S22A8_MOUSE
ID S22A8_MOUSE Reviewed; 537 AA.
AC O88909; Q3TZF9; Q8CCX3; Q8CFH5; Q91WJ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Solute carrier family 22 member 8;
DE AltName: Full=Organic anion transporter 3;
DE Short=mOat3;
DE AltName: Full=Reduced in osteosclerosis transporter;
GN Name=Slc22a8; Synonyms=Oat3, Roct;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10087192; DOI=10.1006/geno.1998.5722;
RA Brady K.P., Dushkin H., Foernzler D., Koike T., Magner F., Her H.,
RA Gullans S., Segre G.V., Green R.M., Beier D.R.;
RT "A novel putative transporter maps to the osteosclerosis (oc) mutation and
RT is not expressed in the oc mutant mouse.";
RL Genomics 56:254-261(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear, Medulla oblongata, and Retina;
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 STRAIN=FVB/N; TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 13-537.
RC TISSUE=Kidney;
RA Kobayashi Y., Shibusawa A., Ohshiro N., Sasaki T., Tokuyama S.,
RA Yamamoto T.;
RT "Cloning and functional characterization of mOAT3 (Roct).";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12011098; DOI=10.1074/jbc.m203803200;
RA Sweet D.H., Miller D.S., Pritchard J.B., Fujiwara Y., Beier D.R.,
RA Nigam S.K.;
RT "Impaired organic anion transport in kidney and choroid plexus of organic
RT anion transporter 3 (Oat3 (Slc22a8)) knockout mice.";
RL J. Biol. Chem. 277:26934-26943(2002).
RN [6]
RP FUNCTION.
RX PubMed=15075193; DOI=10.1152/ajprenal.00356.2003;
RA Sykes D., Sweet D.H., Lowes S., Nigam S.K., Pritchard J.B., Miller D.S.;
RT "Organic anion transport in choroid plexus from wild-type and organic anion
RT transporter 3 (Slc22a8)-null mice.";
RL Am. J. Physiol. 286:F972-F978(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15100168; DOI=10.1124/dmd.32.5.479;
RA Kobayashi Y., Ohshiro N., Tsuchiya A., Kohyama N., Ohbayashi M.,
RA Yamamoto T.;
RT "Renal transport of organic compounds mediated by mouse organic anion
RT transporter 3 (mOat3): further substrate specificity of mOat3.";
RL Drug Metab. Dispos. 32:479-483(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays an important role in the excretion/detoxification of
CC endogenous and exogenous organic anions, especially from the brain and
CC kidney. Mediates the uptake of p-amino-hippurate (PAH) and estron
CC sulfate (ES). Also mediates uptake of several organic compounds such as
CC prostaglandin E(2), prostaglandin F(2-alpha), allopurinol, 6-
CC mercaptopurine (6-MP), 5-fluorouracil (5-FU), and L-carnitine.
CC {ECO:0000269|PubMed:12011098, ECO:0000269|PubMed:15075193,
CC ECO:0000269|PubMed:15100168}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Note=Localizes on the brush border
CC membrane of the choroid epithelial cells. Localizes to the basolateral
CC membrane of the proximal tubular cells. Localizes on the abluminal and
CC possibly, luminal membrane of the brain capillary endothelial cells
CC (BCEC) (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Expressed in developing
CC bone. Weakly expressed in brain and eye. {ECO:0000269|PubMed:10087192,
CC ECO:0000269|PubMed:15100168}.
CC -!- DISRUPTION PHENOTYPE: Mice appear healthy and are fertile. Exhibit a
CC loss of taurocholate, estrone sulfate and para-aminohippurate transport
CC in kidney and of fluorescein (FL) transport in choroid plexus.
CC {ECO:0000269|PubMed:12011098}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; AF078869; AAC61265.1; -; mRNA.
DR EMBL; AK031962; BAC27624.1; -; mRNA.
DR EMBL; AK044336; BAC31873.1; -; mRNA.
DR EMBL; AK157891; BAE34249.1; -; mRNA.
DR EMBL; BC014762; AAH14762.1; -; mRNA.
