TPST_ARATH
ID TPST_ARATH Reviewed; 500 AA.
AC Q3EDG5; C7G3K4; Q9LN06;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein-tyrosine sulfotransferase;
DE EC=2.8.2.20 {ECO:0000269|PubMed:19666544};
DE AltName: Full=Tyrosylprotein sulfotransferase;
DE Flags: Precursor;
GN Name=TPST; OrderedLocusNames=At1g08030; ORFNames=T6D22.29;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19666544; DOI=10.1073/pnas.0902801106;
RA Komori R., Amano Y., Ogawa-Ohnishi M., Matsubayashi Y.;
RT "Identification of tyrosylprotein sulfotransferase in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15067-15072(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
CC -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC motifs of polypeptides. {ECO:0000269|PubMed:19666544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine
CC 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein];
CC Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20;
CC Evidence={ECO:0000269|PubMed:19666544};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19666544}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:19666544}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3EDG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EDG5-2; Sequence=VSP_038231, VSP_038232;
CC -!- TISSUE SPECIFICITY: Expressed throughout the plant body, highest levels
CC of expression are in the root apical meristem.
CC {ECO:0000269|PubMed:19666544}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX842536; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB511980; BAI22702.1; -; mRNA.
DR EMBL; AC026875; AAF79842.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28230.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57804.1; -; Genomic_DNA.
DR EMBL; BX842536; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B86215; B86215.
DR RefSeq; NP_001320287.1; NM_001331750.1. [Q3EDG5-1]
DR RefSeq; NP_563804.4; NM_100677.4. [Q3EDG5-1]
DR AlphaFoldDB; Q3EDG5; -.
DR BioGRID; 22559; 1.
DR STRING; 3702.AT1G08030.1; -.
DR PaxDb; Q3EDG5; -.
DR PRIDE; Q3EDG5; -.
DR ProteomicsDB; 232504; -. [Q3EDG5-1]
DR EnsemblPlants; AT1G08030.1; AT1G08030.1; AT1G08030. [Q3EDG5-1]
DR EnsemblPlants; AT1G08030.2; AT1G08030.2; AT1G08030. [Q3EDG5-1]
DR GeneID; 837318; -.
DR Gramene; AT1G08030.1; AT1G08030.1; AT1G08030. [Q3EDG5-1]
DR Gramene; AT1G08030.2; AT1G08030.2; AT1G08030. [Q3EDG5-1]
DR KEGG; ath:AT1G08030; -.
DR Araport; AT1G08030; -.
DR TAIR; locus:2205135; AT1G08030.
DR eggNOG; ENOG502QVVW; Eukaryota.
DR HOGENOM; CLU_038430_0_0_1; -.
DR InParanoid; Q3EDG5; -.
DR OMA; SCSPWKV; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q3EDG5; -.
DR BRENDA; 2.8.2.20; 399.
DR PRO; PR:Q3EDG5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3EDG5; baseline and differential.
DR Genevisible; Q3EDG5; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IDA:TAIR.
DR GO; GO:0055070; P:copper ion homeostasis; IMP:TAIR.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0010366; P:negative regulation of ethylene biosynthetic process; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..500
FT /note="Protein-tyrosine sulfotransferase"
FT /id="PRO_0000386565"
FT TOPO_DOM 25..467
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 326..327
FT /note="EA -> GW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_038231"
FT VAR_SEQ 328..500
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_038232"
FT CONFLICT 5..10
FT /note="SVWKLS -> PVLKLA (in Ref. 1; BAI22702)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="T -> R (in Ref. 1; BAI22702)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> I (in Ref. 1; BAI22702)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="A -> T (in Ref. 1; BAI22702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56989 MW; 06B1B2EBE2F07CCC CRC64;
MQMNSVWKLS LGLLLLSSVI GSFAELDFGH CETLVKKWAD SSSSREEHVN KDKRSLKDLL
FFLHVPRTGG RTYFHCFLRK LYDSSEECPR SYDKLHFNPR KEKCKLLATH DDYSLMAKLP
RERTSVMTIV RDPIARVLST YEFSVEVAAR FLVHPNLTSA SRMSSRIRKS NVISTLDIWP
WKYLVPWMRE DLFARRDARK LKEVVIIEDD NPYDMEEMLM PLHKYLDAPT AHDIIHNGAT
FQIAGLTNNS HLSEAHEVRH CVQKFKSLGE SVLQVAKRRL DSMLYVGLTE EHRESASLFA
NVVGSQVLSQ VVPSNATAKI KALKSEASVT ISETGSDKSN IQNGTSEVTL NKAEAKSGNM
TVKTLMEVYE GCITHLRKSQ GTRRVNSLKR ITPANFTRGT RTRVPKEVIQ QIKSLNNLDV
ELYKYAKVIF AKEHELVSNK LISSSKRSIV DLPSELKSVL GEMGEEKLWK FVPVALMLLL
IVLFFLFVNA KRRRTSKVKI
