ID C4YJE7_CANAW Unreviewed; 850 AA.
AC C4YJE7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN ORFNames=CAWG_03960 {ECO:0000313|EMBL:EEQ45631.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ45631.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ45631.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ45631.1,
RC ECO:0000313|Proteomes:UP000001429};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362055}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362055}.
CC -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000256|ARBA:ARBA00006104,
CC ECO:0000256|RuleBase:RU362055}.
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DR EMBL; CH672350; EEQ45631.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YJE7; -.
DR PaxDb; 5476-C4YJE7; -.
DR VEuPathDB; FungiDB:CAWG_03960; -.
DR HOGENOM; CLU_009031_2_2_1; -.
DR OMA; PRTRFMD; -.
DR Proteomes; UP000001429; Chromosome 2, Supercontig 1.5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR CDD; cd07232; Pat_PLPL; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF66; TRIACYLGLYCEROL LIPASE PTL2; 1.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362055};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362055};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362055}; Membrane {ECO:0000256|RuleBase:RU362055};
KW Transmembrane {ECO:0000256|RuleBase:RU362055};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362055"
FT DOMAIN 394..586
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 46..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..833
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 97444 MW; 8BE2DB5BCED033CC CRC64;
MTERIPLFEE DKDYIDEDHI SEFAKALIWQ DDYDYDANTT ATTDITDTTP INDEVPGIVS
SLPSTNGNNN NKNKDINGTV SDSSSITDED IMNSSYFDKP HLSTNLKSNS TKNDDDDDDD
DLISRPQSGT TDNTSTTSLS SKRPDLITSK SDWFPIGGSR SSSSSKKGSS NYHKKTTPTS
STSTKSTIEI LKNEFRNSST YTLLRWPILI FVFSWIGILG IFYFMIRIYV AVSEYLFTWR
GERKRLRNKL RNSKTYEEWI NNALELDKFL KLDKWSENPK FSYYDYKTIK LTILKLQKLR
HQGKLIELMV ILQGCLKKNF AGIENRQLYS HRYYGTKNLV EEYYQEVVKC LELINQDNDN
DNDDNDDDDN EKIDIEKKWK FFKIVSKNYG KSALCLSGGA CFAYTHFGIA KALLDQNLLP
QIISGTSGGG LIAALLCTRT NEELKKLLVP QLARKITACE DPWYIWIPRF LKTGARFDAI
DWARKSNFFT HGSTTFEEAF QRTGRKLNIS TIPADPHSPV ILCNDITSPH CIIWSTLLAS
SAVPGILNPV VLMMKNPING KVIPFSLGSK WRDGSLRTDI PIEALNTYYN VNFTIVSQVN
PHISLFFFAP KGTVGRPVTS STRKTRSKQQ YASFRGGFIA TALEQLLRLE IKKWLQIIKS
LDLLPHFLQQ DWSNIWLQNF TGTITIWPKN KLSDFWYILS DPTEFRMKEI IEKGEKCMFP
RLLFIKHRAS IENVIEKGKK LTLTKYKQLK SGGVNYDEDV DVDIDDEEEE GEFGGVVSDY
DAQSFQKVVG WSNEDKKLLD ELDNEDEDED EEEDEEEEEV DVDDDDDDDS LSDSFEITTE
HLKQRRNTIF
//