DR EMBL; AB079895; BAC53618.1; -; mRNA.
DR CCDS; CCDS29537.1; -.
DR RefSeq; NP_001158106.1; NM_001164634.1.
DR RefSeq; NP_001158107.1; NM_001164635.1.
DR RefSeq; NP_112471.3; NM_031194.5.
DR RefSeq; XP_011245473.1; XM_011247171.1.
DR AlphaFoldDB; O88909; -.
DR SMR; O88909; -.
DR STRING; 10090.ENSMUSP00000010251; -.
DR BindingDB; O88909; -.
DR ChEMBL; CHEMBL2073672; -.
DR TCDB; 2.A.1.19.9; the major facilitator superfamily (mfs).
DR GlyGen; O88909; 1 site.
DR iPTMnet; O88909; -.
DR PhosphoSitePlus; O88909; -.
DR jPOST; O88909; -.
DR MaxQB; O88909; -.
DR PaxDb; O88909; -.
DR PRIDE; O88909; -.
DR ProteomicsDB; 260887; -.
DR Antibodypedia; 28883; 192 antibodies from 27 providers.
DR DNASU; 19879; -.
DR Ensembl; ENSMUST00000010251; ENSMUSP00000010251; ENSMUSG00000063796.
DR Ensembl; ENSMUST00000170817; ENSMUSP00000131045; ENSMUSG00000063796.
DR GeneID; 19879; -.
DR KEGG; mmu:19879; -.
DR UCSC; uc008gmc.2; mouse.
DR CTD; 9376; -.
DR MGI; MGI:1336187; Slc22a8.
DR VEuPathDB; HostDB:ENSMUSG00000063796; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154901; -.
DR HOGENOM; CLU_001265_33_3_1; -.
DR InParanoid; O88909; -.
DR OMA; RIPLQPC; -.
DR OrthoDB; 464838at2759; -.
DR PhylomeDB; O88909; -.
DR TreeFam; TF315847; -.
DR Reactome; R-MMU-561048; Organic anion transport.
DR BioGRID-ORCS; 19879; 1 hit in 72 CRISPR screens.
DR PRO; PR:O88909; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O88909; protein.
DR Bgee; ENSMUSG00000063796; Expressed in right kidney and 96 other tissues.
DR Genevisible; O88909; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; ISO:MGI.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; ISO:MGI.
DR GO; GO:0034635; P:glutathione transport; ISO:MGI.
DR GO; GO:0015697; P:quaternary ammonium group transport; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004749; Orgcat_transp/SVOP.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00898; 2A0119; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Detoxification; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..537
FT /note="Solute carrier family 22 member 8"
FT /id="PRO_0000273441"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..537
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 513..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1U7"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 271
FT /note="K -> R (in Ref. 1; AAC61265)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="G -> V (in Ref. 2; BAC27624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 59246 MW; F85FF82002AB26EB CRC64;
MTFSEILDRV GSMGPFQYLH VTLLALPILG IANHNLLQIF TATTPDHHCR PPPNASLEPW
VLPLGPNGKP EKCLRFVHLP NASLPNDTQG ATEPCLDGWI YNSTRDTIVT EWDLVCGSNK
LKEMAQSVFM AGILVGGPVF GELSDRFGRK PILTWSYLLL AASGSSAAFS PSLTVYMIFR
FLCGCSISGI SLSTIILNVE WVPTSTRAIS STTIGYCYTI GQFILPGLAY AVPQWRWLQL
SVSAAFFIFS LLSWWVPESI RWLVLSGKFS KALKTLQRVA TFNGKKEEGE KLTVEELKFN
LQKDITSAKV KYGLSDLFRV SILRRVTFCL SLAWFATGFA YYSLAMGVEE FGVNIYILQI
IFGGVDIPAK FITILSISYL GRRITQGFLL ILAGVAILAL IFVSSEMQLL RTALAVFGKG
CLSGSFSCLF LYTSELYPTV LRQTGMGISN IWARVGSMIA PLVKITGELQ PFIPNVIFGT
MTLLGGSAAF FLLETLNRPL PETIEDIQDW YQQTKKTKQE PEAEKASQTI PLKTGGP
