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GDL14_ARATH
ID   GDL14_ARATH             Reviewed;         364 AA.
AC   Q9C7N5; Q8L9H1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=GDSL esterase/lipase At1g29660 {ECO:0000303|PubMed:18819574};
DE            EC=3.1.1.- {ECO:0000305};
DE   AltName: Full=Apoplastic EDS1-dependent protein 3 {ECO:0000303|PubMed:24755512};
DE   AltName: Full=Extracellular lipase At1g29660;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g29660 {ECO:0000312|Araport:AT1G29660};
GN   ORFNames=F15D2.21 {ECO:0000312|EMBL:AAG51756.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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).
RN   [7]
RP   INDUCTION BY DROUGHT.
RX   PubMed=19901554; DOI=10.4161/psb.4.11.10103;
RA   Ding Y., Lapko H., Ndamukong I., Xia Y., Al-Abdallat A., Lalithambika S.,
RA   Sadder M., Saleh A., Fromm M., Riethoven J.-J., Lu G., Avramova Z.;
RT   "The Arabidopsis chromatin modifier ATX1, the myotubularin-like AtMTM and
RT   the response to drought.";
RL   Plant Signal. Behav. 4:1049-1058(2009).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=22639651; DOI=10.3389/fpls.2012.00053;
RA   Benning U.F., Tamot B., Guelette B.S., Hoffmann-Benning S.;
RT   "New aspects of Phloem-mediated long-distance lipid signaling in plants.";
RL   Front. Plant Sci. 3:53-53(2012).
RN   [9]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   INDUCTION BY PATHOGEN.
RX   PubMed=24755512; DOI=10.1104/pp.114.239665;
RA   Breitenbach H.H., Wenig M., Wittek F., Jorda L., Maldonado-Alconada A.M.,
RA   Sarioglu H., Colby T., Knappe C., Bichlmeier M., Pabst E., Mackey D.,
RA   Parker J.E., Vlot A.C.;
RT   "Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED
RT   DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in
RT   Arabidopsis systemic acquired resistance.";
RL   Plant Physiol. 165:791-809(2014).
CC   -!- FUNCTION: Involved in EDS1-dependent systemic acquired resistance,
CC       maybe in phloem-mediated long-distance signaling.
CC       {ECO:0000269|PubMed:24755512}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:24755512}.
CC   -!- TISSUE SPECIFICITY: Found in phloem exudates.
CC       {ECO:0000269|PubMed:22639651}.
CC   -!- INDUCTION: Down-regulated by drought (PubMed:19901554). Down-regulated
CC       by virulent or avirulent pathogen infection (PubMed:24755512).
CC       {ECO:0000269|PubMed:19901554, ECO:0000269|PubMed:24755512}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AC068667; AAG51756.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31115.1; -; Genomic_DNA.
DR   EMBL; AY050413; AAK91429.1; -; mRNA.
DR   EMBL; AY133560; AAM91390.1; -; mRNA.
DR   EMBL; AY088437; AAM65973.1; -; mRNA.
DR   PIR; H86419; H86419.
DR   RefSeq; NP_174259.1; NM_102706.3.
DR   AlphaFoldDB; Q9C7N5; -.
DR   SMR; Q9C7N5; -.
DR   STRING; 3702.AT1G29660.1; -.
DR   PaxDb; Q9C7N5; -.
DR   PRIDE; Q9C7N5; -.
DR   ProteomicsDB; 247084; -.
DR   EnsemblPlants; AT1G29660.1; AT1G29660.1; AT1G29660.
DR   GeneID; 839843; -.
DR   Gramene; AT1G29660.1; AT1G29660.1; AT1G29660.
DR   KEGG; ath:AT1G29660; -.
DR   Araport; AT1G29660; -.
DR   TAIR; locus:2013658; AT1G29660.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_015101_0_0_1; -.
DR   InParanoid; Q9C7N5; -.
DR   OMA; PPCLNRD; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9C7N5; -.
DR   BioCyc; ARA:AT1G29660-MON; -.
DR   PRO; PR:Q9C7N5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C7N5; baseline and differential.
DR   Genevisible; Q9C7N5; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
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   GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
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   Apoplast; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..364
FT                   /note="GDSL esterase/lipase At1g29660"
FT                   /id="PRO_0000367356"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT   ACT_SITE        328
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT   ACT_SITE        331
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q09LX1"
FT   CONFLICT        235
FT                   /note="Q -> E (in Ref. 4; AAM65973)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="A -> T (in Ref. 4; AAM65973)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  40142 MW;  1224397085D771A5 CRC64;
     MESYLRKWCL VSVWVLLLGL GFKVKAEPQV PCYFIFGDSL VDNGNNNRLR SIARADYFPY
     GIDFGGPTGR FSNGRTTVDV LTELLGFDNY IPAYSTVSGQ EILQGVNYAS AAAGIREETG
     AQLGQRITFS GQVENYKNTV AQVVEILGDE YTAADYLKRC IYSVGMGSND YLNNYFMPQF
     YSTSRQYTPE QYADDLISRY RDQLNALYNY GARKFALVGI GAIGCSPNAL AQGSQDGTTC
     VERINSANRI FNNRLISMVQ QLNNAHSDAS FTYINAYGAF QDIIANPSAY GFTNTNTACC
     GIGRNGGQLT CLPGEPPCLN RDEYVFWDAF HPSAAANTAI AKRSYNAQRS SDVYPIDISQ
     LAQL
 
 
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