TPST2_HUMAN
ID TPST2_HUMAN Reviewed; 377 AA.
AC O60704; B3KQA7; Q6FI98; Q9H0V4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein-tyrosine sulfotransferase 2;
DE EC=2.8.2.20 {ECO:0000269|PubMed:9733778};
DE AltName: Full=Tyrosylprotein sulfotransferase 2;
DE Short=TPST-2;
GN Name=TPST2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9736702; DOI=10.1073/pnas.95.19.11134;
RA Beisswanger R., Corbeil D., Vannier C., Thiele C., Dohrmann U., Kellner R.,
RA Ashman K., Niehrs C., Huttner W.B.;
RT "Existence of distinct tyrosylprotein sulfotransferase genes: molecular
RT characterization of tyrosylprotein sulfotransferase-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11134-11139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=9733778; DOI=10.1074/jbc.273.38.24770;
RA Ouyang Y.-B., Moore K.L.;
RT "Molecular cloning and expression of human and mouse tyrosylprotein
RT sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 273:24770-24774(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bennett E.P.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH TPST1.
RX PubMed=25660941; DOI=10.1016/j.jmb.2015.01.021;
RA Hartmann-Fatu C., Trusch F., Moll C.N., Michin I., Hassinen A.,
RA Kellokumpu S., Bayer P.;
RT "Heterodimers of tyrosylprotein sulfotransferases suggest existence of a
RT higher organization level of transferases in the membrane of the trans-
RT Golgi apparatus.";
RL J. Mol. Biol. 427:1404-1412(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 43-359 IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE AND SUBSTRATE PEPTIDE, DISULFIDE BONDS, SUBUNIT, ACTIVE
RP SITE, AND MUTAGENESIS OF ARG-78; GLU-99; ARG-101; TRP-113; LYS-158; THR-198
RP AND SER-285.
RX PubMed=23481380; DOI=10.1038/ncomms2593;
RA Teramoto T., Fujikawa Y., Kawaguchi Y., Kurogi K., Soejima M., Adachi R.,
RA Nakanishi Y., Mishiro-Sato E., Liu M.C., Sakakibara Y., Suiko M.,
RA Kimura M., Kakuta Y.;
RT "Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the
RT mechanism of protein tyrosine sulfation reaction.";
RL Nat. Commun. 4:1572-1572(2013).
CC -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as
CC cosubstrate. {ECO:0000269|PubMed:9733778}.
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:9733778};
CC -!- SUBUNIT: Homodimer (PubMed:23481380). Can also form heterodimers with
CC TPST1 (PubMed:25660941). {ECO:0000269|PubMed:23481380,
CC ECO:0000269|PubMed:25660941}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:25660941}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:25660941}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9733778,
CC ECO:0000269|PubMed:9736702}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9733778}.
CC -!- MISCELLANEOUS: Substrate peptides must be flexible in order to adopt an
CC L-shaped conformation in the deep binding cleft.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AF061254; AAC34296.1; -; mRNA.
DR EMBL; AF049891; AAC36061.1; -; mRNA.
DR EMBL; AJ006198; CAA06906.1; -; mRNA.
DR EMBL; AL136623; CAB66558.1; -; mRNA.
DR EMBL; CR456597; CAG30483.1; -; mRNA.
DR EMBL; CR533528; CAG38559.1; -; mRNA.
DR EMBL; AK074538; BAG51969.1; -; mRNA.
DR EMBL; AK075139; BAG52071.1; -; mRNA.
DR EMBL; Z95115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59726.1; -; Genomic_DNA.
DR EMBL; BC001057; AAH01057.1; -; mRNA.
DR EMBL; BC017509; AAH17509.1; -; mRNA.
DR CCDS; CCDS13839.1; -.
DR RefSeq; NP_001008566.1; NM_001008566.1.
DR RefSeq; NP_003586.3; NM_003595.3.
DR PDB; 3AP1; X-ray; 1.90 A; A/B=43-359.
DR PDB; 3AP2; X-ray; 2.40 A; A/B=43-359.
DR PDB; 3AP3; X-ray; 3.50 A; A/B/C/D=43-377.
DR PDBsum; 3AP1; -.
DR PDBsum; 3AP2; -.
DR PDBsum; 3AP3; -.
DR AlphaFoldDB; O60704; -.
DR SMR; O60704; -.
DR BioGRID; 114037; 117.
DR IntAct; O60704; 10.
DR STRING; 9606.ENSP00000339813; -.
DR BindingDB; O60704; -.
DR ChEMBL; CHEMBL3178; -.
DR GlyGen; O60704; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O60704; -.
DR PhosphoSitePlus; O60704; -.
DR BioMuta; TPST2; -.
DR EPD; O60704; -.
DR jPOST; O60704; -.
DR MassIVE; O60704; -.
