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Sulfotransferase 1A3 (ST1A3) (EC 2.8.2.1) (Aryl sulfotransferase 1A3/1A4) (Catecholamine-sulfating phenol sulfotransferase) (HAST3) (M-PST) (Monoamine-sulfating phenol sulfotransferase) (Placental estrogen sulfotransferase) (Sulfotransferase 1A3/1A4) (Sulfotransferase, monoamine-preferring) (Thermolabile phenol sulfotransferase) (TL-PST)

 ST1A3_HUMAN             Reviewed;         295 AA.
P0DMM9; B4DNV0; O95603; P50224; Q1ET66; Q6ZWJ5;
03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
03-SEP-2014, sequence version 1.
27-SEP-2017, entry version 33.
RecName: Full=Sulfotransferase 1A3;
Short=ST1A3;
EC=2.8.2.1;
AltName: Full=Aryl sulfotransferase 1A3/1A4;
AltName: Full=Catecholamine-sulfating phenol sulfotransferase;
AltName: Full=HAST3;
AltName: Full=M-PST;
AltName: Full=Monoamine-sulfating phenol sulfotransferase;
AltName: Full=Placental estrogen sulfotransferase;
AltName: Full=Sulfotransferase 1A3/1A4;
AltName: Full=Sulfotransferase, monoamine-preferring;
AltName: Full=Thermolabile phenol sulfotransferase;
Short=TL-PST;
Name=SULT1A3; Synonyms=STM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8363592; DOI=10.1006/bbrc.1993.2018;
Zhu X., Veronese M.E., Bernard C.C., Sansom L.N., McManus M.E.;
"Identification of two human brain aryl sulfotransferase cDNAs.";
Biochem. Biophys. Res. Commun. 195:120-127(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8187949; DOI=10.1016/0303-7207(94)90159-7;
Bernier F., Lopez-Solache I., Labrie F., Luu-The V.;
"Cloning and expression of cDNA encoding human placental estrogen
sulfotransferase.";
Mol. Cell. Endocrinol. 99:R11-R15(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=7802665; DOI=10.1006/bbrc.1994.2810;
Dooley T.P., Probst P., Munroe P.B., Mole S.E., Liu Z., Doggett N.A.;
"Genomic organization and DNA sequence of the human catecholamine-
sulfating phenol sulfotransferase gene (STM).";
Biochem. Biophys. Res. Commun. 205:1325-1332(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 84-101.
TISSUE=Liver;
PubMed=8117269; DOI=10.1006/bbrc.1994.1159;
Wood T.C., Aksoy I.A., Aksoy S., Weinshilboum R.M.;
"Human liver thermolabile phenol sulfotransferase: cDNA cloning,
expression and characterization.";
Biochem. Biophys. Res. Commun. 198:1119-1127(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Platelet;
PubMed=7695637; DOI=10.1006/bbrc.1995.1406;
Aksoy I.A., Weinshilboum R.M.;
"Human thermolabile phenol sulfotransferase gene (STM): molecular
cloning and structural characterization.";
Biochem. Biophys. Res. Commun. 208:786-795(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=7695643; DOI=10.1006/bbrc.1995.1414;
Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H.;
"Human platelet phenolsulfotransferases: cDNA cloning, stable
expression in V79 cells and identification of a novel allelic variant
of the phenol-sulfating form.";
Biochem. Biophys. Res. Commun. 208:855-862(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Leukocyte;
PubMed=7961757;
Bernier F., Leblanc G., Labrie F., Luu-The V.;
"Structure of human estrogen and aryl sulfotransferase gene. Two mRNA
species issued from a single gene.";
J. Biol. Chem. 269:28200-28205(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Gaedigk A., Grant D.M.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Kidney;
Terazawa R., Shimada M., Nagata K., Yamazoe Y.;
"Isolation of seven variants of catecholamine sulfotransferase cDNAs
from human kidney.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-198.
TISSUE=Lymphocyte;
PubMed=7829089; DOI=10.1006/geno.1994.1494;
Aksoy I.A., Callen D.F., Apostolou S., Her C., Weinshilboum R.M.;
"Thermolabile phenol sulfotransferase gene (STM): localization to
human chromosome 16p11.2.";
Genomics 23:275-277(1994).
[14]
CHARACTERIZATION.
