ST2B1_RAT
ID ST2B1_RAT Reviewed; 340 AA.
AC Q29YR5; Q29YR6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sulfotransferase 2B1;
DE EC=2.8.2.2 {ECO:0000269|PubMed:16368200};
DE AltName: Full=Alcohol sulfotransferase;
DE AltName: Full=Hydroxysteroid sulfotransferase 2;
DE AltName: Full=Sulfotransferase family cytosolic 2B member 1;
DE Short=ST2B1;
GN Name=Sult2b1 {ECO:0000312|RGD:1308882};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAX34390.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAX34390.1};
RC TISSUE=Brain {ECO:0000269|PubMed:16368200};
RX PubMed=16368200; DOI=10.1016/j.gene.2005.09.009;
RA Kohjitani A., Fuda H., Hanyu O., Strott C.A.;
RT "Cloning, characterization and tissue expression of rat SULT2B1a and
RT SULT2B1b steroid/sterol sulfotransferase isoforms: divergence of the rat
RT SULT2B1 gene structure from orthologous human and mouse genes.";
RL Gene 367:66-73(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation.
CC Sulfonation increases the water solubility of most compounds, and
CC therefore their renal excretion, but it can also result in
CC bioactivation to form active metabolites. Sulfonates cholesterol
CC (PubMed:16368200). Catalyzes sulfation of the 3beta-hydroxyl groups of
CC steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA)
CC (PubMed:16368200). Conjugates efficiently cholesterol but has a greater
CC affinity for pregnenolone sulfation. Does not show high activity with
CC DHEA (PubMed:16368200). Plays a role in epidermal cholesterol
CC metabolism and in the regulation of epidermal proliferation and
CC differentiation (By similarity). {ECO:0000250|UniProtKB:O00204,
CC ECO:0000269|PubMed:16368200}.
CC -!- FUNCTION: [Isoform 2]: Prefers pregnenolone over DHEA as a substrate
CC and does not sulfate cholesterol. {ECO:0000269|PubMed:16368200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC Evidence={ECO:0000269|PubMed:16368200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-
CC bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133000;
CC Evidence={ECO:0000269|PubMed:16368200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000269|PubMed:16368200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-
CC bisphosphate + cholesterol sulfate + H(+); Xref=Rhea:RHEA:52368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136579;
CC Evidence={ECO:0000269|PubMed:16368200};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for pregnenolone (isoform 2) {ECO:0000269|PubMed:16368200};
CC KM=17.9 uM for dehydroepiandrosterone (DHEA) (isoform 2)
CC {ECO:0000269|PubMed:16368200};
CC KM=1.7 uM for cholesterol (isoform 1) {ECO:0000269|PubMed:16368200};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P52843}. Microsome
CC {ECO:0000250|UniProtKB:O00204}. Nucleus {ECO:0000250|UniProtKB:O00204}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16368200}; Synonyms=SULT2B1b
CC {ECO:0000269|PubMed:16368200};
CC IsoId=Q29YR5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16368200}; Synonyms=SULT2B1a
CC {ECO:0000269|PubMed:16368200};
CC IsoId=Q29YR5-2; Sequence=VSP_052079;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in skin and testis. Higher
CC level of isoform 2 expressed in skin and intestine, moderate level in
CC the kidney, low level in liver, stomach and placenta.
CC {ECO:0000269|PubMed:16368200}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AY827147; AAX34390.1; -; mRNA.
DR EMBL; AY827148; AAX34391.1; -; mRNA.
DR RefSeq; NP_001034754.1; NM_001039665.1. [Q29YR5-2]
DR RefSeq; XP_006229093.1; XM_006229031.3. [Q29YR5-1]
DR AlphaFoldDB; Q29YR5; -.
DR SMR; Q29YR5; -.
DR STRING; 10116.ENSRNOP00000060264; -.
DR iPTMnet; Q29YR5; -.
DR PhosphoSitePlus; Q29YR5; -.
DR jPOST; Q29YR5; -.
DR PaxDb; Q29YR5; -.
DR PRIDE; Q29YR5; -.
DR Ensembl; ENSRNOT00000028570; ENSRNOP00000028570; ENSRNOG00000021046. [Q29YR5-1]
DR Ensembl; ENSRNOT00000067430; ENSRNOP00000060264; ENSRNOG00000021046. [Q29YR5-2]
DR GeneID; 292915; -.
DR KEGG; rno:292915; -.
DR UCSC; RGD:1308882; rat. [Q29YR5-1]
DR CTD; 6820; -.
DR RGD; 1308882; Sult2b1.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000159269; -.
DR HOGENOM; CLU_027239_1_0_1; -.
DR InParanoid; Q29YR5; -.
DR OMA; DPYEKNI; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q29YR5; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.2; 5301.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; Q29YR5; -.
DR PRO; PR:Q29YR5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021046; Expressed in jejunum and 17 other tissues.
DR Genevisible; Q29YR5; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0003676; F:nucleic acid binding; ISO:RGD.
DR GO; GO:1990239; F:steroid hormone binding; ISO:RGD.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISO:RGD.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISO:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0000103; P:sulfate assimilation; ISO:RGD.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW Microsome; Nucleus; Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..340
FT /note="Sulfotransferase 2B1"
FT /id="PRO_0000244488"
FT REGION 301..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 67..72
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 152
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 207
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 241..246
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 271..273
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT VAR_SEQ 1..20
FT /note="MDGPQPPALWGSLENRVSEL -> MSPWSRNTCYSSPSMRLDRSCARNTARW
FT GHWKEGKPHGGLTGETEAGSSWNGGSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16368200"
FT /id="VSP_052079"
SQ SEQUENCE 340 AA; 38322 MW; 9B3496466393A361 CRC64;
MDGPQPPALW GSLENRVSEL SQKLQGEYFR YKGIPFPVGM YTPESLSLAE NTSNVRDDDI
FIVTYPKSGT NWMIEIICLI LKDGDPSWIR SEPIWQRAPW CETTISAFSL PERPSPRLMC
SHLPIELFTK AAFSSKAKVI YLGRNPRDVV VSLYYYSKIA VQLKDPGTPE QFLQNFLKGE
VQFGSWFDHI KGWIRMRGRE NFLFITYEEL QQDLRGSVQL ICEFLGRPLG EEALSSVVAH
SAFAAMKANN MSNYTLLPAS LLDHRQGAFL RKGISGDWKN HFTVAQSETF DQVYREQMHG
LPSFPWDRSA EDGSPDGETE PSPSPSPGLA SDDPNPGSSQ
