GDL21_ARATH
ID GDL21_ARATH Reviewed; 417 AA.
AC Q7XA74; Q8LA76; Q9SYF9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Inactive GDSL esterase/lipase-like protein 25;
DE AltName: Full=GDSL-like lipase 25;
DE AltName: Full=Myrosinase-associated protein GLL25;
DE AltName: Full=Protein ENDOPLASMIC RETICULUM MORPHOLOGY 3;
DE AltName: Full=Protein GOLGI DEFECTS 36;
DE AltName: Full=Protein MODIFIED VACUOLE PHENOTYPE 1;
DE AltName: Full=Protein NUCLEAR CAGE;
DE Flags: Precursor;
GN Name=MVP1; Synonyms=ERMO3, GLL25, GOLD36, NUC; OrderedLocusNames=At1g54030;
GN ORFNames=F15I1.11;
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 GENE FAMILY, AND NOMENCLATURE.
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 FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-80, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20626647; DOI=10.1111/j.1365-313x.2010.04296.x;
RA Marti L., Stefano G., Tamura K., Hawes C., Renna L., Held M.A.,
RA Brandizzi F.;
RT "A missense mutation in the vacuolar protein GOLD36 causes organizational
RT defects in the ER and aberrant protein trafficking in the plant secretory
RT pathway.";
RL Plant J. 63:901-913(2010).
RN [9]
RP FUNCTION, MUTAGENESIS OF GLY-57, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION BY PATHOGENS AND METHYL JASMONATE,
RP INTERACTION WITH TGG2, AND SUBCELLULAR LOCATION.
RX PubMed=19880612; DOI=10.1104/pp.109.145078;
RA Agee A.E., Surpin M., Sohn E.J., Girke T., Rosado A., Kram B.W., Carter C.,
RA Wentzell A.M., Kliebenstein D.J., Jin H.C., Park O.K., Jin H., Hicks G.R.,
RA Raikhel N.V.;
RT "MODIFIED VACUOLE PHENOTYPE1 is an Arabidopsis myrosinase-associated
RT protein involved in endomembrane protein trafficking.";
RL Plant Physiol. 152:120-132(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP GLY-59, AND INTERACTION WITH PYK10 COMPLEX.
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 [11]
RP FUNCTION, AND MUTAGENESIS OF GLY-341.
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 organization of the endomembrane system and is
CC required for endoplasmic reticulum morphology and organelle
CC distribution. May act by inhibiting the formation of PYK10 complex by
CC binding to GLL23 and exporting it from the ER. Required for proper
CC subcellular localization of myrosinase TGG2. Has no lipase or esterase
CC activity. {ECO:0000269|PubMed:19880612, ECO:0000269|PubMed:20626647,
CC ECO:0000269|PubMed:23155454, ECO:0000269|PubMed:24330158}.
CC -!- SUBUNIT: Interacts with the PYK10 complex and TGG2, but not with TGG1
CC or PEN2. {ECO:0000269|PubMed:19880612, ECO:0000269|PubMed:23155454}.
CC -!- SUBCELLULAR LOCATION: Vacuole. Endoplasmic reticulum. Note=Also found
CC in ER bodies. Retained in the ER when mutated.
CC -!- TISSUE SPECIFICITY: Expressed throughout the seedling, rosette leaves,
CC roots, inflorescence and imbibed seed, but not in pollen.
CC {ECO:0000269|PubMed:19880612}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all developmental stages, with
CC the highest accumulation in germinated seeds.
CC {ECO:0000269|PubMed:19880612}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate and upon pathogen
CC infection. {ECO:0000269|PubMed:19880612}.
CC -!- DISRUPTION PHENOTYPE: Defects in endoplasmic reticulum (ER) protein
CC export and organizational defects in the ER, including aggregation of
CC ER around the nucleus. Increased sensitivity to salt.
CC {ECO:0000269|PubMed:19880612, ECO:0000269|PubMed:20626647,
CC ECO:0000269|PubMed:23155454}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved active site 'GDSL' motif and has no lipase
CC activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25775.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM65534.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM65534.1; Type=Miscellaneous discrepancy; Note=The stop codon at position 16 is created by sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC006577; AAD25775.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33038.1; -; Genomic_DNA.
