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GDL64_ARATH
ID   GDL64_ARATH             Reviewed;         368 AA.
AC   O23470; F4JLR0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=GDSL esterase/lipase At4g16230;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase At4g16230;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g16230; ORFNames=dl4155w, FCAALL.318;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   REVIEW.
RX   PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
RA   Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
RT   "GDSL family of serine esterases/lipases.";
RL   Prog. Lipid Res. 43:534-552(2004).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
RA   Ling H.;
RT   "Sequence analysis of GDSL lipase gene family in Arabidopsis thaliana.";
RL   Pak. J. Biol. Sci. 11:763-767(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE83719.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB10402.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB10402.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB78665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78665.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z97340; CAB10402.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161543; CAB78665.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83719.1; ALT_SEQ; Genomic_DNA.
DR   PIR; H71428; H71428.
DR   RefSeq; NP_193358.4; NM_117719.5.
DR   AlphaFoldDB; O23470; -.
DR   SMR; O23470; -.
DR   STRING; 3702.AT4G16230.1; -.
DR   PaxDb; O23470; -.
DR   PeptideAtlas; O23470; -.
DR   PRIDE; O23470; -.
DR   ProteomicsDB; 247102; -.
DR   GeneID; 827317; -.
DR   KEGG; ath:AT4G16230; -.
DR   Araport; AT4G16230; -.
DR   eggNOG; ENOG502QTUA; Eukaryota.
DR   HOGENOM; CLU_015101_0_0_1; -.
DR   InParanoid; O23470; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; O23470; -.
DR   BioCyc; ARA:AT4G16230-MON; -.
DR   PRO; PR:O23470; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O23470; baseline and differential.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..368
FT                   /note="GDSL esterase/lipase At4g16230"
FT                   /id="PRO_0000367405"
FT   ACT_SITE        37
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   368 AA;  40242 MW;  0C39673CD7581397 CRC64;
     MSLLVFLCQI IVLSVLFFSE VCLAGKKIPA NFVFGDSLVD AGNNNYLATL SKANYVPNGI
     DFGSPTGRFT NGRTIVDIVY QALGSDELTP PYLAPTTSGS LILNGVNYAS GGSGILNSTG
     KLFGERINVD AQLDNFATTR QDIISWIGES EAAKLFRSAI FSVTTGSNDL INNYFTPVIS
     TLQRKVVAPE VFVDTMISKF RLQLTRLYQL GARKIVVINI GPIGCIPFER ESDPAAGNNC
     LAEPNEVAQM YNLKLKTLVE ELNKNLQGSR FVYGDVFRIV DDIIQNYSSY GFESEKIPCC
     SLVGKVGGLI PCGPPSKVCM DRSKYVFWDP YHPTEAANII IARRLLSGDT SDIYPINIRQ
     LANLKINA
 
 
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