SGR2_ARATH
ID SGR2_ARATH Reviewed; 271 AA.
AC Q66WT5; Q9T059;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Magnesium dechelatase SGR2, chloroplastic {ECO:0000305};
DE EC=4.99.1.10 {ECO:0000269|PubMed:27604697};
DE AltName: Full=Protein NONYELLOWING 2 {ECO:0000303|PubMed:17468209};
DE AltName: Full=Protein STAY-GREEN 2 {ECO:0000303|PubMed:18301989};
DE AltName: Full=Protein STAYGREEN 2 {ECO:0000303|PubMed:17513504};
DE Flags: Precursor;
GN Name=SGR2 {ECO:0000303|PubMed:24043799};
GN Synonyms=NYE2 {ECO:0000303|PubMed:17468209},
GN SGN2 {ECO:0000303|PubMed:17513504};
GN OrderedLocusNames=At4g11910 {ECO:0000312|Araport:AT4G11910};
GN ORFNames=T26M18.120 {ECO:0000312|EMBL:CAB44329.1};
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=17513504; DOI=10.1105/tpc.106.044891;
RA Park S.Y., Yu J.W., Park J.S., Li J., Yoo S.C., Lee N.Y., Lee S.K.,
RA Jeong S.W., Seo H.S., Koh H.J., Jeon J.S., Park Y.I., Paek N.C.;
RT "The senescence-induced staygreen protein regulates chlorophyll
RT degradation.";
RL Plant Cell 19:1649-1664(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17468209; DOI=10.1104/pp.107.100172;
RA Ren G., An K., Liao Y., Zhou X., Cao Y., Zhao H., Ge X., Kuai B.;
RT "Identification of a novel chloroplast protein AtNYE1 regulating
RT chlorophyll degradation during leaf senescence in Arabidopsis.";
RL Plant Physiol. 144:1429-1441(2007).
RN [3]
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 [4]
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18301989; DOI=10.1007/s11103-008-9314-8;
RA Aubry S., Mani J., Hortensteiner S.;
RT "Stay-green protein, defective in Mendel's green cotyledon mutant, acts
RT independent and upstream of pheophorbide a oxygenase in the chlorophyll
RT catabolic pathway.";
RL Plant Mol. Biol. 67:243-256(2008).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24043799; DOI=10.1073/pnas.1308114110;
RA Delmas F., Sankaranarayanan S., Deb S., Widdup E., Bournonville C.,
RA Bollier N., Northey J.G., McCourt P., Samuel M.A.;
RT "ABI3 controls embryo degreening through Mendel's I locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3888-E3894(2013).
RN [7]
RP INTERACTION WITH LHCII AND RCCR, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24719469; DOI=10.1093/mp/ssu045;
RA Sakuraba Y., Park S.Y., Kim Y.S., Wang S.H., Yoo S.C., Hoertensteiner S.,
RA Paek N.C.;
RT "Arabidopsis STAY-GREEN2 is a negative regulator of chlorophyll degradation
RT during leaf senescence.";
RL Mol. Plant 7:1288-1302(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH RCCR.
RX PubMed=26732493; DOI=10.1016/j.molp.2015.12.016;
RA Wu S., Li Z., Yang L., Xie Z., Chen J., Zhang W., Liu T., Gao S., Gao J.,
RA Zhu Y., Xin J., Ren G., Kuai B.;
RT "NON-YELLOWING2 (NYE2), a close paralog of NYE1, plays a positive role in
RT chlorophyll degradation in Arabidopsis.";
RL Mol. Plant 9:624-627(2016).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27604697; DOI=10.1105/tpc.16.00428;
RA Shimoda Y., Ito H., Tanaka A.;
RT "Arabidopsis STAY-GREEN, Mendel's green cotyledon gene, encodes magnesium-
RT dechelatase.";
RL Plant Cell 28:2147-2160(2016).
RN [10]
RP FUNCTION.
RX PubMed=28873256; DOI=10.1111/tpj.13710;
RA Li Z., Wu S., Chen J., Wang X., Gao J., Ren G., Kuai B.;
RT "NYEs/SGRs-mediated chlorophyll degradation is critical for detoxification
RT during seed maturation in Arabidopsis.";
RL Plant J. 92:650-661(2017).
CC -!- FUNCTION: Magnesium chelatase involved in chlorophyll a degradation in
CC the chlorophyll-protein complexes of photosystem I (PSI) and
CC photosystem II (PSII) (PubMed:26732493, PubMed:27604697). Contributes
CC to the degradation of PSI and PSII in the thylakoid membranes
CC (PubMed:26732493, PubMed:27604697). Required to trigger chlorophyll
CC degradation during natural and dark-induced leaf senescence (Probable)
CC (PubMed:26732493). Mediates chlorophyll degradation during embryo
CC degreening (PubMed:24043799, PubMed:26732493, PubMed:28873256).
