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GDL1_CARPA
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   03-AUG-2022, entry version 26.
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:MON-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; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
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
 
 
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