ID GDL1_CARPA Reviewed; 343 AA.
AC P86276;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GDSL esterase/lipase {ECO:0000250|UniProtKB:Q9FLN0};
DE EC=3.1.1.-;
DE AltName: Full=CpEST {ECO:0000303|PubMed:19555778};
DE AltName: Full=Extracellular lipase {ECO:0000250|UniProtKB:Q9FLN0};
DE Flags: Precursor;
OS Carica papaya (Papaya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18432245; DOI=10.1038/nature06856;
RA Ming R., Hou S., Feng Y., Yu Q., Dionne-Laporte A., Saw J.H., Senin P.,
RA Wang W., Ly B.V., Lewis K.L., Salzberg S.L., Feng L., Jones M.R.,
RA Skelton R.L., Murray J.E., Chen C., Qian W., Shen J., Du P., Eustice M.,
RA Tong E., Tang H., Lyons E., Paull R.E., Michael T.P., Wall K., Rice D.W.,
RA Albert H., Wang M.L., Zhu Y.J., Schatz M., Nagarajan N., Acob R.A.,
RA Guan P., Blas A., Wai C.M., Ackerman C.M., Ren Y., Liu C., Wang J.,
RA Wang J., Na J.K., Shakirov E.V., Haas B., Thimmapuram J., Nelson D.,
RA Wang X., Bowers J.E., Gschwend A.R., Delcher A.L., Singh R., Suzuki J.Y.,
RA Tripathi S., Neupane K., Wei H., Irikura B., Paidi M., Jiang N., Zhang W.,
RA Presting G., Windsor A., Navajas-Perez R., Torres M.J., Feltus F.A.,
RA Porter B., Li Y., Burroughs A.M., Luo M.C., Liu L., Christopher D.A.,
RA Mount S.M., Moore P.H., Sugimura T., Jiang J., Schuler M.A., Friedman V.,
RA Mitchell-Olds T., Shippen D.E., dePamphilis C.W., Palmer J.D., Freeling M.,
RA Paterson A.H., Gonsalves D., Wang L., Alam M.;
RT "The draft genome of the transgenic tropical fruit tree papaya (Carica
RT papaya Linnaeus).";
RL Nature 452:991-996(2008).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 72-92; 125-138; 178-208; 261-309 AND 315-343, FUNCTION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Latex {ECO:0000269|PubMed:19555778};
RX PubMed=19555778; DOI=10.1016/j.bbalip.2009.06.002;
RA Abdelkafi S., Ogata H., Barouh N., Fouquet B., Lebrun R., Pina M.,
RA Scheirlinckx F., Villeneuve P., Carriere F.;
RT "Identification and biochemical characterization of a GDSL-motif
RT carboxylester hydrolase from Carica papaya latex.";
RL Biochim. Biophys. Acta 1791:1048-1056(2009).
CC -!- FUNCTION: Has lipolytic activity towards triacylglycerols, vinyl esters
CC and phospholipid. Of the triacylglycerols, the highest activity is
CC towards tributyrin. {ECO:0000269|PubMed:19555778}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:19555778};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9FLN0}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000255}.
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DR EMBL; ABIM01007310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86276; -.
DR SMR; P86276; -.
DR BioCyc; MetaCyc:MONOMER-16178; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR044552; GLIP1-5/GLL25.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR035669; SGNH_plant_lipase-like.
DR PANTHER; PTHR45966; GDSL-LIKE LIPASE/ACYLHYDROLASE; 1.
DR PANTHER; PTHR45966:SF39; INACTIVE GDSL ESTERASE_LIPASE-LIKE PROTEIN 25; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..343
FT /note="GDSL esterase/lipase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000382238"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT ACT_SITE 310
FT /evidence="ECO:0000250|UniProtKB:Q9FLN0"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 268
FT /note="G -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37991 MW; 2B3F65C0A4A2AF2C CRC64;
MEKPSGQFLG LSLLLLPLLL PISCNAQQLF IFGDSLYDNG NKPFLATDVP STFWPYGLSI
DFPNGRWSDG RIVPDFIAEF LGIPFPPPVL DRSANFSSGV TFATADATIL GTPPQTLTLG
DQVKAFAQIK STWTDAQRQK GIYMFYIGAN DYLNYTNANL NATAQQQEAF VSQVIAKLKD
QLLAIYGLGG RKFAFQNLAP LGCLPIVKQD FKTGNFCLPL ASNLAAQHNQ LLSETLENLS
ETLDGFNYII YDYFNSSLRR MARPNNYGYF TTNLACCGTG SHDAFGCGFK NVHSNLCSYQ
RGYMFFDGRH NAEKTNEAVA HLIFSADPSV VFPMNLRELF VHP
//