CC Recombinant SGR2 possesses high dechelating activity against
CC chlorophyll a, very low activity against chlorophyllide a, and no
CC activity against chlorophyll b (PubMed:27604697).
CC {ECO:0000269|PubMed:24043799, ECO:0000269|PubMed:26732493,
CC ECO:0000269|PubMed:27604697, ECO:0000269|PubMed:28873256,
CC ECO:0000305|PubMed:17513504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyll a + 2 H(+) = Mg(2+) + pheophytin a;
CC Xref=Rhea:RHEA:52788, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:58416, ChEBI:CHEBI:136840; EC=4.99.1.10;
CC Evidence={ECO:0000269|PubMed:27604697};
CC -!- SUBUNIT: Interacts with the light harvesting complex II (LHCII)
CC (PubMed:24719469). Interacts with the chlorophyll catabolic enzyme
CC (CCE) RCCR (PubMed:26732493, PubMed:24719469).
CC {ECO:0000269|PubMed:24719469, ECO:0000269|PubMed:26732493}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:24719469}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed at low level during leaf
CC development, but up-regulated during seed maturation and senescence,
CC when the leaf color changes from green to yellow.
CC {ECO:0000269|PubMed:17513504, ECO:0000269|PubMed:24043799}.
CC -!- INDUCTION: Induced during natural and dark-induced leaf senescence.
CC {ECO:0000269|PubMed:24719469}.
CC -!- DISRUPTION PHENOTYPE: No effect on seed degreening; probably due to
CC redundancy with SGR1. Sgr1 and sgr2 double mutant has an embryo stay-
CC green phenotype. {ECO:0000269|PubMed:18301989,
CC ECO:0000269|PubMed:24043799}.
CC -!- SIMILARITY: Belongs to the staygreen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB44329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78234.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY699948; AAU05981.1; -; mRNA.
DR EMBL; DQ437532; ABD77556.1; -; mRNA.
DR EMBL; AL078606; CAB44329.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161533; CAB78234.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83068.1; -; Genomic_DNA.
DR PIR; T09350; T09350.
DR RefSeq; NP_192928.2; NM_117261.6.
DR AlphaFoldDB; Q66WT5; -.
DR BioGRID; 12096; 1.
DR IntAct; Q66WT5; 1.
DR MINT; Q66WT5; -.
DR STRING; 3702.AT4G11910.1; -.
DR PaxDb; Q66WT5; -.
DR PRIDE; Q66WT5; -.
DR ProteomicsDB; 232584; -.
DR EnsemblPlants; AT4G11910.1; AT4G11910.1; AT4G11910.
DR GeneID; 826798; -.
DR Gramene; AT4G11910.1; AT4G11910.1; AT4G11910.
DR KEGG; ath:AT4G11910; -.
DR Araport; AT4G11910; -.
DR TAIR; locus:2137020; AT4G11910.
DR eggNOG; ENOG502S3TG; Eukaryota.
DR HOGENOM; CLU_073517_0_0_1; -.
DR InParanoid; Q66WT5; -.
DR OMA; ELGETQM; -.
DR OrthoDB; 1194276at2759; -.
DR PhylomeDB; Q66WT5; -.
DR PRO; PR:Q66WT5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q66WT5; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:TAIR.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0015996; P:chlorophyll catabolic process; IEA:UniProtKB-KW.
DR GO; GO:1903647; P:negative regulation of chlorophyll catabolic process; IMP:TAIR.
DR InterPro; IPR024438; Staygreen.
DR Pfam; PF12638; Staygreen; 1.
PE 1: Evidence at protein level;
KW Chlorophyll catabolism; Chloroplast; Lyase; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..271
FT /note="Magnesium dechelatase SGR2, chloroplastic"
FT /id="PRO_0000425232"
SQ SEQUENCE 271 AA; 30753 MW; D852EBB81756F32B CRC64;
MCSLATNLLL PSKMKPVFPE KLSTSSLCVT TRRSKMKNRS IVPVARLFGP AIFEASKLKV
LFLGVDEKKH PAKLPRTYTL THSDITAKLT LAISQSINNS QLQGWANKLF RDEVVGEWKK
VKGKMSLHVH CHISGGHFFL NLIAKLRYYI FCKELPVVLE AFAHGDEYLL NNHPELQESP
VWVYFHSNIP EYNKVECWGP LWEAMSQHQH DGRTHKKSET LPELPCPDEC KCCFPTVSTI
PWSHRHYQHT AADENVADGL LEIPNPGKSK G
