ID   S22A7_MOUSE             Reviewed;         540 AA.
AC   Q91WU2; Q3UNX2; Q8BUQ9; Q8K4S9; Q8R0M7; Q8R125;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Solute carrier family 22 member 7 {ECO:0000303|PubMed:16256982};
DE   AltName: Full=Organic anion transporter 2 {ECO:0000303|PubMed:16141072};
DE            Short=mOAT2 {ECO:0000303|PubMed:16141072};
GN   Name=Slc22a7 {ECO:0000312|MGI:MGI:1859559}; Synonyms=Oat2;
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), FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=12065749; DOI=10.1124/mol.62.1.7;
RA   Kobayashi Y., Ohshiro N., Shibusawa A., Sasaki T., Tokuyama S., Sekine T.,
RA   Endou H., Yamamoto T.;
RT   "Isolation, characterization and differential gene expression of
RT   multispecific organic anion transporter 2 in mice.";
RL   Mol. Pharmacol. 62:7-14(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX   PubMed=16256982; DOI=10.1016/j.ejphar.2005.09.054;
RA   Kobayashi Y., Ohbayashi M., Kohyama N., Yamamoto T.;
RT   "Mouse organic anion transporter 2 and 3 (mOAT2/3[Slc22a7/8]) mediates the
RT   renal transport of bumetanide.";
RL   Eur. J. Pharmacol. 524:44-48(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16885152; DOI=10.1152/ajprenal.00207.2006;
RA   Ljubojevic M., Balen D., Breljak D., Kusan M., Anzai N., Bahn A.,
RA   Burckhardt G., Sabolic I.;
RT   "Renal expression of organic anion transporter OAT2 in rats and mice is
RT   regulated by sex hormones.";
RL   Am. J. Physiol. 292:F361-F372(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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: Functions as a Na(+)-independent bidirectional multispecific
CC       transporter (PubMed:12065749). Contributes to the renal and hepatic
CC       elimination of endogenous organic compounds from the systemic
CC       circulation into the urine and bile, respectively (PubMed:12065749).
CC       Capable of transporting a wide range of purine and pyrimidine
CC       nucleobases, nucleosides, and nucleotides with cGMP, 2'deoxyguanosine
CC       and GMP being the preferred substrates (By similarity). Functions as a
CC       pH- and chloride-independent cGMP bidirectional facilitative
CC       transporter that can regulate both intracellular and extracellular
CC       levels of cGMP and may be involved in cGMP signaling pathways (By
CC       similarity). Mediates orotate/glutamate bidirectional exchange and most
CC       likely display a physiological role in hepatic release of glutamate
CC       into the blood (By similarity). Involved in renal secretion and
CC       possible reabsorption of creatinine (By similarity). Able to uptake
CC       prostaglandin E2 (PGE2) and may contribute to PGE2 renal excretion
CC       (Probable). Also transports alpha-ketoglutarate and urate
CC       (PubMed:12065749). Unlike human hortolog, able to transport glutarate
CC       (PubMed:12065749). Apart from the orotate/glutamate exchange, the
CC       counterions for the uptake of other SLC22A7/OAT2 substrates remain to
CC       be identified (By similarity). {ECO:0000250|UniProtKB:Q9Y694,
CC       ECO:0000269|PubMed:12065749, ECO:0000305|PubMed:12065749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate(in) + orotate(out) = L-glutamate(out) +
CC         orotate(in); Xref=Rhea:RHEA:72043, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30839; Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP(in) = 3',5'-cyclic GMP(out);
CC         Xref=Rhea:RHEA:76207, ChEBI:CHEBI:57746;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GMP(in) = GMP(out); Xref=Rhea:RHEA:76211, ChEBI:CHEBI:58115;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyguanosine(in) = 2'-deoxyguanosine(out);
CC         Xref=Rhea:RHEA:76215, ChEBI:CHEBI:17172;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP(in) = GDP(out); Xref=Rhea:RHEA:76219, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371,
CC         ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP(in) = GTP(out); Xref=Rhea:RHEA:75787, ChEBI:CHEBI:37565;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP(in) = 3',5'-cyclic AMP(out);
CC         Xref=Rhea:RHEA:76223, ChEBI:CHEBI:58165;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=creatinine(in) = creatinine(out); Xref=Rhea:RHEA:74539,
CC         ChEBI:CHEBI:16737; Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:12065749, ECO:0000269|PubMed:16256982};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate(in) = 2-oxoglutarate(out);
CC         Xref=Rhea:RHEA:76231, ChEBI:CHEBI:16810;
CC         Evidence={ECO:0000269|PubMed:12065749};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutarate(in) = glutarate(out); Xref=Rhea:RHEA:76251,
CC         ChEBI:CHEBI:30921; Evidence={ECO:0000269|PubMed:12065749};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368,
CC         ChEBI:CHEBI:17775; Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15.8 uM for glutarate {ECO:0000269|PubMed:12065749};
CC         KM=0.0052 uM for prostaglandin E2 {ECO:0000269|PubMed:12065749};
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y694}. Apical cell membrane
CC       {ECO:0000269|PubMed:16256982}; Multi-pass membrane protein
CC       {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass
CC       membrane protein {ECO:0000305}. Note=Apical side of the renal tubule.