PubMed=8093002; DOI=10.1042/bj3020497;
Veronese M.E., Burgess W., Zhu X., McManus M.E.;
"Functional characterization of two human sulphotransferase cDNAs that
encode monoamine- and phenol-sulphating forms of phenol
sulphotransferase: substrate kinetics, thermal-stability and
inhibitor-sensitivity studies.";
Biochem. J. 302:497-502(1994).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
TISSUE=Brain;
PubMed=10543947; DOI=10.1006/jmbi.1999.3153;
Bidwell L.M., McManus M.E., Gaedigk A., Kakuta Y., Negishi M.,
Pedersen L., Martin J.L.;
"Crystal structure of human catecholamine sulfotransferase.";
J. Mol. Biol. 293:521-530(1999).
[17]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH
ADENOSINE-3'-5'-DIPHOSPHATE AND L-DOPAMINE.
PubMed=16083857; DOI=10.1016/j.bbrc.2005.07.091;
Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., Chang W.R.;
"Crystal structure of human sulfotransferase SULT1A3 in complex with
dopamine and 3'-phosphoadenosine 5'-phosphate.";
Biochem. Biophys. Res. Commun. 335:417-423(2005).
[18]
VARIANT ASN-234, AND CHARACTERIZATION OF VARIANT ASN-234.
PubMed=14622112; DOI=10.1046/j.1471-4159.2003.02027.x;
Thomae B.A., Rifki O.F., Theobald M.A., Eckloff B.W., Wieben E.D.,
Weinshilboum R.M.;
"Human catecholamine sulfotransferase (SULT1A3) pharmacogenetics:
functional genetic polymorphism.";
J. Neurochem. 87:809-819(2003).
[19]
VARIANTS LEU-101; HIS-101 AND CYS-144, AND CHARACTERIZATION OF
VARIANTS LEU-101; HIS-101 AND CYS-144.
PubMed=15358107; DOI=10.1016/j.bbrc.2004.07.038;
Hildebrandt M.A.T., Salavaggione O.E., Martin Y.N., Flynn H.C.,
Jalal S., Wieben E.D., Weinshilboum R.M.;
"Human SULT1A3 pharmacogenetics: gene duplication and functional
genomic studies.";
Biochem. Biophys. Res. Commun. 321:870-878(2004).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the sulfate
conjugation of phenolic monoamines (neurotransmitters such as
dopamine, norepinephrine and serotonin) and phenolic and catechol
drugs.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + a phenol =
adenosine 3',5'-bisphosphate + an aryl sulfate.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16083857}.
-!- INTERACTION:
Q5VWX1:KHDRBS2; NbExp=3; IntAct=EBI-10196922, EBI-742808;
Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-10196922, EBI-740897;
P34896:SHMT1; NbExp=3; IntAct=EBI-10196922, EBI-715117;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P0DMM9-1; Sequence=Displayed;
Name=2;
IsoId=P0DMM9-2; Sequence=VSP_012326;
Note=No experimental confirmation available. Ref.10 (BAC85507)
sequence differs from that shown due to a frameshift in position
101. {ECO:0000305};
Name=3;
IsoId=P0DMM9-3; Sequence=VSP_047771;
-!- TISSUE SPECIFICITY: Liver, colon, kidney, lung, brain, spleen,
small intestine, placenta and leukocyte.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
-!- CAUTION: Found in a segmental duplication on p arm of chromosome
16 giving rise to two identical copies of this gene sharing exons
with SLX1A and SLX1B. The ORFs of SULT1A3 and SULT1A4 differ with
only a single nucleotide change that does not alter the encoded
amino acid. It is not possible to determine whether any individual
polymorphism is present within SULT1A3 or SULT1A4
(PubMed:15358107). {ECO:0000305|PubMed:15358107}.
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EMBL; L19956; AAA02943.1; -; mRNA.
EMBL; L25275; AAA36523.1; -; mRNA.
EMBL; L19956; AAA17723.1; -; mRNA.
EMBL; U20499; AAA64490.1; -; Genomic_DNA.
EMBL; X84653; CAA59146.1; -; mRNA.
EMBL; L34160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U37686; AAA86536.1; -; Genomic_DNA.
EMBL; U34199; AAC99987.1; -; mRNA.
EMBL; AK122733; BAC85507.1; ALT_FRAME; mRNA.
EMBL; AK298073; BAG60362.1; -; mRNA.
