SOT14_ARATH
ID SOT14_ARATH Reviewed; 347 AA.
AC Q8GZ53; Q9FL46;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytosolic sulfotransferase 14;
DE Short=AtSOT14;
DE EC=2.8.2.-;
DE AltName: Full=Sulfotransferase 2b;
DE Short=AtST2b;
GN Name=SOT14; Synonyms=ST2B; OrderedLocusNames=At5g07000; ORFNames=MOJ9.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 IDENTIFICATION, AND FUNCTION.
RX PubMed=12637544; DOI=10.1074/jbc.m211943200;
RA Gidda S.K., Miersch O., Levitin A., Schmidt J., Wasternack C., Varin L.;
RT "Biochemical and molecular characterization of a hydroxyjasmonate
RT sulfotransferase from Arabidopsis thaliana.";
RL J. Biol. Chem. 278:17895-17900(2003).
RN [6]
RP GENE FAMILY, 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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor. Not active with 11-hydroxyjasmonate or 12-
CC hydroxyjasmonate. {ECO:0000269|PubMed:12637544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11158.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010697; BAB11158.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91097.1; -; Genomic_DNA.
DR EMBL; BT006241; AAP12890.1; -; mRNA.
DR EMBL; AK117202; BAC41878.1; -; mRNA.
DR RefSeq; NP_196317.2; NM_120782.4.
DR AlphaFoldDB; Q8GZ53; -.
DR SMR; Q8GZ53; -.
DR STRING; 3702.AT5G07000.1; -.
DR PaxDb; Q8GZ53; -.
DR PRIDE; Q8GZ53; -.
DR ProteomicsDB; 232548; -.
DR EnsemblPlants; AT5G07000.1; AT5G07000.1; AT5G07000.
DR GeneID; 830591; -.
DR Gramene; AT5G07000.1; AT5G07000.1; AT5G07000.
DR KEGG; ath:AT5G07000; -.
DR Araport; AT5G07000; -.
DR TAIR; locus:2169469; AT5G07000.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_1_1; -.
DR InParanoid; Q8GZ53; -.
DR OMA; NYFTPKQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q8GZ53; -.
DR BioCyc; ARA:AT5G07000-MON; -.
DR PRO; PR:Q8GZ53; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GZ53; baseline and differential.
DR Genevisible; Q8GZ53; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..347
FT /note="Cytosolic sulfotransferase 14"
FT /id="PRO_0000417061"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 87..92
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 310..312
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 39653 MW; 612BD77F7A92BF24 CRC64;
MAIPSFSMCH KPELLKEGKS EGQEEEGLSY EFQEMLDSLP KERGRRNRYL YLFQGFRCQA
KEIQAITSFQ KHFQSLPDDV VLATIPKSGT TWLKALTFTI LTRHRFDPVS SSSSDHPLLT
SNPHDLVPFF EYKLYANGNV PDLSGLASPR TFATHVPFGA LKDSVENPSV KVVYLCRNPF
DTFISMWHYI NNITSESVSA VLLDEAFDLY CRGLLIGFGP FWEHMLGYWR ESLKRPEKVL
FLKYEDLKED IETNLKKLAS FLGLPFTEEE EQKGVVKAIA DLCSFENLKK LEVNKSSKLI
QNYENRFLFR KGEVSDLVNY LSPSQVERLS ALVDDKLAGS GLTFRLS
