SOT12_ARATH
ID SOT12_ARATH Reviewed; 326 AA.
AC P52839; Q9SJW2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cytosolic sulfotransferase 12;
DE Short=AtSOT12;
DE EC=2.8.2.-;
DE AltName: Full=Sulfotransferase 1;
DE Short=AtST1;
GN Name=SOT12; Synonyms=RAR047, ST1; OrderedLocusNames=At2g03760;
GN ORFNames=F19B11.21;
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], INDUCTION BY PATHOGENS, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8639757; DOI=10.1007/bf00020810;
RA Lacomme C., Roby D.;
RT "Molecular cloning of a sulfotransferase in Arabidopsis thaliana and
RT regulation during development and in response to infection with pathogenic
RT bacteria.";
RL Plant Mol. Biol. 30:995-1008(1996).
RN [2]
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 [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].
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] OF 1-93.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=9212075; DOI=10.1096/fasebj.11.7.9212075;
RA Varin L., Marsolais F., Richard M., Rouleau M.;
RT "Sulfation and sulfotransferases 6: Biochemistry and molecular biology of
RT plant sulfotransferases.";
RL FASEB J. 11:517-525(1997).
RN [7]
RP GENE FAMILY, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=15234990; DOI=10.1093/jxb/erh183;
RA Klein M., Papenbrock J.;
RT "The multi-protein family of Arabidopsis sulphotransferases and their
RT relatives in other plant species.";
RL J. Exp. Bot. 55:1809-1820(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=17039368; DOI=10.1007/s00425-006-0413-y;
RA Marsolais F., Boyd J., Paredes Y., Schinas A.M., Garcia M., Elzein S.,
RA Varin L.;
RT "Molecular and biochemical characterization of two brassinosteroid
RT sulfotransferases from Arabidopsis, AtST4a (At2g14920) and AtST1
RT (At2g03760).";
RL Planta 225:1233-1244(2007).
RN [9]
RP SUBUNIT.
RX PubMed=19173308; DOI=10.1002/prot.22347;
RA Weitzner B., Meehan T., Xu Q., Dunbrack R.L. Jr.;
RT "An unusually small dimer interface is observed in all available crystal
RT structures of cytosolic sulfotransferases.";
RL Proteins 75:289-295(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20374532; DOI=10.1111/j.1365-3040.2010.02156.x;
RA Baek D., Pathange P., Chung J.S., Jiang J., Gao L., Oikawa A., Hirai M.Y.,
RA Saito K., Pare P.W., Shi H.;
RT "A stress-inducible sulphotransferase sulphonates salicylic acid and
RT confers pathogen resistance in Arabidopsis.";
RL Plant Cell Environ. 33:1383-1392(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=15317023; DOI=10.1002/prot.20258;
RA Smith D.W., Johnson K.A., Bingman C.A., Aceti D.J., Blommel P.G.,
RA Wrobel R.L., Frederick R.O., Zhao Q., Sreenath H., Fox B.G., Volkman B.F.,
RA Jeon W.B., Newman C.S., Ulrich E.L., Hegeman A.D., Kimball T., Thao S.,
RA Sussman M.R., Markley J.L., Phillips G.N. Jr.;
RT "Crystal structure of At2g03760, a putative steroid sulfotransferase from
RT Arabidopsis thaliana.";
RL Proteins 57:854-857(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the stereospecific sulfate
CC conjugation of 24-epibrassinosteroids. Preferred substrates are 24-
CC epicathasterone and 6-deoxo-24-epicathasterone. Low activity with 22-
CC deoxy-24-epiteasterone. No activity with 24-epimers catasterone and
CC brassinolide. Sulfonates salicylic acid. May be involved in
CC detoxification. Enhances plant response to pathogen infection and
CC contributes to long distance signaling in systemic acquired resistance
CC (SAR). {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for 24-epicathasterone {ECO:0000269|PubMed:17039368,
CC ECO:0000269|PubMed:20374532};
CC KM=1.9 uM for 6-deoxo-24-epicathasterone
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC KM=3.0 uM for 17-beta-estradiol {ECO:0000269|PubMed:17039368,
CC ECO:0000269|PubMed:20374532};
CC KM=1.1 uM for dehydroepiandrosterone {ECO:0000269|PubMed:17039368,
CC ECO:0000269|PubMed:20374532};
CC KM=13 uM for pregnenolone {ECO:0000269|PubMed:17039368,
CC ECO:0000269|PubMed:20374532};
CC KM=0.44 mM for salicylic acid {ECO:0000269|PubMed:17039368,
CC ECO:0000269|PubMed:20374532};
CC KM=3 uM for 3'-phospho-5'-adenylyl sulfate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=57 pmol/sec/mg enzyme with 24-epicathasterone as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=4.4 pmol/sec/mg enzyme with 24-epicathasterone as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=1.6 pmol/sec/mg enzyme with 17-beta-estradiol as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=1.3 pmol/sec/mg enzyme with dehydroepiandrosterone as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=5.9 pmol/sec/mg enzyme with pregnenolone as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC Vmax=2.67 pmol/sec/mg enzyme with salicylic acid as substrate
CC {ECO:0000269|PubMed:17039368, ECO:0000269|PubMed:20374532};
CC -!- SUBUNIT: Dimer. {ECO:0000305|PubMed:19173308}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the aerial parts of seedlings, in
CC roots, leaves and flowers. Not detected in stems and siliques.