EMBL; AC106782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB111094; BAE94928.1; -; mRNA.
EMBL; BC014471; AAH14471.1; -; mRNA.
EMBL; BC078144; AAH78144.1; -; mRNA.
EMBL; U08099; AAA82126.1; -; Genomic_DNA.
CCDS; CCDS10674.1; -. [P0DMM9-1]
PIR; A55451; A55451.
RefSeq; NP_001017390.1; NM_001017390.2. [P0DMM9-1]
RefSeq; NP_808220.1; NM_177552.3. [P0DMM9-1]
RefSeq; XP_011506903.1; XM_011508601.1. [P0DMM9-3]
RefSeq; XP_016855108.1; XM_016999619.1. [P0DMM9-1]
UniGene; Hs.460558; -.
UniGene; Hs.744871; -.
PDB; 1CJM; X-ray; 2.40 A; A=1-295.
PDB; 2A3R; X-ray; 2.60 A; A/B=1-295.
PDBsum; 1CJM; -.
PDBsum; 2A3R; -.
DisProt; DP00011; -.
ProteinModelPortal; P0DMM9; -.
SMR; P0DMM9; -.
BioGrid; 112687; 13.
BioGrid; 138644; 4.
IntAct; P0DMM9; 4.
STRING; 9606.ENSP00000343645; -.
ChEMBL; CHEMBL1743293; -.
iPTMnet; P0DMM9; -.
PhosphoSitePlus; P0DMM9; -.
DMDM; 1711609; -.
PaxDb; P0DMM9; -.
PeptideAtlas; P0DMM9; -.
PRIDE; P0DMM9; -.
TopDownProteomics; P0DMM9-2; -. [P0DMM9-2]
DNASU; 445329; -.
DNASU; 6818; -.
Ensembl; ENST00000338971; ENSP00000343645; ENSG00000261052. [P0DMM9-1]
Ensembl; ENST00000395138; ENSP00000378570; ENSG00000261052. [P0DMM9-1]
Ensembl; ENST00000563322; ENSP00000454518; ENSG00000261052. [P0DMM9-3]
GeneID; 105369243; -.
GeneID; 445329; -.
GeneID; 6818; -.
KEGG; hsa:105369243; -.
KEGG; hsa:445329; -.
KEGG; hsa:6818; -.
UCSC; uc010bzt.4; human. [P0DMM9-1]
CTD; 445329; -.
CTD; 6818; -.
DisGeNET; 105369243; -.
DisGeNET; 445329; -.
DisGeNET; 6818; -.
EuPathDB; HostDB:ENSG00000261052.5; -.
GeneCards; SULT1A3; -.
HGNC; HGNC:11455; SULT1A3.
HPA; HPA049500; -.
HPA; HPA051051; -.
MIM; 600641; gene.
neXtProt; NX_P0DMM9; -.
OpenTargets; ENSG00000261052; -.
eggNOG; KOG1584; Eukaryota.
eggNOG; ENOG4111H56; LUCA.
GeneTree; ENSGT00760000118932; -.
HOVERGEN; HBG001195; -.
KO; K01014; -.
OMA; QNFFKAR; -.
PhylomeDB; P0DMM9; -.
TreeFam; TF321745; -.
Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
PRO; PR:P0DMM9; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000261052; -.
CleanEx; HS_SULT1A3; -.
CleanEx; HS_SULT1A4; -.
ExpressionAtlas; P0DMM9; baseline and differential.
Genevisible; P0DMM9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0047685; F:amine sulfotransferase activity; IDA:CAFA.
GO; GO:0004062; F:aryl sulfotransferase activity; IMP:CACAO.
GO; GO:0043199; F:sulfate binding; IDA:CAFA.
GO; GO:0008146; F:sulfotransferase activity; IDA:BHF-UCL.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
GO; GO:0097720; P:calcineurin-mediated signaling; IDA:CAFA.
GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
GO; GO:0042420; P:dopamine catabolic process; IDA:CAFA.
GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:CAFA.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
GO; GO:0009812; P:flavonoid metabolic process; IDA:BHF-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:1901215; P:negative regulation of neuron death; IMP:CAFA.
GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; IDA:CAFA.
GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:BHF-UCL.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Catecholamine metabolism;
Complete proteome; Cytoplasm; Direct protein sequencing;
Lipid metabolism; Polymorphism; Reference proteome;
Steroid metabolism; Transferase.
