ID   F13_VACCI               Reviewed;         372 AA.
AC   P26653;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   23-FEB-2022, entry version 89.
DE   RecName: Full=Envelope phospholipase F13;
DE            EC=3.1.1.-;
DE   AltName: Full=37 kDa protein;
DE   AltName: Full=Envelope protein F13;
DE   AltName: Full=Palmitoylated EV membrane protein;
DE   AltName: Full=p37K;
GN   ORFNames=F13L;
OS   Vaccinia virus (strain IHD-J) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10251;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ASP-280.
RX   PubMed=2041074; DOI=10.1128/jvi.65.7.3435-3442.1991;
RA   Schmutz C., Payne L.G., Gubser J., Wittek R.;
RT   "A mutation in the gene encoding the vaccinia virus 37,000-M(r) protein
RT   confers resistance to an inhibitor of virus envelopment and release.";
RL   J. Virol. 65:3435-3442(1991).
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       Produces the wrapped form of virus that is required for cell-to-cell
CC       spread. Acts as a lipase with broad specificity including phospholipase
CC       C, phospholipase A, and triacylglycerol lipase activities.
CC       {ECO:0000250|UniProtKB:P04021}.
CC   -!- SUBUNIT: Interacts with protein B5. {ECO:0000250|UniProtKB:P04021}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P04021};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P04021}. Host Golgi apparatus, host
CC       trans-Golgi network {ECO:0000250|UniProtKB:P04021}. Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P04021}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P04021}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P04021}. Note=Component of the inner side of the
CC       enveloped virion (EV) membrane. F13 is associated post-translationally
CC       with membranes. {ECO:0000250|UniProtKB:P04021}.
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 LYPX(n)L motif,
CC       which might interact with PDCD6IP/AIP1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Palmitoylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The mutation in position 280 confers resistance to an
CC       inhibitor of virus envelopment and release.
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DR   EMBL; M60412; AAA48236.1; -; Genomic_DNA.
DR   EMBL; M60413; AAA48237.1; -; Genomic_DNA.
DR   PIR; A40339; WMVZID.
DR   SMR; P26653; -.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
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; Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral envelope protein; Viral release from host cell; Virion.
FT   CHAIN           1..372
FT                   /note="Envelope phospholipase F13"
FT                   /id="PRO_0000099196"
FT   DOMAIN          307..334
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   MOTIF           153..156
FT                   /note="YPPL"
FT   MUTAGEN         280
FT                   /note="D->Y: Resistance to IMCBH."
FT                   /evidence="ECO:0000269|PubMed:2041074"
SQ   SEQUENCE   372 AA;  41806 MW;  A2757EA5C60116A2 CRC64;
     MWPFAPVPAG 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