SOAT_RAT
ID SOAT_RAT Reviewed; 370 AA.
AC Q70EX6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sodium-dependent organic anion transporter {ECO:0000303|PubMed:15020217};
DE Short=Soat {ECO:0000303|PubMed:15020217};
DE AltName: Full=Solute carrier family 10 member 6;
DE Short=SLC10A6;
GN Name=Slc10a6; Synonyms=Soat;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Adrenal gland;
RX PubMed=15020217; DOI=10.1016/j.bbrc.2004.02.048;
RA Geyer J., Godoy J.R., Petzinger E.;
RT "Identification of a sodium-dependent organic anion transporter from rat
RT adrenal gland.";
RL Biochem. Biophys. Res. Commun. 316:300-306(2004).
CC -!- FUNCTION: Transports sulfoconjugated steroid hormones from the
CC extracellular compartment into the cytosol in a sodium-dependent manner
CC without hydrolysis (PubMed:15020217). Steroid sulfate hormones are
CC commonly considered to be biologically inactive metabolites, that may
CC be activated by steroid sulfatases into free steroids (By similarity).
CC May play an important role by delivering sulfoconjugated steroids to
CC specific target cells in reproductive organs (By similarity). May play
CC a role transporting the estriol precursor 16alpha-
CC hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal
CC blood vessel endothelium (By similarity). Can also transport other
CC sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and
CC sulfoconjugated pyrenes (By similarity). {ECO:0000250|UniProtKB:Q3KNW5,
CC ECO:0000250|UniProtKB:Q9CXB2, ECO:0000269|PubMed:15020217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in)
CC + 2 Na(+)(in); Xref=Rhea:RHEA:71083, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:15020217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 3-sulfate(out) + 2 Na(+)(out) = 17beta-
CC estradiol 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71087,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:136582;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroepiandrosterone 3-sulfate(out) + 2 Na(+)(out) =
CC dehydroepiandrosterone 3-sulfate(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:71091, ChEBI:CHEBI:29101, ChEBI:CHEBI:57905;
CC Evidence={ECO:0000269|PubMed:15020217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-diol 3-sulfate(out) + 2 Na(+)(out) = androst-5-
CC ene-diol 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71099,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:190287;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + pregnenolone sulfate(out) = 2 Na(+)(in) +
CC pregnenolone sulfate(in); Xref=Rhea:RHEA:71095, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:133000; Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + taurolithocholate 3-sulfate(out) = 2 Na(+)(in)
CC + taurolithocholate 3-sulfate(in); Xref=Rhea:RHEA:71275,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58301;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androsterone 3alpha-sulfate(out) + 2 Na(+)(out) = androsterone
CC 3alpha-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71351,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:133003;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-dihydrotestosterone sulfate(out) + 2 Na(+)(out) =
CC 5alpha-dihydrotestosterone sulfate(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:71355, ChEBI:CHEBI:29101, ChEBI:CHEBI:136982;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-sulfate(out) + 2 Na(+)(out) = 17beta-
CC estradiol 17-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71359,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:190469;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxypregnenolone 3-sulfate(out) + 2 Na(+)(out) =
CC 17alpha-hydroxypregnenolone 3-sulfate(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:71363, ChEBI:CHEBI:29101, ChEBI:CHEBI:133742;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=epiandrosterone 3-sulfate(out) + 2 Na(+)(out) =
CC epiandrosterone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71367,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:133729;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=epitestosterone 17-sulfate(out) + 2 Na(+)(out) =
CC epitestosterone 17-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71371,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:190485;
CC Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + testosterone 17-sulfate(out) = 2 Na(+)(in) +
CC testosterone 17-sulfate(in); Xref=Rhea:RHEA:71375, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:190489; Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha-hydroxydehydroepiandrosterone 3-sulfate(out) + 2
CC Na(+)(out) = 16alpha-hydroxydehydroepiandrosterone 3-sulfate(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:71391, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:87538; Evidence={ECO:0000250|UniProtKB:Q3KNW5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for estrone 3-sulfate (E1S) {ECO:0000269|PubMed:15020217};
CC KM=30 uM for dehydroepiandrosterone 3-sulfate (DHEAS)
CC {ECO:0000269|PubMed:15020217};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, lung, spleen and adrenal
CC gland. Moderately expressed in skeletal muscle, testis and small
CC intestine. {ECO:0000269|PubMed:15020217}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: In humans, 3-beta-sulfooxy-androst-5-en-17-one (DHEAS)
CC is the most abundant circulating steroid sulfate in the human body, it
CC is mainly synthesized from adrenal glands and gonads, whereas rats and
CC mice have low circulating concentrations of DHEAS in the periphery as
CC they can only produce DHEAS in their gonads.
