STR15_ARATH
ID STR15_ARATH Reviewed; 182 AA.
AC Q38853; F4JNT6; Q38852; Q8LEW3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Rhodanese-like domain-containing protein 15, chloroplastic;
DE AltName: Full=Protein DARK INDUCIBLE 1;
DE AltName: Full=Senescence-associated protein 1;
DE Short=AtSEN1;
DE AltName: Full=Sulfurtransferase 15;
DE Short=AtStr15;
DE Flags: Precursor;
GN Name=STR15; Synonyms=DIN1, SEN1; OrderedLocusNames=At4g35770;
GN ORFNames=F4B14.3, F8D20.280;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND INDUCTION.
RX PubMed=8624406; DOI=10.1007/bf00019008;
RA Oh S.A., Lee S.Y., Chung I.K., Lee C.H., Nam H.G.;
RT "A senescence-associated gene of Arabidopsis thaliana is distinctively
RT regulated during natural and artificially induced leaf senescence.";
RL Plant Mol. Biol. 30:739-754(1996).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=11080291; DOI=10.1104/pp.124.3.1139;
RA Fujiki Y., Ito M., Nishida I., Watanabe A.;
RT "Multiple signaling pathways in gene expression during sugar starvation.
RT Pharmacological analysis of din gene expression in suspension-cultured
RT cells of Arabidopsis.";
RL Plant Physiol. 124:1139-1148(2000).
RN [7]
RP INDUCTION.
RX PubMed=15295076; DOI=10.1093/pcp/pch110;
RA Woo H.R., Kim J.H., Nam H.G., Lim P.O.;
RT "The delayed leaf senescence mutants of Arabidopsis, ore1, ore3, and ore9
RT are tolerant to oxidative stress.";
RL Plant Cell Physiol. 45:923-932(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15181206; DOI=10.1104/pp.104.040121;
RA Bauer M., Dietrich C., Nowak K., Sierralta W.D., Papenbrock J.;
RT "Intracellular localization of Arabidopsis sulfurtransferases.";
RL Plant Physiol. 135:916-926(2004).
RN [9]
RP INDUCTION.
RX PubMed=16325410; DOI=10.1016/j.plaphy.2005.09.002;
RA Schenk P.M., Kazan K., Rusu A.G., Manners J.M., Maclean D.J.;
RT "The SEN1 gene of Arabidopsis is regulated by signals that link plant
RT defence responses and senescence.";
RL Plant Physiol. Biochem. 43:997-1005(2005).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA Bartels A., Mock H.P., Papenbrock J.;
RT "Differential expression of Arabidopsis sulfurtransferases under various
RT growth conditions.";
RL Plant Physiol. Biochem. 45:178-187(2007).
RN [11]
RP INDUCTION.
RX PubMed=20238146; DOI=10.1007/s11103-010-9618-3;
RA Fischer-Kilbienski I., Miao Y., Roitsch T., Zschiesche W., Humbeck K.,
RA Krupinska K.;
RT "Nuclear targeted AtS40 modulates senescence associated gene expression in
RT Arabidopsis thaliana during natural development and in darkness.";
RL Plant Mol. Biol. 73:379-390(2010).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15181206}. Thylakoid {ECO:0000269|PubMed:15181206}.
CC Note=Associated with membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38853-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38853-2; Sequence=VSP_042635, VSP_042636;
CC -!- INDUCTION: By senescence, dark, sucrose starvation, 3-O-methylglucose,
CC salicylic acid, methyl jasmonate, methyl viologen and infection by the
CC pathogens A.brassicicola and P.syringae pv. tomato.
CC {ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:15295076,
CC ECO:0000269|PubMed:16325410, ECO:0000269|PubMed:20238146,
CC ECO:0000269|PubMed:8624406}.
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DR EMBL; U26944; AAA80302.1; -; Genomic_DNA.
DR EMBL; U26945; AAA80303.1; -; mRNA.
DR EMBL; AL031135; CAA20047.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81486.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86560.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86561.1; -; Genomic_DNA.
DR EMBL; AY078973; AAL79579.1; -; mRNA.
DR EMBL; AY091671; AAM10270.1; -; mRNA.
DR EMBL; AY085192; AAM61743.1; -; mRNA.
DR PIR; T04682; T04682.
DR RefSeq; NP_001078496.1; NM_001085027.2. [Q38853-2]
DR RefSeq; NP_195302.1; NM_119743.4. [Q38853-1]
DR AlphaFoldDB; Q38853; -.
DR SMR; Q38853; -.
DR BioGRID; 15012; 6.
DR IntAct; Q38853; 2.
DR STRING; 3702.AT4G35770.1; -.
DR iPTMnet; Q38853; -.
DR PaxDb; Q38853; -.
DR PRIDE; Q38853; -.
DR EnsemblPlants; AT4G35770.1; AT4G35770.1; AT4G35770. [Q38853-1]
DR EnsemblPlants; AT4G35770.2; AT4G35770.2; AT4G35770. [Q38853-2]
DR GeneID; 829730; -.
DR Gramene; AT4G35770.1; AT4G35770.1; AT4G35770. [Q38853-1]
DR Gramene; AT4G35770.2; AT4G35770.2; AT4G35770. [Q38853-2]
DR KEGG; ath:AT4G35770; -.
DR Araport; AT4G35770; -.
DR TAIR; locus:2128038; AT4G35770.
DR eggNOG; KOG1530; Eukaryota.
DR HOGENOM; CLU_089574_3_0_1; -.
DR InParanoid; Q38853; -.
DR OMA; FPNFRRE; -.
DR PhylomeDB; Q38853; -.
DR BRENDA; 2.8.1.1; 399.
DR PRO; PR:Q38853; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38853; baseline and differential.
DR Genevisible; Q38853; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0007568; P:aging; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 66..182
FT /note="Rhodanese-like domain-containing protein 15,
FT chloroplastic"
FT /id="PRO_0000416536"
FT DOMAIN 82..182
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 142
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT VAR_SEQ 159..161
FT /note="GFT -> VCV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042635"
FT VAR_SEQ 162..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042636"
FT CONFLICT 6
FT /note="F -> Y (in Ref. 5; AAM61743)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..81
FT /note="EL -> DV (in Ref. 1; AAA80302)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20079 MW; 9A72C7179B250530 CRC64;
METTAFNTTS RIGNWSSAIS PPLQTCGSFK CQLPTRRGVI VADLRNSNFR WRKATTTSRG
NVAAEAVKIP TSVPVRVARE LAQAGYRYLD VRTPDEFSIG HPTRAINVPY MYRVGSGMVK
NPSFLRQVSS HFRKHDEIII GCESGQMSFM ASTDLLTAGF TAITDIAGGY VAWTENELPV
EE
