GDL19_ARATH
ID GDL19_ARATH Reviewed; 386 AA.
AC Q8W4H8; Q8LGI1; Q9SYF7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Inactive GDSL esterase/lipase-like protein 23;
DE AltName: Full=GDSL-like lipase 23;
DE AltName: Full=Probable myrosinase-associated protein GLL23;
DE Flags: Precursor;
GN Name=GLL23; OrderedLocusNames=At1g54010; ORFNames=F15I1.9;
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 FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND IDENTIFICATION
RP IN THE PYK10 COMPLEX.
RX PubMed=18467340; DOI=10.1093/pcp/pcn075;
RA Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.;
RT "Antagonistic jacalin-related lectins regulate the size of ER body-type
RT beta-glucosidase complexes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:969-980(2008).
RN [8]
RP INTERACTION WITH MVP1.
RX PubMed=23155454; DOI=10.1371/journal.pone.0049103;
RA Nakano R.T., Matsushima R., Nagano A.J., Fukao Y., Fujiwara M., Kondo M.,
RA Nishimura M., Hara-Nishimura I.;
RT "ERMO3/MVP1/GOLD36 is involved in a cell type-specific mechanism for
RT maintaining ER morphology in Arabidopsis thaliana.";
RL PLoS ONE 7:E49103-E49103(2012).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=24330158; DOI=10.1111/tpj.12408;
RA Jancowski S., Catching A., Pighin J., Kudo T., Foissner I., Wasteneys G.O.;
RT "Trafficking of the myrosinase-associated protein GLL23 requires
RT NUC/MVP1/GOLD36/ERMO3 and the p24 protein CYB.";
RL Plant J. 77:497-510(2014).
CC -!- FUNCTION: Involved in the control of the PYK10 complex size and
CC possibly substrate specificity. May be exported from the endoplasmic
CC reticulum upon interaction with MVP1. {ECO:0000269|PubMed:18467340,
CC ECO:0000269|PubMed:24330158}.
CC -!- SUBUNIT: Part of the PYK10 complex. Interacts with MVP1.
CC {ECO:0000269|PubMed:18467340, ECO:0000269|PubMed:23155454}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:24330158}. Note=Only transiently resident in a
CC specific ER subcompartment and is either post-translationally modified
CC prior to export or targeted for degradation.
CC -!- TISSUE SPECIFICITY: Expressed mainly in roots.
CC {ECO:0000269|PubMed:18467340}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 10-day-old seedlings.
CC {ECO:0000269|PubMed:24330158}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site 'GDSL' motif. Its enzyme
CC activity is therefore unsure. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM67268.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006577; AAD25773.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33034.1; -; Genomic_DNA.
DR EMBL; AY062552; AAL32630.1; -; mRNA.
DR EMBL; AY093330; AAM13329.1; -; mRNA.
DR EMBL; AY084258; AAM67268.1; ALT_INIT; mRNA.
DR PIR; F96580; F96580.
DR RefSeq; NP_564647.1; NM_104278.4.
DR AlphaFoldDB; Q8W4H8; -.
DR SMR; Q8W4H8; -.
DR BioGRID; 27064; 6.
DR IntAct; Q8W4H8; 2.
DR STRING; 3702.AT1G54010.1; -.
DR MetOSite; Q8W4H8; -.
DR PaxDb; Q8W4H8; -.
DR PRIDE; Q8W4H8; -.
DR ProteomicsDB; 221919; -.
DR EnsemblPlants; AT1G54010.1; AT1G54010.1; AT1G54010.
DR GeneID; 841839; -.
DR Gramene; AT1G54010.1; AT1G54010.1; AT1G54010.
DR KEGG; ath:AT1G54010; -.
DR Araport; AT1G54010; -.
DR TAIR; locus:2014390; AT1G54010.
DR eggNOG; ENOG502S4IX; Eukaryota.
DR HOGENOM; CLU_015101_7_0_1; -.
DR InParanoid; Q8W4H8; -.
DR OMA; NVHSRLC; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q8W4H8; -.
DR BioCyc; ARA:AT1G54010-MON; -.
DR PRO; PR:Q8W4H8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4H8; baseline and differential.
DR Genevisible; Q8W4H8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
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 Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..386
FT /note="Inactive GDSL esterase/lipase-like protein 23"
FT /id="PRO_0000367361"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 177
FT /note="T -> A (in Ref. 4; AAM67268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 43143 MW; 247E0DDFF1AC125C CRC64;
MMAKNCNLVS VLCVFLVLTL FNKPITVAGQ NIPAVGLFTF GDSNFDAGNK QTLTKTLLPQ
TFWPYGKSRD DPNGKFSDGL IAPDFLAKFM RIPIVIPPAL QPNVNVSRGA SFAVADATLL
GAPVESLTLN QQVRKFNQMK AANWNDDFVK KSVFMIYIGA NDYLNFTKNN PNADASTQQA
FVTSVTNKLK NDISLLYSSG ASKFVIQTLA PLGCLPIVRQ EFNTGMDQCY EKLNDLAKQH
NEKIGPMLNE LARTAPASAP FQFTVFDFYN AILTRTQRNQ NFRFFVTNAS CCGVGTHDAY
GCGFPNVHSR LCEYQRSYLF FDGRHNTEKA QEMFGHLLFG ADTNVIQPMN IRELVVYPAD
EPMRESWVPP TSATVQLRES RGYEYY
