to-cell spread
CC (PubMed:27466413, PubMed:29540596). Acts as a lipase with broad
CC specificity including phospholipase C, phospholipase A, and
CC triacylglycerol lipase activities (PubMed:9405398).
CC {ECO:0000269|PubMed:17475658, ECO:0000269|PubMed:27466413,
CC ECO:0000269|PubMed:29540596, ECO:0000269|PubMed:8999886,
CC ECO:0000269|PubMed:9405398}.
CC -!- SUBUNIT: Interacts with protein B5. {ECO:0000269|PubMed:22238237}.
CC -!- INTERACTION:
CC P04021; P68617: VACWR156; NbExp=2; IntAct=EBI-7736497, EBI-7133633;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:12706074};
CC Lipid-anchor {ECO:0000269|PubMed:12706074}. Host Golgi apparatus, host
CC trans-Golgi network {ECO:0000269|PubMed:27466413,
CC ECO:0000269|PubMed:29540596}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12706074}; Lipid-anchor
CC {ECO:0000269|PubMed:12706074}; Cytoplasmic side
CC {ECO:0000269|PubMed:12706074}. Note=Component of the inner side of the
CC enveloped virion (EV) membrane. F13 is associated post-translationally
CC with membranes.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. F13 contains one L domain: a YPPL motif,
CC which might interact with PDCD6IP/AIP1. {ECO:0000269|PubMed:17475658}.
CC -!- PTM: Palmitoylated. Attachment of the palmitate moiety is essential for
CC correct intracellular targeting and protein function.
CC {ECO:0000269|PubMed:11017799, ECO:0000269|PubMed:8999886}.
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DR EMBL; M12882; AAA48235.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89331.1; -; Genomic_DNA.
DR PIR; A03869; WMVZ37.
DR RefSeq; YP_232934.1; NC_006998.1.
DR SMR; P04021; -.
DR IntAct; P04021; 2.
DR MINT; P04021; -.
DR ChEMBL; CHEMBL4296170; -.
DR SwissPalm; P04021; -.
DR DNASU; 3707509; -.
DR GeneID; 3707509; -.
DR KEGG; vg:3707509; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0036338; C:viral membrane; IDA:UniProtKB.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR InterPro; IPR032803; PLDc_3.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13918; PLDc_3; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 1.
PE 1: Evidence at protein level;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Hydrolase; Late protein; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral envelope protein;
KW Viral release from host cell; Virion.
FT CHAIN 1..372
FT /note="Envelope phospholipase F13"
FT /id="PRO_0000099198"
FT DOMAIN 307..334
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT MOTIF 153..156
FT /note="YPPL"
FT LIPID 185
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8999886"
FT LIPID 186
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8999886"
SQ SEQUENCE 372 AA; 41796 MW; 27AE138A382EE934 CRC64;
MWPFASVPAG AKCRLVETLP ENMDFRSDHL TTFECFNEII TLAKKYIYIA SFCCNPLSTT
RGALIFDKLK EASEKGIKII VLLDERGKRN LGELQSHCPD INFITVNIDK KNNVGLLLGC
FWVSDDERCY VGNASFTGGS IHTIKTLGVY SDYPPLATDL RRRFDTFKAF NSAKNSWLNL
CSAACCLPVS TAYHIKNPIG GVFFTDSPEH LLGYSRDLDT DVVIDKLKSA KTSIDIEHLA
IVPTTRVDGN SYYWPDIYNS IIEAAINRGV KIRLLVGNWD KNDVYSMATA RSLDALCVQN
DLSVKVFTIQ NNTKLLIVDD EYVHITSANF DGTHYQNHGF VSFNSIDKQL VSEAKKIFER
DWVSSHSKSL KI