CHAIN 1 295 Sulfotransferase 1A3.
/FTId=PRO_0000085159.
NP_BIND 48 53 PAPS.
NP_BIND 227 232 PAPS.
NP_BIND 257 259 PAPS.
REGION 106 108 Substrate binding.
ACT_SITE 108 108 Proton acceptor. {ECO:0000250}.
BINDING 86 86 Substrate.
BINDING 130 130 PAPS.
BINDING 138 138 PAPS.
BINDING 146 146 Substrate.
BINDING 193 193 PAPS.
VAR_SEQ 167 295 VSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKI
LEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELM
DHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSL
SFRSEL -> GGLDWRKEGVKPRGGGYNVQQPCVGAPCPLL
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012326.
VAR_SEQ 198 198 E -> EEPSAAQ (in isoform 3).
{ECO:0000303|Ref.9}.
/FTId=VSP_047771.
VARIANT 101 101 P -> H (decreases levels of
sulfotransferase activity).
{ECO:0000269|PubMed:15358107}.
/FTId=VAR_071108.
VARIANT 101 101 P -> L (decreases levels of
sulfotransferase activity;
dbSNP:rs751527244).
{ECO:0000269|PubMed:15358107}.
/FTId=VAR_071109.
VARIANT 144 144 R -> C (no effect on sulfotransferase
activity). {ECO:0000269|PubMed:15358107}.
/FTId=VAR_071110.
VARIANT 234 234 K -> N (decreases levels of
sulfotransferase activity; accelerates
proteasome-dependent degradation).
{ECO:0000269|PubMed:14622112}.
/FTId=VAR_071111.
CONFLICT 220 225 MDFMVQ -> VDLMVE (in Ref. 8; AAC99987).
{ECO:0000305}.
CONFLICT 235 235 N -> T (in Ref. 8; AAC99987).
{ECO:0000305}.
CONFLICT 244 245 PQ -> RR (in Ref. 8; AAC99987).
{ECO:0000305}.
CONFLICT 290 290 S -> T (in Ref. 8; AAC99987).
{ECO:0000305}.
STRAND 12 15 {ECO:0000244|PDB:1CJM}.
STRAND 18 21 {ECO:0000244|PDB:1CJM}.
HELIX 22 27 {ECO:0000244|PDB:1CJM}.
HELIX 30 33 {ECO:0000244|PDB:1CJM}.
STRAND 41 45 {ECO:0000244|PDB:1CJM}.
HELIX 51 62 {ECO:0000244|PDB:1CJM}.
TURN 63 65 {ECO:0000244|PDB:2A3R}.
HELIX 67 70 {ECO:0000244|PDB:2A3R}.
HELIX 75 78 {ECO:0000244|PDB:2A3R}.
TURN 95 98 {ECO:0000244|PDB:1CJM}.
STRAND 104 107 {ECO:0000244|PDB:1CJM}.
HELIX 111 113 {ECO:0000244|PDB:1CJM}.
HELIX 116 120 {ECO:0000244|PDB:1CJM}.
STRAND 124 129 {ECO:0000244|PDB:1CJM}.
HELIX 132 145 {ECO:0000244|PDB:1CJM}.
HELIX 155 163 {ECO:0000244|PDB:1CJM}.
HELIX 172 182 {ECO:0000244|PDB:1CJM}.
TURN 183 185 {ECO:0000244|PDB:1CJM}.
STRAND 188 192 {ECO:0000244|PDB:1CJM}.
HELIX 193 198 {ECO:0000244|PDB:1CJM}.
HELIX 200 211 {ECO:0000244|PDB:1CJM}.
HELIX 217 226 {ECO:0000244|PDB:2A3R}.
HELIX 229 234 {ECO:0000244|PDB:2A3R}.
TURN 236 238 {ECO:0000244|PDB:2A3R}.
TURN 245 247 {ECO:0000244|PDB:2A3R}.
TURN 250 252 {ECO:0000244|PDB:2A3R}.
HELIX 264 266 {ECO:0000244|PDB:1CJM}.
HELIX 270 283 {ECO:0000244|PDB:1CJM}.
SEQUENCE 295 AA; 34196 MW; ECDDEC03DBE30D46 CRC64;
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM
IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD
QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY
TTVPQELMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL


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