DR EMBL; BT010163; AAQ22632.1; -; mRNA.
DR EMBL; AY087988; AAM65534.1; ALT_SEQ; mRNA.
DR PIR; H96580; H96580.
DR RefSeq; NP_175805.1; NM_104280.4.
DR AlphaFoldDB; Q7XA74; -.
DR SMR; Q7XA74; -.
DR BioGRID; 27066; 4.
DR IntAct; Q7XA74; 1.
DR STRING; 3702.AT1G54030.1; -.
DR PaxDb; Q7XA74; -.
DR PRIDE; Q7XA74; -.
DR ProteomicsDB; 221920; -.
DR EnsemblPlants; AT1G54030.1; AT1G54030.1; AT1G54030.
DR GeneID; 841841; -.
DR Gramene; AT1G54030.1; AT1G54030.1; AT1G54030.
DR KEGG; ath:AT1G54030; -.
DR Araport; AT1G54030; -.
DR TAIR; locus:2014385; AT1G54030.
DR eggNOG; ENOG502S4IX; Eukaryota.
DR HOGENOM; CLU_015101_7_0_1; -.
DR InParanoid; Q7XA74; -.
DR OMA; CAKPEEY; -.
DR OrthoDB; 704138at2759; -.
DR PhylomeDB; Q7XA74; -.
DR BioCyc; ARA:AT1G54030-MON; -.
DR PRO; PR:Q7XA74; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7XA74; baseline and differential.
DR Genevisible; Q7XA74; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IMP:TAIR.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:TAIR.
DR CDD; cd01837; SGNH_plant_lipase_like; 1.
DR Gene3D; 3.40.50.1110; -; 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; PTHR45966; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..417
FT /note="Inactive GDSL esterase/lipase-like protein 25"
FT /id="PRO_0000367363"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 57
FT /note="G->E: In mvp1-1; defects in endoplasmic reticulum
FT (ER) protein export and organizational defects in the ER."
FT /evidence="ECO:0000269|PubMed:19880612"
FT MUTAGEN 59
FT /note="G->S: Restored lipase activity, but no effect on ER
FT morphology."
FT /evidence="ECO:0000269|PubMed:23155454"
FT MUTAGEN 80
FT /note="P->L: Defects in endoplasmic reticulum (ER) protein
FT export and organizational defects in the ER."
FT /evidence="ECO:0000269|PubMed:20626647"
FT MUTAGEN 341
FT /note="G->R: In nuc; formation of large perinuclear
FT aggregates accumulating GLL23."
FT /evidence="ECO:0000269|PubMed:24330158"
FT CONFLICT 5
FT /note="P -> R (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="N -> I (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="E -> R (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> V (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="P -> L (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="T -> N (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="Q -> E (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="N -> D (in Ref. 4; AAM65534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46083 MW; B0F628CA85617B14 CRC64;
MLLIPSFTAN SNEPPPSKLS LSDLSMAILK SHFFLLFPLL LLHFHTVSFA QTLFVFGDGL
YDAGNKQFLS QNRVDASFPP YGVTVGQATG RWSDGSIVPD YLAKFMGIPK ISPILLTTAD
FSHGANFAIA DATVLGSPPE TMTLSQQVKK FSENKNKWTN QTRSEAIYLI YIGSDDYLSY
AKSNPSPSDT QKQAFVDQVI TTIKAEIKVV YGSGGRKFAF QNLAPLGCLP AVKQASGNVQ
ECVKLPSEMA ALHNKKLLQL LVELSRELNG FQYSFYDFFS SIQNRVIKSK TYTFETGNAA
CCGTGSINGS NCSAKNVCAK PEEYIFFDGK HLTQEANLQV GHLMWGADPE VIGPNNIREL
MVLPLDITVI LAGIQEAMAA MRPRQSNIES LYDIKKMESE MDNHWLYQVD KAISFMI