CC {ECO:0000250|UniProtKB:Q9CXB2}.
CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC
CC 2.A.28) family. {ECO:0000305}.
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DR EMBL; AJ583503; CAE47478.1; -; mRNA.
DR RefSeq; NP_932166.1; NM_198049.1.
DR AlphaFoldDB; Q70EX6; -.
DR SMR; Q70EX6; -.
DR STRING; 10116.ENSRNOP00000002819; -.
DR TCDB; 2.A.28.1.3; the bile acid:na(+) symporter (bass) family.
DR GlyGen; Q70EX6; 2 sites.
DR PaxDb; Q70EX6; -.
DR PRIDE; Q70EX6; -.
DR Ensembl; ENSRNOT00000088508; ENSRNOP00000072386; ENSRNOG00000002057.
DR GeneID; 289459; -.
DR KEGG; rno:289459; -.
DR CTD; 345274; -.
DR RGD; 727800; Slc10a6.
DR eggNOG; KOG2718; Eukaryota.
DR GeneTree; ENSGT00950000182808; -.
DR HOGENOM; CLU_034788_7_5_1; -.
DR InParanoid; Q70EX6; -.
DR OMA; KWPKQSK; -.
DR OrthoDB; 1148347at2759; -.
DR PhylomeDB; Q70EX6; -.
DR TreeFam; TF315811; -.
DR Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:Q70EX6; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002057; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q70EX6; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0008508; F:bile acid:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0043250; F:sodium-dependent organic anion transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR GO; GO:0043251; P:sodium-dependent organic anion transport; IDA:RGD.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR002657; BilAc:Na_symport/Acr3.
DR InterPro; IPR004710; Bilac:Na_transpt.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR030203; SLC10A6.
DR PANTHER; PTHR10361; PTHR10361; 1.
DR PANTHER; PTHR10361:SF55; PTHR10361:SF55; 1.
DR Pfam; PF01758; SBF; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Lipid transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..370
FT /note="Sodium-dependent organic anion transporter"
FT /id="PRO_0000309217"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 40310 MW; 27CBA6E42B0733D7 CRC64;
MSADCEGNST CPANSTEEDP PVGMEGQGSL KLVFTVLSAV MVGLVMFSFG CSVESRKLWL
HLRRPWGIAV GLLCQFGLMP LTAYLLAIGF GLKPFQAIAV LIMGSCPGGT VSNVLTFWVD
GDMDLSISMT TCSTVAALGM MPLCLYVYTR SWTLPQSLTI PYQSIGITLV SLVVPVASGI
YVNYRWPKQA TFILKVGAAV GGMLLLVVAV TGVVLAKGWN IDVTLLVISC IFPLVGHVMG
FLLAFLTHQS WQRCRTISIE TGAQNIQLCI AMMQLSFSAE YLVQLLNFAL AYGLFQVLHG
LLIVAAYQAY KRRQKSQYRR QHPECQDISS EKQPRETSAF LDKGAEAAVT LGLEQHHRTA
ELTSHVPSCE
