ID   VLIP_GAHVM              Reviewed;         756 AA.
AC   Q77MS9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Virulence factor MDV010;
DE   AltName: Full=Viral lipase homolog;
DE            Short=vLIP;
DE   Flags: Precursor;
GN   Name=MDV010;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=15890938; DOI=10.1128/jvi.79.11.6984-6996.2005;
RA   Kamil J.P., Tischer B.K., Trapp S., Nair V.K., Osterrieder N., Kung H.J.;
RT   "vLIP, a viral lipase homologue, is a virulence factor of Marek's disease
RT   virus.";
RL   J. Virol. 79:6984-6996(2005).
CC   -!- FUNCTION: May play a role in host immune modulation since the protein
CC       is secreted and provides an advantage for growth in vivo while it is
CC       completely dispensable in cell culture. {ECO:0000269|PubMed:15890938}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: The recombinant protein experimentally lacks lipase
CC       activity. Additionally, it possesses an uncharged asparagine instead of
CC       an aspartic acid residue at the catalytic-triad acid position found in
CC       conventional cellular lipases.
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DR   EMBL; AF243438; AAG14190.1; -; Genomic_DNA.
DR   RefSeq; YP_001033926.1; NC_002229.3.
DR   GeneID; 4811470; -.
DR   KEGG; vg:4811470; -.
DR   Proteomes; UP000008072; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   Pfam; PF00151; Lipase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..756
FT                   /note="Virulence factor MDV010"
FT                   /id="PRO_0000406514"
FT   REGION          96..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        660
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        684
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        715
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        744
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   756 AA;  84802 MW;  D107C06DCC296FD4 CRC64;
     MPSKSIADHH AGYGVALAIV ALLLIHGTAL VMIFSDIKVG SQPQDLKDQL SYPSNYDAYT
     SHISGADHGH SEMWTDINPP SRKPLHGDSL DIKTNEEHIT LSSPRTSTKT TNENGHEKDS
     KDIKFSFSTN RHPISVSPTT DIVSIAVSHN NPMGGDTWQV SRNGPNTVHV PIYGKPILRL
     NGEELSTQIA HMSMWDELAG SFKTFAATAE SFHMITTTHL FNKTLHKDVF FVVHGWHGIT
     NDTHIFLSAV RLLTRMMPTS CIIYLSWESQ GAIGTAADAI LLARRVNITQ FLSAMPSQLR
     IHCMGHSLGS YVCGSICRQY HSLMSGICKG ILGINPYEVL FSAPDLYARM HVDTIRLDAE
     YVAIFATTSQ YLSTSDSDAD EYIIVNDAVF MNSVCANPYE WNIHLCTTGY GELKSCERFG
     AANVTTSPGV VEDGSQICLR MLPIIAVLQS LDLKSSYPLL RIAPPDASNE VTHLPSIWNI
     YVVGKDYRYS TYAKNDSLWY SSAICAGDTG FSIPSVFTVF APPSISLRVR AAVQQSSTIY
     KNITIYSAFL KNTSRYYPTV TLETLGPILS AYAWRGRMHN SSYYPLPLPE QEIMEYKCTH
     IDRTYTCIPT DLIYATTVWR QIFSMGHIFP VYPSNNCLPY RPTNAIIWRR PVLEIGVWNN
     ITASFQRNKQ LMALTFENHN TATNTTLLTF HDVCRESKIR SVVYFEYDWL ETSMNITVLI
     PGLYTLRWFF PFEIIEMPVR VSYNNSFAQA LTTSRV