P50224 (ST1A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfotransferase 1A3/1A4
Short name=ST1A3/ST1A4
EC=2.8.2.1

Alternative name(s):
Aryl sulfotransferase 1A3/1A4
Catecholamine-sulfating phenol sulfotransferase
HAST3
M-PST
Monoamine-sulfating phenol sulfotransferase
Placental estrogen sulfotransferase
Sulfotransferase, monoamine-preferring
Thermolabile phenol sulfotransferase
Short name=TL-PST

Gene names

Name:	SULT1A3
Synonyms:	STM
AND
Name:	SULT1A4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the sulfotransferase 1 family.
Sequence caution	Isoform 2: The sequence BAC85507.1 differs from that shown. Reason: Frameshift at position 101.

Ontologies

Keywords
Biological process	Catecholamine metabolism Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW flavonoid metabolic process Inferred from direct assay PubMed 20056724. Source: BHF-UCL steroid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL xenobiotic metabolic process Inferred from direct assay PubMed 20056724. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	aryl sulfotransferase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50224-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P50224-2)

The sequence of this isoform differs from the canonical sequence as follows:
     167-295: VSYGSWYQHV...GCSLSFRSEL → GGLDWRKEGVKPRGGGYNVQQPCVGAPCPLL

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Sulfotransferase 1A3/1A4

PRO_0000085159

Regions

Nucleotide binding

48 – 53

6

PAPS

Nucleotide binding

227 – 232

6

PAPS

Nucleotide binding

257 – 259

3

PAPS

Region

106 – 108

3

Substrate binding

Sites

Active site

108

1

Proton acceptor By similarity

Binding site

86

1

Substrate

Binding site

130

1

PAPS

Binding site

138

1

PAPS

Binding site

146

1

Substrate

Binding site

193

1

PAPS

Natural variations

Alternative sequence

167 – 295

129

VSYGS…FRSEL → GGLDWRKEGVKPRGGGYNVQ QPCVGAPCPLL in isoform 2.

