PGM48_ARATH
ID PGM48_ARATH Reviewed; 344 AA.
AC Q9LSC4; Q8LE96;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Plastoglobule-localized metallopeptidase 48, chloroplastic {ECO:0000303|PubMed:27895226};
DE EC=3.4.24.- {ECO:0000269|PubMed:27895226};
DE Flags: Precursor;
GN Name=PGM48 {ECO:0000303|PubMed:27895226};
GN OrderedLocusNames=At3g27110 {ECO:0000312|Araport:AT3G27110};
GN ORFNames=MOJ10.19 {ECO:0000312|EMBL:BAB01093.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, COFACTOR, INTERACTION
RP WITH ABC1K3; PES1 AND CCD4, AND DEVELOPMENTAL STAGE.
RX PubMed=27895226; DOI=10.1105/tpc.16.00745;
RA Bhuiyan N.H., Friso G., Rowland E., Majsec K., van Wijk K.J.;
RT "The plastoglobule-localized metallopeptidase PGM48 is a positive regulator
RT of senescence in Arabidopsis thaliana.";
RL Plant Cell 28:3020-3037(2016).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=28534654; DOI=10.1080/15592324.2017.1331197;
RA Bhuiyan N.H., van Wijk K.J.;
RT "Functions and substrates of plastoglobule-localized metallopeptidase
RT PGM48.";
RL Plant Signal. Behav. 12:e1331197-e1331197(2017).
CC -!- FUNCTION: Metalloendopeptidase with a Zn-dependent proteolytic activity
CC and substrate cleavage upstream of hydrophobic residues
CC (PubMed:27895226). Positive regulator of senescence, probably by
CC degrading CCD4, thus participating in the controlled removal of
CC carotenoids from the thylakoid membrane during the senescence process
CC (PubMed:27895226, PubMed:28534654). {ECO:0000269|PubMed:27895226,
CC ECO:0000269|PubMed:28534654}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:27895226};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
CC -!- SUBUNIT: Interacts with plastoglobule (PG) core proteins ABC1K3, PES1
CC and CCD4. {ECO:0000269|PubMed:27895226}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:27895226}. Plastid, chloroplast membrane
CC {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers (e.g. sepals, petals
CC and stamen), seeds, leaves and cotyledons.
CC {ECO:0000269|PubMed:28534654}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during leaf senescence.
CC {ECO:0000269|PubMed:27895226, ECO:0000269|PubMed:28534654}.
CC -!- DISRUPTION PHENOTYPE: Delayed senescence.
CC {ECO:0000269|PubMed:27895226}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. M48D subfamily.
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DR EMBL; AB026649; BAB01093.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77268.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77269.1; -; Genomic_DNA.
DR EMBL; AY045604; AAK73962.1; -; mRNA.
DR EMBL; BT002704; AAO11620.1; -; mRNA.
DR EMBL; AK316844; BAH19556.1; -; mRNA.
DR EMBL; AY085546; AAM62770.1; -; mRNA.
DR RefSeq; NP_566808.1; NM_113625.4.
DR RefSeq; NP_850640.1; NM_180309.3.
DR AlphaFoldDB; Q9LSC4; -.
DR STRING; 3702.AT3G27110.1; -.
DR MEROPS; M48.021; -.
DR PaxDb; Q9LSC4; -.
DR PRIDE; Q9LSC4; -.
DR ProteomicsDB; 252049; -.
DR EnsemblPlants; AT3G27110.1; AT3G27110.1; AT3G27110.
DR EnsemblPlants; AT3G27110.2; AT3G27110.2; AT3G27110.
DR GeneID; 822330; -.
DR Gramene; AT3G27110.1; AT3G27110.1; AT3G27110.
DR Gramene; AT3G27110.2; AT3G27110.2; AT3G27110.
DR Araport; AT3G27110; -.
DR TAIR; locus:2092010; AT3G27110.
DR eggNOG; ENOG502QUG6; Eukaryota.
DR HOGENOM; CLU_052979_1_0_1; -.
DR InParanoid; Q9LSC4; -.
DR OMA; PNAMCIG; -.
DR OrthoDB; 974822at2759; -.
DR PhylomeDB; Q9LSC4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSC4; baseline and differential.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0010287; C:plastoglobule; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:TAIR.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:1900055; P:regulation of leaf senescence; IDA:UniProtKB.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Membrane; Metal-binding; Metalloprotease; Plastid;
KW Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Zinc.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..344
FT /note="Plastoglobule-localized metallopeptidase 48,
FT chloroplastic"
FT /id="PRO_0000454277"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 192
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75844"
FT CONFLICT 267
FT /note="G -> A (in Ref. 5; AAM62770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37948 MW; 5F86A821C85C8888 CRC64;
MAVSVSAPVL SLCYNQSGEL SRSLGYRLPK KVGFSSGRRS VSYIGFGAEK VGRFRVRVPI
CRAVPPLLFK DLDADDFRHP FDKQNTLLLR AIPGLNEFGK ALLGSMTEQI MLLENIGTSV
LVSKNQLSDL HGLLVEAAEI LNIEAPDLYV RQSPVPNAYT LAISGKKPFI VVHTSLIELL
TSAELQAVLA HELGHLKCDH GVWLTFANIL TLGAYTVPAF GQMIARTLEE QLLRWLRSAE
LTCDRAALLV AQDPKVVVSV LMKLAGGCPS IADQLNVDAF LEQARSYDKA SSSPLGWYIR
NAQTSQLSHP LPVLRAREID EWSRSLEYKS LLKRANRKST VQKV
