ID   F13_VACCC               Reviewed;         372 AA.
AC   P20638;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   23-FEB-2022, entry version 106.
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 Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   COMPLETE GENOME.
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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 YPPL motif,
CC       which might interact with PDCD6IP/AIP1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Palmitoylated. {ECO:0000250}.
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DR   EMBL; M35027; AAA48031.1; -; Genomic_DNA.
DR   PIR; I42507; WMVZCN.
DR   SMR; P20638; -.
DR   Proteomes; UP000008269; Genome.
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   3: Inferred from homology;
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_0000099195"
FT   DOMAIN          307..334
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   MOTIF           153..156
FT                   /note="YPPL"
SQ   SEQUENCE   372 AA;  41824 MW;  B488783DC82EFB83 CRC64;
     MWPFASVPAG AKCRLVETLP ENMDFRSDHL TTFECFNEII TLAKKYIYIA SFCCNPLSTT
     RGALIFDKLK EASEKGIKII VLLDERGKRN LGELQSHCPD INFITVNIDK KNNVGLLLGC
     FWVSDDERCY VGNASFTGGS IHTIKTLGVY SDYPPLATDL RRRFDTFKAF NSAKNSWLNL
     CSAACCLPVS TAYHIKNPIG GVFFTDSPEH LLGYSRDLDT DVVIDKLRSA KTSIDIEHLA
     IVPTTRVDGN SYYWPDIYNS IIEAAINRGV KIRLLVGNWD KNDVYSMATA RSLDALCVQN
     DLSVKVFTIQ NNTKLLIVDD EYVHITSANF DGTHYQNHGF VSFNSIDKQL VSEAKKIFER
     DWVSSHSKSL KI