VSP_012326

Experimental info

Sequence conflict

220 – 225

6

MDFMVQ → VDLMVE in AAC99987. Ref.8

Sequence conflict

235

1

N → T in AAC99987. Ref.8

Sequence conflict

244 – 245

2

PQ → RR in AAC99987. Ref.8

Sequence conflict

290

1

S → T in AAC99987. Ref.8

Secondary structure

1

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295

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Beta strand

18 – 21

4

Helix

22 – 27

6

Helix

30 – 33

4

Beta strand

41 – 45

5

Helix

51 – 62

12

Turn

63 – 65

3

Helix

67 – 70

4

Helix

75 – 78

4

Turn

95 – 98

4

Beta strand

104 – 107

4

Helix

111 – 113

3

Helix

116 – 120

5

Beta strand

124 – 129

6

Helix

132 – 145

14

Helix

155 – 163

9

Helix

172 – 182

11

Turn

183 – 185

3

Beta strand

188 – 192

5

Helix

193 – 198

6

Helix

200 – 211

12

Helix

217 – 226

10

Helix

229 – 234

6

Turn

236 – 238

3

Turn

245 – 247

3

Turn

250 – 252

3

Helix

264 – 266

3

Helix

270 – 283

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: ECDDEC03DBE30D46	FASTA	295	34,196
	10 20 30 40 50 60 MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM 70 80 90 100 110 120 IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD 130 140 150 160 170 180 QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW 190 200 210 220 230 240 ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY 250 260 270 280 290 TTVPQELMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
	Isoform 2 [UniParc]. Checksum: 44C5F13EDA71BC1D	FASTA	197	22,069
	10 20 30 40 50 60 MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM 70 80 90 100 110 120 IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD 130 140 150 160 170 180 QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEGGLD WRKEGVKPRG 190 GGYNVQQPCV GAPCPLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two human brain aryl sulfotransferase cDNAs." Zhu X., Veronese M.E., Bernard C.C., Sansom L.N., McManus M.E. Biochem. Biophys. Res. Commun. 195:120-127(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Cloning and expression of cDNA encoding human placental estrogen sulfotransferase." Bernier F., Lopez-Solache I., Labrie F., Luu-The V. Mol. Cell. Endocrinol. 99:R11-R15(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM)." Dooley T.P., Probst P., Munroe P.B., Mole S.E., Liu Z., Doggett N.A. Biochem. Biophys. Res. Commun. 205:1325-1332(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization." Wood T.C., Aksoy I.A., Aksoy S., Weinshilboum R.M. Biochem. Biophys. Res. Commun. 198:1119-1127(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-101. Tissue: Liver.
[5]	"Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization." Aksoy I.A., Weinshilboum R.M. Biochem. Biophys. Res. Commun. 208:786-795(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Platelet.
[6]	"Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form." Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H. Biochem. Biophys. Res. Commun. 208:855-862(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Blood.
[7]	"Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene." Bernier F., Leblanc G., Labrie F., Luu-The V. J. Biol. Chem. 269:28200-28205(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Leukocyte.
[8]	Gaedigk A., Grant D.M. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung and Pancreas.
[11]	"Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2." Aksoy I.A., Callen D.F., Apostolou S., Her C., Weinshilboum R.M. Genomics 23:275-277(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-198. Tissue: Lymphocyte.
[12]	"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." Veronese M.E., Burgess W., Zhu X., McManus M.E. Biochem. J. 302:497-502(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Crystal structure of human catecholamine sulfotransferase." Bidwell L.M., McManus M.E., Gaedigk A., Kakuta Y., Negishi M., Pedersen L., Martin J.L. J. Mol. Biol. 293:521-530(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). Tissue: Brain.
[15]	"Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate." Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., Chang W.R. Biochem. Biophys. Res. Commun. 335:417-423(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND L-DOPAMINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L19956 mRNA. Translation: AAA02943.1.
L25275 mRNA. Translation: AAA36523.1.
U08032 mRNA. Translation: AAA17723.1.
U20499 Genomic DNA. Translation: AAA64490.1.
X84653 mRNA. Translation: CAA59146.1.
L34160 Genomic DNA. No translation available.
U37686 Genomic DNA. Translation: AAA86536.1.
U34199 mRNA. Translation: AAC99987.1.
AK122733 mRNA. Translation: BAC85507.1. Frameshift.
AK298073 mRNA. Translation: BAG60362.1.
BC014471 mRNA. Translation: AAH14471.1.
BC078144 mRNA. Translation: AAH78144.1.
U08099 Genomic DNA. Translation: AAA82126.1.

IPI

IPI00030730.
IPI00446834.

PIR

A55451.

RefSeq

NP_001017390.1. NM_001017390.2.
NP_808220.1. NM_177552.3.
XP_003960686.1. XM_003960637.1.
XP_003960687.1. XM_003960638.1.

UniGene

Hs.460558.
Hs.741198.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CJM	X-ray	2.40	A	1-295	[»]
2A3R	X-ray	2.60	A/B	1-295	[»]

DisProt

DP00011.

ProteinModelPortal

P50224.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000339221.

PTM databases

PhosphoSite

P50224.

2D gel databases

OGP

P50224.

Proteomic databases

PRIDE

P50224.

Protocols and materials databases

DNASU

445329.
6818.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338971; ENSP00000343645; ENSG00000261052.
ENST00000344620; ENSP00000339221; ENSG00000213648.
ENST00000354723; ENSP00000346760; ENSG00000261052.
ENST00000355544; ENSP00000347739; ENSG00000261052.
ENST00000360423; ENSP00000353600; ENSG00000213648.
ENST00000395137; ENSP00000378569; ENSG00000261052.
ENST00000395138; ENSP00000378570; ENSG00000261052.
ENST00000395400; ENSP00000378796; ENSG00000213648.

GeneID

101060714.
445329.
6818.

KEGG

hsa:101060714.
hsa:445329.
hsa:6818.

UCSC

uc002dsw.3. human.
uc010vdp.2. human.

Organism-specific databases

CTD

445329.
6818.

GeneCards

GC16P029466.
GC16P030206.

HGNC

HGNC:11455. SULT1A3.
HGNC:30004. SULT1A4.

MIM

600641. gene.

neXtProt

NX_P50224.

PharmGKB

PA344.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

KO

K01014.

OMA

PPRLIKS.

OrthoDB

EOG4255T9.

PhylomeDB

P50224.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05608-MONOMER.

BRENDA

2.8.2.1. 2681.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

SABIO-RK

P50224.

Gene expression databases

ArrayExpress

P50224.

Bgee

P50224.

CleanEx

HS_SULT1A3.
HS_SULT1A4.

Genevestigator

P50224.

GermOnline

ENSG00000132207. Homo sapiens.
ENSG00000181625. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1743293.

EvolutionaryTrace

P50224.

NextBio

111370.

SOURCE

Search...

Entry information

Entry name

ST1A3_HUMAN

Accession

Primary (citable) accession number: P50224
Secondary accession number(s): B4DNV0, O95603, Q6ZWJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.