DR MaxQB; O60704; -.
DR PaxDb; O60704; -.
DR PeptideAtlas; O60704; -.
DR PRIDE; O60704; -.
DR ProteomicsDB; 49532; -.
DR Antibodypedia; 10022; 202 antibodies from 27 providers.
DR DNASU; 8459; -.
DR Ensembl; ENST00000338754.9; ENSP00000339813.4; ENSG00000128294.16.
DR Ensembl; ENST00000398110.6; ENSP00000381180.2; ENSG00000128294.16.
DR Ensembl; ENST00000403880.5; ENSP00000385192.1; ENSG00000128294.16.
DR GeneID; 8459; -.
DR KEGG; hsa:8459; -.
DR MANE-Select; ENST00000338754.9; ENSP00000339813.4; NM_003595.5; NP_003586.3.
DR UCSC; uc003acw.4; human.
DR CTD; 8459; -.
DR DisGeNET; 8459; -.
DR GeneCards; TPST2; -.
DR HGNC; HGNC:12021; TPST2.
DR HPA; ENSG00000128294; Tissue enhanced (pancreas).
DR MIM; 603126; gene.
DR neXtProt; NX_O60704; -.
DR OpenTargets; ENSG00000128294; -.
DR PharmGKB; PA36700; -.
DR VEuPathDB; HostDB:ENSG00000128294; -.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_1_1; -.
DR InParanoid; O60704; -.
DR OMA; DSNHVEY; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; O60704; -.
DR TreeFam; TF312910; -.
DR BRENDA; 2.8.2.20; 2681.
DR PathwayCommons; O60704; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR Reactome; R-HSA-9674519; Defective F8 sulfation at Y1699.
DR SignaLink; O60704; -.
DR BioGRID-ORCS; 8459; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; TPST2; human.
DR EvolutionaryTrace; O60704; -.
DR GenomeRNAi; 8459; -.
DR Pharos; O60704; Tbio.
DR PRO; PR:O60704; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O60704; protein.
DR Bgee; ENSG00000128294; Expressed in body of pancreas and 177 other tissues.
DR ExpressionAtlas; O60704; baseline and differential.
DR Genevisible; O60704; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026634; TPST.
DR PANTHER; PTHR12788; PTHR12788; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="Protein-tyrosine sulfotransferase 2"
FT /id="PRO_0000189829"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 101..105
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000269|PubMed:23481380"
FT ACT_SITE 99
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23481380"
FT BINDING 78..82
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 191
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 195
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 238
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 285..294
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT BINDING 300
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT SITE 158
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:23481380"
FT SITE 285
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:23481380"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..156
FT /evidence="ECO:0000269|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT DISULFID 225..233
FT /evidence="ECO:0000269|PubMed:23481380,
FT ECO:0007744|PDB:3AP1, ECO:0007744|PDB:3AP2,
FT ECO:0007744|PDB:3AP3"
FT MUTAGEN 78
FT /note="R->A: Strongly reduced enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 99
FT /note="E->A: Loss of sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 101
FT /note="R->A: Prevents dimerization and strongly decreases
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 113
FT /note="W->A: Prevents dimerization and decreases enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 158
FT /note="K->A: Nearly complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 198
FT /note="T->A: Slightly decreased sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT MUTAGEN 285
FT /note="S->A: Abolishes sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:23481380"
FT CONFLICT 26
FT /note="Q -> L (in Ref. 4; CAB66558 and 6; CAG38559)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="V -> E (in Ref. 4; CAB66558 and 6; CAG38559)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> M (in Ref. 6; CAG38559)"
FT /evidence="ECO:0000305"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3AP2"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3AP2"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 207..228
FT /evidence="ECO:0007829|PDB:3AP1"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3AP3"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:3AP1"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:3AP1"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3AP1"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:3AP1"
SQ SEQUENCE 377 AA; 41912 MW; A658E50151FDBC12 CRC64;
MRLSVRRVLL AAGCALVLVL AVQLGQQVLE CRAVLAGLRS PRGAMRPEQE ELVMVGTNHV
EYRYGKAMPL IFVGGVPRSG TTLMRAMLDA HPEVRCGEET RIIPRVLAMR QAWSKSGREK
LRLDEAGVTD EVLDAAMQAF ILEVIAKHGE PARVLCNKDP FTLKSSVYLS RLFPNSKFLL
MVRDGRASVH SMITRKVTIA GFDLSSYRDC LTKWNKAIEV MYAQCMEVGK EKCLPVYYEQ
LVLHPRRSLK LILDFLGIAW SDAVLHHEDL IGKPGGVSLS KIERSTDQVI KPVNLEALSK
WTGHIPGDVV RDMAQIAPML AQLGYDPYAN PPNYGNPDPF VINNTQRVLK GDYKTPANLK
GYFQVNQNST SSHLGSS
