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PLPL_CANAL
ID   PLPL_CANAL              Reviewed;         852 AA.
AC   Q5AM72; A0A1D8PGG8; Q5ALS2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein CaO19.1504;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=CAALFM_C201920CA; ORFNames=CaO19.1504, CaO19.9080;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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DR   EMBL; CP017624; AOW27235.1; -; Genomic_DNA.
DR   RefSeq; XP_722550.2; XM_717457.2.
DR   AlphaFoldDB; Q5AM72; -.
DR   STRING; 237561.Q5AM72; -.
DR   PRIDE; Q5AM72; -.
DR   GeneID; 3635792; -.
DR   KEGG; cal:CAALFM_C201920CA; -.
DR   CGD; CAL0000177360; orf19.9080.
DR   VEuPathDB; FungiDB:C2_01920C_A; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   InParanoid; Q5AM72; -.
DR   OrthoDB; 425613at2759; -.
DR   PRO; PR:Q5AM72; -.
DR   Proteomes; UP000000559; Chromosome 2.
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..852
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   CaO19.1504"
FT                   /id="PRO_0000295554"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          396..588
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          41..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           427..431
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        41..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..835
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        575
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   852 AA;  97426 MW;  AC749BF5B2436DE5 CRC64;
     MTERIPLFEE DKDYIDEDHI SEFAKALVWQ DDYDYDANTT ATTDITTTPI NDEVPGIVSS
     LPSTNGNNKN KNKDINGTVS DSSSITDEDI MNSSYFDKPH SSTNLKSNST KNDDDDDDDD
     DDLISRPQSG TTDNTSTTSL SSKRPDLITS KSDWFPIGGS RSSSSSKKGS SNYHKKTTPT
     SSTSTKSTIE ILKNEFRNSS TYTLLRWPIL IFVFSWIGIL GIFYFMIRIY VAVSEYLFTW
     RGERKRLRNK LRNSKTYEEW INNALELDKF LKLDKWSENP KFSYYDYKTI KLTILKLQKL
     RHQGKLIELM VILQGCLKKN FAGIENRQLY SHRYYGTKNL VEEYYQEVVK CLELINQDNN
     NGDDNDDDDN DNEKIDIEKK WKFFKIVSKN YGKSALCLSG GACFAYTHFG IAKALLDQNL
     LPQIISGTSG GGLIAALLCT RTNEELKKLL VPQLARKITA CEDPWYIWIP RFLKTGARFD
     AIDWARKSNF FTHGSTTFEE AFQRTGRKLN ISTIPADPHS PVILCNDITS PHCIIWSTLL
     ASSAVPGILN PVVLMMKNPI NGKVIPFSLG SKWRDGSLRT DIPIEALNTY YNVNFTIVSQ
     VNPHISLFFF APKGTVGRPV TSSTRKTRSK QQYASFRGGF IATALEQLLR LEIKKWLQII
     KSLDLLPHFL QQDWSNIWLQ NFTGTITIWP KNKLSDFWYI LSDPTEFRMK EIIEKGEKCM
     FPRLLFIKHR ASIENVIEKG KKLTLTKYKQ LKSGGVDCDE DVDVDVDIDD EEEEGESGGV
     VSDYDAQSFQ KVVGWSNEDK KLLDELDNED EEEDEEEEEV DVDDDDDDDD DSLSDSFEIT
     TEHLKQRRNT IF
 
 
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