SOAT_MOUSE
ID SOAT_MOUSE Reviewed; 373 AA.
AC Q9CXB2; B2RTH4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Sodium-dependent organic anion transporter {ECO:0000303|PubMed:23562556};
DE Short=SOAT {ECO:0000303|PubMed:23562556};
DE AltName: Full=Solute carrier family 10 member 6;
DE Short=SLC10A6 {ECO:0000303|PubMed:23562556};
GN Name=Slc10a6; Synonyms=Soat;
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].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Geyer J., Godoy J.R., Petzinger E.;
RT "Cloning of a sodium-dependent organic anion transporter (SOAT) from mouse
RT liver.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [4]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23562556; DOI=10.1016/j.jsbmb.2013.03.009;
RA Grosser G., Fietz D., Guenther S., Bakhaus K., Schweigmann H., Ugele B.,
RA Brehm R., Petzinger E., Bergmann M., Geyer J.;
RT "Cloning and functional characterization of the mouse sodium-dependent
RT organic anion transporter Soat (Slc10a6).";
RL J. Steroid Biochem. Mol. Biol. 138:90-99(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=28743544; DOI=10.1016/j.jsbmb.2017.07.019;
RA Bakhaus K., Bennien J., Fietz D., Sanchez-Guijo A., Hartmann M.,
RA Serafini R., Love C.C., Golovko A., Wudy S.A., Bergmann M., Geyer J.;
RT "Sodium-dependent organic anion transporter (Slc10a6-/-) knockout mice show
RT normal spermatogenesis and reproduction, but elevated serum levels for
RT cholesterol sulfate.";
RL J. Steroid Biochem. Mol. Biol. 179:45-54(2018).
CC -!- FUNCTION: Transports sulfoconjugated steroid hormones from the
CC extracellular compartment into the cytosol in a sodium-dependent manner
CC without hydrolysis (PubMed:23562556). 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 (PubMed:23562556). May
CC play 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:0000269|PubMed:23562556}.
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:23562556};
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:23562556};
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:0000269|PubMed:23562556};
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=60.3 uM for dehydroepiandrosterone 3-sulfate (DHEAS)
CC {ECO:0000269|PubMed:23562556};
CC KM=2.1 uM for estrone 3-sulfate (E1S) {ECO:0000269|PubMed:23562556};
CC KM=2.5 uM for pregnenolone sulfate (PREGS)
CC {ECO:0000269|PubMed:23562556};
CC Vmax=362.8 pmol/min/mg enzyme with dehydroepiandrosterone 3-sulfate
CC (DHEAS) as substrate {ECO:0000269|PubMed:23562556};
CC Vmax=26.6 pmol/min/mg enzyme with estrone 3-sulfate (E1S) as
CC substrate {ECO:0000269|PubMed:23562556};
CC Vmax=377.3 pmol/min/mg enzyme with pregnenolone sulfate (PREGS) as
CC substrate {ECO:0000269|PubMed:23562556};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23562556}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highest expression in lung and testis, moderate
CC expression in heart, bladder and skin, and low expression in blood,
CC liver, stomach, small intestine, spleen, kidney, adrenal gland, seminal
CC vesicle, preputial gland, coagulating gland, lacrimal gland/eye, and
CC brain. {ECO:0000269|PubMed:23562556}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice have normal reproductive phenotype,
CC however, males show higher cholesterol sulfate serum levels than wild-
CC type. {ECO:0000269|PubMed:28743544}.
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:0000303|PubMed:23562556}.
CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC
CC 2.A.28) family. {ECO:0000305}.
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DR EMBL; AJ583504; CAE47479.1; -; mRNA.
DR EMBL; AK018423; BAB31203.1; -; mRNA.
DR EMBL; BC127608; AAI27609.1; -; mRNA.
DR EMBL; BC139343; AAI39344.1; -; mRNA.
DR EMBL; BC139346; AAI39347.1; -; mRNA.
DR CCDS; CCDS19477.1; -.
DR RefSeq; NP_083691.1; NM_029415.2.
DR AlphaFoldDB; Q9CXB2; -.
DR SMR; Q9CXB2; -.
DR STRING; 10090.ENSMUSP00000031263; -.
DR GlyGen; Q9CXB2; 2 sites.
DR PaxDb; Q9CXB2; -.
DR PRIDE; Q9CXB2; -.
DR ProteomicsDB; 261396; -.
DR Antibodypedia; 14387; 47 antibodies from 13 providers.
DR DNASU; 75750; -.
DR Ensembl; ENSMUST00000031263; ENSMUSP00000031263; ENSMUSG00000029321.
DR GeneID; 75750; -.
DR KEGG; mmu:75750; -.
DR UCSC; uc008yjp.1; mouse.
DR CTD; 345274; -.
DR MGI; MGI:1923000; Slc10a6.
DR VEuPathDB; HostDB:ENSMUSG00000029321; -.
DR eggNOG; KOG2718; Eukaryota.
DR GeneTree; ENSGT00950000182808; -.
DR HOGENOM; CLU_034788_7_5_1; -.
DR InParanoid; Q9CXB2; -.
DR OMA; KWPKQSK; -.
DR OrthoDB; 1148347at2759; -.
DR PhylomeDB; Q9CXB2; -.
DR TreeFam; TF315811; -.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR BioGRID-ORCS; 75750; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Slc10a6; mouse.
DR PRO; PR:Q9CXB2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXB2; protein.
DR Bgee; ENSMUSG00000029321; Expressed in right lung lobe and 98 other tissues.
DR Genevisible; Q9CXB2; MM.
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; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR GO; GO:0043251; P:sodium-dependent organic anion transport; ISO:MGI.
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..373
FT /note="Sodium-dependent organic anion transporter"
FT /id="PRO_0000309216"
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..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..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..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
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 373 AA; 40681 MW; 0902D18506A8AC55 CRC64;
MSTDCAGNST CPVNSTEEDP PVGMEGHANL KLLFTVLSAV MVGLVMFSFG CSVESQKLWL
HLRRPWGIAV GLLSQFGLMP LTAYLLAIGF GLKPFQAIAV LMMGSCPGGT ISNVLTFWVD
GDMDLSISMT TCSTVAALGM MPLCLYIYTR SWTLTQNLVI PYQSIGITLV SLVVPVASGV
YVNYRWPKQA TVILKVGAIL GGMLLLVVAV TGMVLAKGWN TDVTLLVISC IFPLVGHVTG
FLLAFLTHQS WQRCRTISIE TGAQNIQLCI AMLQLSFSAE YLVQLLNFAL AYGLFQVLHG
LLIVAAYQAY KRRQKSKCRR QHPDCPDVCY EKQPRETSAF LDKGDEAAVT LGPVQPEQHH
RAAELTSHIP SCE
