S22A7_MOUSE
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 03-AUG-2022, entry version 140.
DE RecName: Full=Solute carrier family 22 member 7;
DE AltName: Full=Organic anion transporter 2;
DE Short=mOAT2;
GN Name=Slc22a7; 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), TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 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: Mediates sodium-independent multispecific organic anion
CC transport. High affinity transport of glutarate and prostaglandin E2 in
CC a sodium-independent manner. Mediates also the uptake of alpha-
CC ketoglutarate, p-aminohippuric acid, methotrexate, ochratoxin A,
CC valproate, allopurinol and bumetanide. {ECO:0000269|PubMed:16256982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.8 uM for glutarate {ECO:0000269|PubMed:12065749,
CC ECO:0000269|PubMed:16256982};
CC KM=5.2 nM for prostaglandin E2 {ECO:0000269|PubMed:12065749,
CC ECO:0000269|PubMed:16256982};
CC KM=9.12 uM for bumetanide {ECO:0000269|PubMed:12065749,
CC ECO:0000269|PubMed:16256982};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Note=Apical side of the renal tubule. {ECO:0000250}.
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 and
CC also in female liver. {ECO:0000269|PubMed:12065749}.
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; Q91WU2; -.
DR PRIDE; Q91WU2; -.
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 CTD; 10864; -.
DR MGI; MGI:1859559; Slc22a7.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q91WU2; -.
DR OrthoDB; 435631at2759; -.
DR PhylomeDB; Q91WU2; -.
DR TreeFam; TF315847; -.
DR Reactome; R-MMU-561048; Organic anion transport.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 108114; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q91WU2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91WU2; protein.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
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 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
