ID   PLPL_COCIM              Reviewed;         730 AA.
AC   Q1DXR6; J3KEZ1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein CIMG_04897;
DE            EC=3.1.1.-;
GN   ORFNames=CIMG_04897;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PLPL 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; GG704914; EAS33873.3; -; Genomic_DNA.
DR   RefSeq; XP_001245456.1; XM_001245455.2.
DR   AlphaFoldDB; Q1DXR6; -.
DR   STRING; 246410.Q1DXR6; -.
DR   EnsemblFungi; EAS33873; EAS33873; CIMG_04897.
DR   GeneID; 4564555; -.
DR   KEGG; cim:CIMG_04897; -.
DR   VEuPathDB; FungiDB:CIMG_04897; -.
DR   InParanoid; Q1DXR6; -.
DR   OMA; DMNKWLR; -.
DR   OrthoDB; 425613at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..730
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   CIMG_04897"
FT                   /id="PRO_0000295556"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          281..472
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           312..316
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        11..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        314
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        459
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   730 AA;  83048 MW;  3DC254C23DEA6601 CRC64;
     MTANSSRRRL QMKSPRTDGD EKEEDYGLPD FHTRFINDED LEEFEKALNA PQALSLIAIN
     DWRPIHRRVR KPGKLPKVPQ RTKDETREGV VYTLLKWPFL LFVLSWIVFL GALYILTRLY
     ISLYEHFFAW TGQRQRLRRA LHSTVDYQHW KNAAKELDEY LGNDAWKERP QYAYYDNTTV
     MTVVSQLRQL RAQTEAGGIN GKAAAEELCT LLEGCIKTNF AGIENPRLYS ETYYGTKDLV
     QEFIEEAHTS LRLVLTSQQL SDERKQGLFR HLDTNFGRTV LCLSGGATLA YYHFGVIKAL
     LDNDVLPDII SGTSGGALVA ALVATRTDEE LKKLLVPELA HKIKACQDGI TTWAVRCWRT
     GARFDVMQWA EQCSWFCRGS TTFREAYERT GRVLNVSCVP SDPHSPTILA NYLTSPNCVI
     WSAVLASAAV PGILNPVVLM MKKPDGTLAP YSFGHKWKDG SLRTDIPLKA LDVHFNASFS
     IVSQVNPHIS LFFFSSRGSV GRPVTHRKGR GWRGGFLGSA LEQYIKLDLN KWLKVMRHLE
     LLPRPLGQDW SEIWLQRFSG TVTIWPKSVL SDLYYILSDP SVQRLARMLH EGQQCTFPKI
     KFISNRMKIE RVIAEGLMKD PEWAGSGRWN NVPFRSRTDQ TLPLEENAQQ RSASMLADTM
     SHLRDTGHFR EAPTSHPTGS PVRPTSGRRN SLMEEIRRQS AVFFDDTDDT MPSDDEKFPY
     QGQSSGTKIG