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Protein

Estrogen sulfotransferase, testis isoform

Gene

Sult1e1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol.1 Publication

Catalytic activityi

3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Proton acceptor1 Publication
Binding sitei130 – 1301PAPS
Binding sitei138 – 1381PAPS
Binding sitei193 – 1931PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 536PAPS
Nucleotide bindingi227 – 2326PAPS
Nucleotide bindingi257 – 2593PAPS

GO - Molecular functioni

GO - Biological processi

  • estrogen metabolic process Source: UniProtKB
  • female pregnancy Source: MGI
  • positive regulation of fat cell differentiation Source: MGI
  • sulfation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Lipid-binding, Steroid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Estrogen sulfotransferase, testis isoform (EC:2.8.2.4)
Alternative name(s):
Sulfotransferase 1E1
Short name:
ST1E1
Sulfotransferase, estrogen-preferring
Gene namesi
Name:Sult1e1
Synonyms:Ste
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:98431. Sult1e1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481K → M: Loss of enzyme activity. 1 Publication
Mutagenesisi48 – 481K → R: Reduced enzyme activity. 1 Publication
Mutagenesisi106 – 1061K → A: Strongly reduced enzyme activity. Strongly reduced affinity for estradiol. 1 Publication
Mutagenesisi106 – 1061K → R or S: Strongly reduced enzyme activity. Strongly reduced affinity for estradiol. 1 Publication
Mutagenesisi108 – 1081H → K, L, S or R: Loss of enzyme activity. 1 Publication
Mutagenesisi240 – 2401Y → F: Slightly decreased enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Estrogen sulfotransferase, testis isoformPRO_0000085154Add
BLAST

Proteomic databases

MaxQBiP49891.
PaxDbiP49891.
PRIDEiP49891.

PTM databases

PhosphoSiteiP49891.

Expressioni

Tissue specificityi

Testis and at very low level in the placenta.

Gene expression databases

CleanExiMM_SULT1E1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP49891. 1 interaction.
STRINGi10090.ENSMUSP00000031201.

Chemistry

BindingDBiP49891.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Beta strandi12 – 154Combined sources
Beta strandi18 – 214Combined sources
Helixi22 – 243Combined sources
Turni25 – 273Combined sources
Helixi28 – 325Combined sources
Beta strandi41 – 455Combined sources
Helixi51 – 6212Combined sources
Turni63 – 653Combined sources
Helixi75 – 784Combined sources
Turni87 – 893Combined sources
Helixi92 – 976Combined sources
Beta strandi104 – 1074Combined sources
Helixi111 – 1133Combined sources
Helixi116 – 1205Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 14514Combined sources
Helixi155 – 16410Combined sources
Helixi172 – 18211Combined sources
Beta strandi188 – 1925Combined sources
Helixi193 – 1986Combined sources
Helixi200 – 21011Combined sources
Helixi217 – 22610Combined sources
Helixi229 – 2346Combined sources
Turni236 – 2427Combined sources
Turni245 – 2473Combined sources
Turni250 – 2523Combined sources
Helixi263 – 2664Combined sources
Helixi270 – 28415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQUX-ray1.60A/B1-295[»]
1AQYX-ray1.75A/B1-295[»]
1BO6X-ray2.10A/B1-295[»]
ProteinModelPortaliP49891.
SMRiP49891. Positions 7-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49891.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1083Substrate binding

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP49891.
PhylomeDBiP49891.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P49891-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METSMPEYYE VFGEFRGVLM DKRFTKYWED VEMFLARPDD LVIATYPKSG
60 70 80 90 100
TTWISEVVYM IYKEGDVEKC KEDAIFNRIP YLECRNEDLI NGIKQLKEKE
110 120 130 140 150
SPRIVKTHLP PKLLPASFWE KNCKMIYLCR NAKDVAVSYY YFLLMITSYP
160 170 180 190 200
NPKSFSEFVE KFMQGQVPYG SWYDHVKAWW EKSKNSRVLF MFYEDMKEDI
210 220 230 240 250
RREVVKLIEF LERKPSAELV DRIIQHTSFQ EMKNNPSTNY TMMPEEMMNQ
260 270 280 290
KVSPFMRKGI IGDWKNHFPE ALRERFDEHY KQQMKDCTVK FRMEL
Length:295
Mass (Da):35,590
Last modified:July 15, 1999 - v2
Checksum:i8E85AB47952BFB1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131L → V in AAB34320 (PubMed:7750469).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78182 mRNA. Translation: AAB34320.1.
CCDSiCCDS19392.1.
PIRiI53296.
UniGeneiMm.89655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78182 mRNA. Translation: AAB34320.1.
CCDSiCCDS19392.1.
PIRiI53296.
UniGeneiMm.89655.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQUX-ray1.60A/B1-295[»]
1AQYX-ray1.75A/B1-295[»]
1BO6X-ray2.10A/B1-295[»]
ProteinModelPortaliP49891.
SMRiP49891. Positions 7-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP49891. 1 interaction.
STRINGi10090.ENSMUSP00000031201.

Chemistry

BindingDBiP49891.
ChEMBLiCHEMBL3052.

PTM databases

PhosphoSiteiP49891.

Proteomic databases

MaxQBiP49891.
PaxDbiP49891.
PRIDEiP49891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:98431. Sult1e1.

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP49891.
PhylomeDBiP49891.

Miscellaneous databases

EvolutionaryTraceiP49891.
PROiP49891.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SULT1E1.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of a testis-specific estrogen sulfotransferase and aberrant liver expression in obese and diabetogenic C57BL/KsJ-db/db mice."
    Song W.-C., Moore R., McLachlan J.A., Negishi M.
    Endocrinology 136:2477-2484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/KSJ-DB/DB.
    Tissue: Testis.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH ADENOSINE 3',5'-BISPHOSPHATE (PAP), SEQUENCE REVISION TO 113.
    Strain: C57BL/KSJ-DB/DB.
    Tissue: Testis.
  3. "The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis."
    Kakuta Y., Petrotchenko E.V., Pedersen L.C., Negishi M.
    J. Biol. Chem. 273:27325-27330(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADENOSINE 3',5'BISPHOSPHATE AND VANADATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF LYS-48; LYS-106; HIS-108 AND TYR-240.

Entry informationi

Entry nameiST1E1_MOUSE
AccessioniPrimary (citable) accession number: P49891
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: January 20, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Abnormal high expression in liver in obese and diabetogenic C57BL/KSJ-DB/DB strain mice. Female > male. Normal level in liver.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.