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 22-FEB-2023, entry version 82.
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 EnsemblFungi; C2_01920C_A-T; C2_01920C_A-T-p1; C2_01920C_A.
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; 154387at2759; -.
DR PRO; PR:Q5AM72; -.
DR Proteomes; UP000000559; Chromosome 2.
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-KW.
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; 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
//
