(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 133.
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};
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   SMR; P52839; -.
DR   BioGrid; 304; 2.
DR   STRING; 3702.AT2G03760.1; -.
DR   iPTMnet; P52839; -.
DR   PaxDb; P52839; -.
DR   PRIDE; P52839; -.
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   eggNOG; ENOG4111H56; LUCA.
DR   HOGENOM; HOG000037210; -.
DR   InParanoid; P52839; -.
DR   OMA; ILMTKMI; -.
DR   OrthoDB; 780670at2759; -.
DR   PhylomeDB; P52839; -.
DR   BioCyc; ARA:AT2G03760-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G03760-MONOMER; -.
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: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   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;
DR   PRODOM; P52839.
DR   SWISS-2DPAGE; P52839.
KW   3D-structure; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..326
FT                   /note="Cytosolic sulfotransferase 12"
FT                   /id="PRO_0000085181"
FT   NP_BIND         75..80
FT                   /note="PAPS"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         290..292
FT                   /note="PAPS"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        2..6
FT                   /note="Poly-Ser"
FT   COMPBIAS        252..255
FT                   /note="Poly-Glu"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /note="PAPS"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /note="PAPS"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /note="PAPS"
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:0000244|PDB:1Q44"
FT   STRAND          29..31
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          33..41
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          44..46
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           48..60
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          68..71
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           79..89
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   TURN            90..95
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           96..101
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           103..106
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           109..112
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           116..122
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           128..130
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          136..139
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           143..145
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           148..152
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          156..161
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           164..177
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           188..197
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           205..218
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   TURN            220..222
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   STRAND          223..227
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           228..233
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           235..246
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           253..263
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           297..300
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   HELIX           303..316
FT                   /evidence="ECO:0000244|PDB:1Q44"
FT   TURN            317..319
FT                   /evidence="ECO:0000244|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
//

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