CC {ECO:0000269|PubMed:20374532, ECO:0000269|PubMed:8639757,
CC ECO:0000269|PubMed:9212075}.
CC -!- INDUCTION: Up-regulated by pathogens, methyljasmonate, salicylic acid,
CC salt, osmotic stress, cold, auxin, cytokinin and abscisic acid
CC treatments. Not induced by desiccation and ethylene treatment.
CC {ECO:0000269|PubMed:20374532, ECO:0000269|PubMed:8639757,
CC ECO:0000269|PubMed:9212075}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to NaCl and ABA in seed
CC germination, and to salicylic acid (SA) in seedling growth.
CC {ECO:0000269|PubMed:20374532}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80546.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA86850.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z46823; CAA86850.1; ALT_FRAME; mRNA.
DR EMBL; AC006836; AAD20078.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05746.1; -; Genomic_DNA.
DR EMBL; AF375458; AAK53042.1; -; mRNA.
DR EMBL; AY113050; AAM47358.1; -; mRNA.
DR EMBL; Z23001; CAA80546.1; ALT_INIT; mRNA.
DR PIR; A84452; A84452.
DR PIR; S69188; S69188.
DR RefSeq; NP_178471.1; NM_126423.4.
DR PDB; 1Q44; X-ray; 1.90 A; A=1-326.
DR PDB; 2Q3M; X-ray; 1.90 A; A=1-326.
DR PDBsum; 1Q44; -.
DR PDBsum; 2Q3M; -.
DR AlphaFoldDB; P52839; -.
DR SMR; P52839; -.
DR BioGRID; 304; 2.
DR STRING; 3702.AT2G03760.1; -.
DR iPTMnet; P52839; -.
DR PaxDb; P52839; -.
DR PRIDE; P52839; -.
DR ProteomicsDB; 232602; -.
DR DNASU; 814903; -.
DR EnsemblPlants; AT2G03760.1; AT2G03760.1; AT2G03760.
DR GeneID; 814903; -.
DR Gramene; AT2G03760.1; AT2G03760.1; AT2G03760.
DR KEGG; ath:AT2G03760; -.
DR Araport; AT2G03760; -.
DR TAIR; locus:2044234; AT2G03760.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_2_1; -.
DR InParanoid; P52839; -.
DR OMA; CRGVSLY; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P52839; -.
DR BioCyc; ARA:AT2G03760-MON; -.
DR BioCyc; MetaCyc:AT2G03760-MON; -.
DR BRENDA; 2.8.2.2; 399.
DR SABIO-RK; P52839; -.
DR EvolutionaryTrace; P52839; -.
DR PRO; PR:P52839; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P52839; baseline and differential.
DR Genevisible; P52839; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0080118; F:brassinosteroid sulfotransferase activity; IDA:TAIR.
DR GO; GO:1990135; F:flavonoid sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:TAIR.
DR GO; GO:0016131; P:brassinosteroid metabolic process; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..326
FT /note="Cytosolic sulfotransferase 12"
FT /id="PRO_0000085181"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 75..80
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 290..292
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CONFLICT 85..93
FT /note="VFALLNRHK -> ALPSDTVPV (in Ref. 5; CAA80546)"
FT /evidence="ECO:0000305"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1Q44"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:1Q44"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1Q44"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1Q44"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:1Q44"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1Q44"
SQ SEQUENCE 326 AA; 37139 MW; 085069A2EBD4E10A CRC64;
MSSSSSVPAY LGDEDLTQET RALISSLPKE KGWLVSEIYE FQGLWHTQAI LQGILICQKR
FEAKDSDIIL VTNPKSGTTW LKALVFALLN RHKFPVSSSG NHPLLVTNPH LLVPFLEGVY
YESPDFDFSS LPSPRLMNTH ISHLSLPESV KSSSCKIVYC CRNPKDMFVS LWHFGKKLAP
EETADYPIEK AVEAFCEGKF IGGPFWDHIL EYWYASRENP NKVLFVTYEE LKKQTEVEMK
RIAEFLECGF IEEEEVREIV KLCSFESLSN LEVNKEGKLP NGIETKTFFR KGEIGGWRDT
LSESLAEEID RTIEEKFKGS GLKFSS