CC       {ECO:0000269|PubMed:16256982}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91WU2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91WU2-2; Sequence=VSP_030995, VSP_030996;
CC   -!- TISSUE SPECIFICITY: Abundant expression in male and female kidney
CC       (PubMed:12065749). In kidney, expressed at the brush border of the
CC       proximal tubule S3 segment (S3) in the outer stripe and medullary rays
CC       (PubMed:16256982, PubMed:16885152). In kidney, expression is higher in
CC       female than male (PubMed:16885152). Also expressed in female liver
CC       (PubMed:12065749). {ECO:0000269|PubMed:12065749,
CC       ECO:0000269|PubMed:16256982, ECO:0000269|PubMed:16885152}.
CC   -!- MISCELLANEOUS: Involved in the uptake of clinically used drugs such as
CC       bumetanide, and contributes to renal and hepatic drug elimination.
CC       {ECO:0000269|PubMed:16256982}.
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; AB069965; BAC02736.1; -; mRNA.
DR   EMBL; AK082865; BAC38659.1; -; mRNA.
DR   EMBL; AK143949; BAE25625.1; -; mRNA.
DR   EMBL; BC013474; AAH13474.1; -; mRNA.
DR   EMBL; BC024119; AAH24119.1; -; mRNA.
DR   EMBL; BC025813; AAH25813.1; -; mRNA.
DR   EMBL; BC026598; AAH26598.1; -; mRNA.
DR   EMBL; BC026597; AAH26597.1; -; mRNA.
DR   CCDS; CCDS28829.1; -. [Q91WU2-1]
DR   RefSeq; NP_659105.2; NM_144856.2.
DR   AlphaFoldDB; Q91WU2; -.
DR   SMR; Q91WU2; -.
DR   STRING; 10090.ENSMUSP00000084234; -.
DR   ChEMBL; CHEMBL2073716; -.
DR   iPTMnet; Q91WU2; -.
DR   PhosphoSitePlus; Q91WU2; -.
DR   jPOST; Q91WU2; -.
DR   MaxQB; Q91WU2; -.
DR   PaxDb; 10090-ENSMUSP00000084234; -.
DR   ProteomicsDB; 260755; -. [Q91WU2-1]
DR   ProteomicsDB; 260756; -. [Q91WU2-2]
DR   DNASU; 108114; -.
DR   GeneID; 108114; -.
DR   KEGG; mmu:108114; -.
DR   UCSC; uc008csw.2; mouse. [Q91WU2-1]
DR   AGR; MGI:1859559; -.
DR   CTD; 10864; -.
DR   MGI; MGI:1859559; Slc22a7.
DR   eggNOG; KOG0255; Eukaryota.
DR   InParanoid; Q91WU2; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; Q91WU2; -.
DR   TreeFam; TF315847; -.
DR   Reactome; R-MMU-561048; Organic anion transport.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   SABIO-RK; Q91WU2; -.
DR   BioGRID-ORCS; 108114; 1 hit in 76 CRISPR screens.
DR   PRO; PR:Q91WU2; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q91WU2; Protein.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015742; P:alpha-ketoglutarate transport; IDA:UniProtKB.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR   GO; GO:0015732; P:prostaglandin transport; IDA:UniProtKB.
DR   GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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   NCBIfam; TIGR00898; 2A0119; 1.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   PANTHER; PTHR24064:SF33; SOLUTE CARRIER FAMILY 22 MEMBER 7; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..540
FT                   /note="Solute carrier family 22 member 7"
FT                   /id="PRO_0000317482"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..124
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030995"
FT   VAR_SEQ         125..131
FT                   /note="SSTIATE -> MGESSET (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030996"
FT   CONFLICT        46
FT                   /note="A -> T (in Ref. 1; BAC02736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="R -> H (in Ref. 1; BAC02736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="Y -> C (in Ref. 2; BAC38659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="E -> Q (in Ref. 2; BAC38659/BAE25625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="Y -> N (in Ref. 2; BAC38659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="W -> S (in Ref. 3; AAH26598)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   540 AA;  59614 MW;  2A5AA5A5E0F30BAE CRC64;
     MGFEELLHKV GGFGPFQLRN LVLLALPRFL LPMHFLLPIF MAAVPAHHCA LPDAPANLSH
     QDLWLKTHLP RETDGSFSSC LRFAYPQALP NVTLGTEVYN SGEPEGEPLT VPCSQGWEYD
     RSEFSSTIAT EWDLVCEQRG LNKVTSTCFF IGVLLGAVVY GYLSDRFGRR RLLLVAYVST
     LALGLMSAAS VNYIMFVTTR MLTGSALAGF TIIVLPLELE WLDVEHRTVA GVISTTFWTG
     GVLLLTLVGY LIRSWRWLLL AATLPCVPGI ISIWWVPESA RWLLTQGRVE EAKKYLSICA
     KLNGRPISED SLSQEALNKV ITMERVSQRP SYLDLFRTSQ LRHVSLCCMM MWFGVNFSYY
     GLTLDASGLG LTVYQTQLLF GAVEVPSKIT VFFLVRLVGR RLTEAGMLLA TALTFGISLL
     VSSDTKSWIT ALVVIGKAFS EAAFTTAYLF TSELYPTVLR QTGMGFTALI GRLGASLAPL
     VVLLDGVWLL LPKLAYGGIS FLAACTVLLL PETKKAQLPE TIQDVERKGR KIDRSGTELA
//