SAG13_ARATH
ID SAG13_ARATH Reviewed; 269 AA.
AC Q9ZW18; F4IKM5; F4IKM6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Senescence-associated protein 13 {ECO:0000303|PubMed:9617813};
DE AltName: Full=Tropinone reductase homolog SAG13 {ECO:0000250|UniProtKB:P50162};
DE EC=1.1.1.- {ECO:0000305};
GN Name=SAG13 {ECO:0000303|PubMed:9617813};
GN OrderedLocusNames=At2g29350 {ECO:0000312|Araport:AT2G29350};
GN ORFNames=F16P2.27 {ECO:0000312|EMBL:AAC95203.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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] (ISOFORM 1).
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 DEVELOPMENTAL STAGE, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=9617813; DOI=10.1023/a:1005934428906;
RA Weaver L.M., Gan S., Quirino B., Amasino R.M.;
RT "A comparison of the expression patterns of several senescence-associated
RT genes in response to stress and hormone treatment.";
RL Plant Mol. Biol. 37:455-469(1998).
RN [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [8]
RP FUNCTION, 3D-STRUCTURE MODELING, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24583623; DOI=10.1016/j.bioorg.2014.01.004;
RA Reinhardt N., Fischer J., Coppi R., Blum E., Brandt W., Draeger B.;
RT "Substrate flexibility and reaction specificity of tropinone reductase-like
RT short-chain dehydrogenases.";
RL Bioorg. Chem. 53:37-49(2014).
CC -!- FUNCTION: Unspecific reductase providing both diastereomeric alcohols
CC from the prochiral ketones. Active on cyclic monoterpenes and small
CC flexible lipophilic carbonyls. No activity with tropinone, nitrogen-
CC containing tropinone analogs, tropine or pseudotropine as substrate.
CC {ECO:0000269|PubMed:24583623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30.1 uM for NADPH {ECO:0000269|PubMed:24583623};
CC KM=37.8 uM for NADP {ECO:0000269|PubMed:24583623};
CC KM=264.1 uM for citronellal {ECO:0000269|PubMed:24583623};
CC KM=612.0 uM for pentanal {ECO:0000269|PubMed:24583623};
CC KM=98.1 uM for nerol {ECO:0000269|PubMed:24583623};
CC KM=504.9 uM for 3-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=57.2 uM for 3-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=5.1 uM for 4-methylcyclohexanone {ECO:0000269|PubMed:24583623};
CC KM=29.2 uM for 4-methylcyclohexanol {ECO:0000269|PubMed:24583623};
CC KM=118.1 uM for (-)-menthone {ECO:0000269|PubMed:24583623};
CC KM=50.1 uM for (-)-menthol {ECO:0000269|PubMed:24583623};
CC KM=75.7 uM for (-)-carvone {ECO:0000269|PubMed:24583623};
CC KM=1340.0 uM for (-)-alpha-thujone {ECO:0000269|PubMed:24583623};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ZW18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZW18-2; Sequence=VSP_057491, VSP_057492;
CC Name=3;
CC IsoId=Q9ZW18-3; Sequence=VSP_057490;
CC -!- DEVELOPMENTAL STAGE: Expressed 2 days before visible senescence began
CC (PubMed:9617813). Detected from day 24 (PubMed:18978034).
CC {ECO:0000269|PubMed:18978034, ECO:0000269|PubMed:9617813}.
CC -!- INDUCTION: No basal expression in untreated young leaves, but rapidly
CC and strongly up-regulated upon abscisic acid treatment
CC (PubMed:9617813). Strongly up-regulated (10'000-fold higher expression
CC at day 33) in the quinolinate synthase mutant old5 (PubMed:18978034).
CC {ECO:0000269|PubMed:18978034, ECO:0000269|PubMed:9617813}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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DR EMBL; AC004561; AAC95203.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08239.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08240.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08241.1; -; Genomic_DNA.
DR EMBL; AY065111; AAL38287.1; -; mRNA.
DR EMBL; AY081642; AAM10204.1; -; mRNA.
DR EMBL; AY085321; AAM62552.1; -; mRNA.
DR PIR; C84695; C84695.
DR RefSeq; NP_001031442.1; NM_001036365.1. [Q9ZW18-3]
DR RefSeq; NP_180496.1; NM_128489.3. [Q9ZW18-1]
DR RefSeq; NP_973558.1; NM_201829.2. [Q9ZW18-2]
DR AlphaFoldDB; Q9ZW18; -.
DR SMR; Q9ZW18; -.
DR IntAct; Q9ZW18; 6.
DR STRING; 3702.AT2G29350.1; -.
DR PaxDb; Q9ZW18; -.
DR PRIDE; Q9ZW18; -.
DR ProteomicsDB; 226685; -. [Q9ZW18-1]
DR EnsemblPlants; AT2G29350.1; AT2G29350.1; AT2G29350. [Q9ZW18-1]
DR EnsemblPlants; AT2G29350.2; AT2G29350.2; AT2G29350. [Q9ZW18-2]
DR EnsemblPlants; AT2G29350.3; AT2G29350.3; AT2G29350. [Q9ZW18-3]
DR GeneID; 817484; -.
DR Gramene; AT2G29350.1; AT2G29350.1; AT2G29350. [Q9ZW18-1]
DR Gramene; AT2G29350.2; AT2G29350.2; AT2G29350. [Q9ZW18-2]
DR Gramene; AT2G29350.3; AT2G29350.3; AT2G29350. [Q9ZW18-3]
DR KEGG; ath:AT2G29350; -.
DR Araport; AT2G29350; -.
DR TAIR; locus:2043177; AT2G29350.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q9ZW18; -.
DR OMA; QFSMKGK; -.
DR PhylomeDB; Q9ZW18; -.
DR BioCyc; ARA:AT2G29350-MON; -.
DR SABIO-RK; Q9ZW18; -.
DR PRO; PR:Q9ZW18; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW18; baseline and differential.
DR Genevisible; Q9ZW18; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; TAS:TAIR.
DR GO; GO:0007568; P:aging; IEP:TAIR.
DR GO; GO:0002213; P:defense response to insect; IEP:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR045000; TR.
DR PANTHER; PTHR42898; PTHR42898; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..269
FT /note="Senescence-associated protein 13"
FT /id="PRO_0000432216"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 21..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /id="VSP_057490"
FT VAR_SEQ 208..225
FT /note="FFDEEFKKEAVRTTPMGR -> VRPKFIFLLRTMKNKKNT (in isoform
FT 2)"
FT /id="VSP_057491"
FT VAR_SEQ 226..269
FT /note="Missing (in isoform 2)"
FT /id="VSP_057492"
SQ SEQUENCE 269 AA; 28820 MW; F39DCB95A2C920BF CRC64;
MAKEGGLGEN SRWSLGGMTA LVTGGSKGIG EAVVEELAML GAKVHTCARD ETQLQERLRE
WQAKGFQVTT SVCDVSSRDQ RVKLMETVSS LYQGKLNILV NNVGTSIFKP TTEYTAEDFS
FVMATNLESA FHLSQLAHPL LKASGSGSIV LISSAAGVVH VNVGSIYGAT KGAMNQLARN
LACEWASDNI RTNSVCPWYI TTPLSNDFFD EEFKKEAVRT TPMGRVGEAN EVSPLVAFLC
LPSASYITGQ TICVDGGATV NGFSFKTMP
