ST2B1_MOUSE
ID ST2B1_MOUSE Reviewed; 338 AA.
AC O35400; Q8K472; Q91V03;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sulfotransferase 2B1;
DE EC=2.8.2.2 {ECO:0000269|PubMed:12639899, ECO:0000269|PubMed:9647753};
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; Synonyms=Sult2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RX PubMed=9647753; DOI=10.1006/bbrc.1998.8872;
RA Sakakibara Y., Yanagisawa K., Takami Y., Nakayama T., Suiko M., Liu M.-C.;
RT "Molecular cloning, expression, and functional characterization of novel
RT mouse sulfotransferases.";
RL Biochem. Biophys. Res. Commun. 247:681-686(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES
RP (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=12639899; DOI=10.1210/en.2002-221011;
RA Shimizu C., Fuda H., Yanai H., Strott C.A.;
RT "Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure
RT in the mouse: pre- and postnatal expression, kinetic analysis of isoforms,
RT and comparison with prototypical SULT2A1.";
RL Endocrinology 144:1186-1193(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation.
CC Preferentially sulfonates cholesterol (PubMed:12639899). Catalyzes
CC sulfation of the 3beta-hydroxyl groups of steroids, such as,
CC pregnenolone and dehydroepiandrosterone (DHEA). Cholesterol sulfation
CC is approximately 10-fold higher than for pregnenolone and 20-fold
CC higher than for DHEA (PubMed:12639899). Plays a role in epidermal
CC cholesterol metabolism and in the regulation of epidermal proliferation
CC and differentiation (By similarity). {ECO:0000250|UniProtKB:O00204,
CC ECO:0000269|PubMed:12639899}.
CC -!- FUNCTION: [Isoform 2]: Strongly sulfonates pregnenolone, however is
CC capable to sulfonate cholesterol with a high degree of efficiency. DHEA
CC is a relatively poor substrate. {ECO:0000269|PubMed:12639899}.
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:12639899};
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:12639899};
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:12639899, ECO:0000269|PubMed:9647753};
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:12639899};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.88 uM for cholesterol (isoform 2) {ECO:0000269|PubMed:12639899};
CC KM=17.7 uM for pregnenolone (isoform 2)
CC {ECO:0000269|PubMed:12639899};
CC KM=0.87 uM for cholesterol (isoform 1) {ECO:0000269|PubMed:12639899};
CC KM=16.7 uM for pregnenolone (isoform 1)
CC {ECO:0000269|PubMed:12639899};
CC KM=19.7 uM for 3beta-hydroxyandrost-5-en-17-one (DHEA)(isoform 1)
CC {ECO:0000269|PubMed:12639899};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00204}. Microsome
CC {ECO:0000250|UniProtKB:O00204}. Nucleus {ECO:0000250|UniProtKB:O00204}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SULT2B1b, B;
CC IsoId=O35400-1; Sequence=Displayed;
CC Name=2; Synonyms=SULT2B1a, A;
CC IsoId=O35400-2; Sequence=VSP_012511;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in epididymis, intestine
CC and uterus, and low levels in brain and hypothalamus (PubMed:9647753).
CC Isoform 2 is most prominent in the brain and spinal cord, with modest
CC expression in the lung, skin and spleen (PubMed:12639899). Isoform 1 is
CC most prominently expressed in skin and small intestine, with modest
CC expression in muscle and prostate (PubMed:12639899).
CC {ECO:0000269|PubMed:12639899, ECO:0000269|PubMed:9647753}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 and isoform 2 are expressed from stages
CC 8.5-19 dpc. {ECO:0000269|PubMed:12639899}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF026072; AAC69918.1; -; mRNA.
DR EMBL; AF478566; AAM46788.1; -; mRNA.
DR EMBL; BC009811; AAH09811.1; -; mRNA.
DR EMBL; BC009813; AAH09813.1; -; mRNA.
DR CCDS; CCDS21263.1; -. [O35400-1]
DR PIR; JE0196; JE0196.
DR RefSeq; NP_059493.2; NM_017465.2. [O35400-1]
DR AlphaFoldDB; O35400; -.
DR SMR; O35400; -.
DR IntAct; O35400; 7.
DR MINT; O35400; -.
DR STRING; 10090.ENSMUSP00000075005; -.
DR iPTMnet; O35400; -.
DR PhosphoSitePlus; O35400; -.
DR EPD; O35400; -.
DR MaxQB; O35400; -.
DR PaxDb; O35400; -.
DR PeptideAtlas; O35400; -.
DR PRIDE; O35400; -.
DR ProteomicsDB; 254568; -. [O35400-1]
DR ProteomicsDB; 254569; -. [O35400-2]
DR Antibodypedia; 31732; 263 antibodies from 28 providers.
DR DNASU; 54200; -.
DR Ensembl; ENSMUST00000075571; ENSMUSP00000075005; ENSMUSG00000003271. [O35400-1]
DR GeneID; 54200; -.
DR KEGG; mmu:54200; -.
DR UCSC; uc009gxb.2; mouse. [O35400-1]
DR CTD; 6820; -.
DR MGI; MGI:1926342; Sult2b1.
DR VEuPathDB; HostDB:ENSMUSG00000003271; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000159269; -.
DR HOGENOM; CLU_027239_1_0_1; -.
DR InParanoid; O35400; -.
DR OMA; DPYEKNI; -.
DR PhylomeDB; O35400; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.2; 3474.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; O35400; -.
DR BioGRID-ORCS; 54200; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Sult2b1; mouse.
DR PRO; PR:O35400; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35400; protein.
DR Bgee; ENSMUSG00000003271; Expressed in lip and 122 other tissues.
DR ExpressionAtlas; O35400; baseline and differential.
DR Genevisible; O35400; MM.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:MGI.
DR GO; GO:0003676; F:nucleic acid binding; ISO:MGI.
DR GO; GO:1990239; F:steroid hormone binding; ISO:MGI.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR GO; GO:0000103; P:sulfate assimilation; IDA:MGI.
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..338
FT /note="Sulfotransferase 2B1"
FT /id="PRO_0000085150"
FT REGION 301..338
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="MDGPQPRALWSSSEKNVSEM -> MTSRDCCCGGVEVDLLLRWTHGAQRKDT
FT PHWRVNEGPCDSCPPPWSSLHVPFPSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12639899"
FT /id="VSP_012511"
FT CONFLICT 329
FT /note="S -> F (in Ref. 1; AAC69918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38347 MW; EA21BAB0917034C1 CRC64;
MDGPQPRALW SSSEKNVSEM SWNFGGEYFR YKGIPFPVGM YSPESLSLAE NTSNVRDDDI
FIVTYPKSGT NWMIEIVCLI LKDGDPSWIR SEPIWQRAPW CETIISAFNV LDRPSPRIMS
SHLPIELFTK AFFSSKAKVI YVGRNPRDVV VSLYYYSKIA GQLKDPGTPD QFLQNFLKGE
VQFGSWFDHI KGWIRMQNQE NFLFITYEEL QQDLRGSVQR ICEFLGRPLG EEALSSVVAH
SAFAAMKANT MSNYSLLPAS LLDHRQGEFL RKGISGDWKN HFTVAQSEAF DSVYREQMHG
VQRFPWDTSE EDSSPDGQPD PEPSPSPASD DPNPGSSQ
