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PLPL_DEBHA
ID   PLPL_DEBHA              Reviewed;         788 AA.
AC   Q6BXC8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein DEHA2B04136g;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=DEHA2B04136g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382134; CAG85135.2; -; Genomic_DNA.
DR   RefSeq; XP_457141.2; XM_457141.1.
DR   AlphaFoldDB; Q6BXC8; -.
DR   STRING; 4959.XP_457141.2; -.
DR   EnsemblFungi; CAG85135; CAG85135; DEHA2B04136g.
DR   GeneID; 2913031; -.
DR   KEGG; dha:DEHA2B04136g; -.
DR   VEuPathDB; FungiDB:DEHA2B04136g; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   InParanoid; Q6BXC8; -.
DR   OMA; DMNKWLR; -.
DR   OrthoDB; 425613at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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..788
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   DEHA2B04136g"
FT                   /id="PRO_0000295558"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          311..503
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          662..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           342..346
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        662..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..702
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..745
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        344
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        490
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   788 AA;  90454 MW;  7FB35C3D4BE23BB0 CRC64;
     MEKTNRKKLF DEDIDYVNED HISSFAKALA WEEQYEILEN EKSGASSDKE SQDAATIQKE
     TEELDDLGAD ELSTALNGMH KPDLISSKSD WWPINTSKSI PKTKIRKKSK KSSVNEGHSK
     ITNEFRSSAS YTMLRWPILI FISCWISLLC FMYIIVRAYV ALSEYFLTWV GKRKELRNKL
     RASQNYEEWV QNALELDRFL NLDKWSENPK FSYYDSKTVE LTISKLASLR EEGRDNDLMV
     ILQGCIKKNF AGIENRQLYS HRYYGTKYLV EKYIDEVIVC IDKVIESQQI SFNDKRRFFR
     TVSKNYGKTA LCLSGGACFT YTHFGIVKAL LDNDLLPSII SGTSGGGLIA ALSCTRTDDE
     LKKLLVPELA RKITACEDPW YVWIPRWWRT GARFDSLEWA RKANFFTRGS TTFYESFKRT
     GRRLNISTVP SNPHSPVILC NNITSPNCII WSSLLASSAV PGILNPVVLL MKDLKTDRVV
     PFSLGSKWRD GSLRTDIPID ALNTYYNVNF SIVSQVNPHI SLFFFAPKGT VGRPVAIPRR
     KTHKEKYASL RGGFIATALE QLFKLEITKW LQMIKSLDLL PHLLEQDWSN IWLQRFSGSI
     TIWPRNRLKD FWYILSDPTE ERLAEMLSKG ERAMFPRILF VKHRLSIEKA IEKGRKQTKL
     SANFNTLTSS DSGRTELSPE AAELQVEPAM FDDDEYDSDS SDDEVLSPNN KKHIDKFGTP
     NTEDGDDDED AYEYYDDDDY GLSTEDEANQ ENTGNSQGEE NDTGSRFLKS FFRAGSRDSK
     LHRRNTVF
 
 
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