ID S22A7_BOVIN Reviewed; 547 AA.
AC A6QLW8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 08-NOV-2023, entry version 82.
DE RecName: Full=Solute carrier family 22 member 7 {ECO:0000250|UniProtKB:Q9Y694};
DE AltName: Full=Organic anion transporter 2 {ECO:0000250|UniProtKB:Q9Y694};
GN Name=SLC22A7; Synonyms=OAT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a Na(+)-independent bidirectional multispecific
CC transporter. Contributes to the renal and hepatic elimination of
CC endogenous organic compounds from the systemic circulation into the
CC urine and bile, respectively. Capable of transporting a wide range of
CC purine and pyrimidine nucleobases, nucleosides and nucleotides, with
CC cGMP, 2'deoxyguanosine and GMP being the preferred substrates.
CC Functions as a pH- and chloride-independent cGMP bidirectional
CC facilitative transporter that can regulate both intracellular and
CC extracellular levels of cGMP and may be involved in cGMP signaling
CC pathways. Mediates orotate/glutamate bidirectional exchange and most
CC likely display a physiological role in hepatic release of glutamate
CC into the blood. Involved in renal secretion and possible reabsorption
CC of creatinine. Able to uptake prostaglandin E2 (PGE2) and may
CC contribute to PGE2 renal excretion. Also transports alpha-ketoglutarate
CC and urate. Apart from the orotate/glutamate exchange, the counterions
CC for the uptake of other SLC22A7/OAT2 substrates remain to be
CC identified. {ECO:0000250|UniProtKB:Q9Y694}.
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:0000250|UniProtKB:Q9Y694};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(in) = 2-oxoglutarate(out);
CC Xref=Rhea:RHEA:76231, ChEBI:CHEBI:16810;
CC Evidence={ECO:0000250|UniProtKB:Q9Y694};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutarate(in) = glutarate(out); Xref=Rhea:RHEA:76251,
CC ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q91WU2};
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 -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein
CC {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y694};
CC Multi-pass membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y694}; Multi-pass membrane protein
CC {ECO:0000305}.
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; BC148112; AAI48113.1; -; mRNA.
DR RefSeq; NP_001094517.1; NM_001101047.2.
DR AlphaFoldDB; A6QLW8; -.
DR SMR; A6QLW8; -.
DR STRING; 9913.ENSBTAP00000008336; -.
DR PaxDb; 9913-ENSBTAP00000008336; -.
DR PeptideAtlas; A6QLW8; -.
DR GeneID; 407224; -.
DR KEGG; bta:407224; -.
DR CTD; 10864; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; A6QLW8; -.
DR OrthoDB; 2088942at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015132; F:prostaglandin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015732; P:prostaglandin transport; ISS: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 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="Solute carrier family 22 member 7"
FT /id="PRO_0000317480"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 60004 MW; 4F4CD1B0DE4AD9A9 CRC64;
MGFEELLDKV GGFGPFQLRN VALLALPRVL LPMHFLLPIF LAAVPAHRCA LPGVPDNFSN
EDAWLEAHLP REPDGRLSAC LRFTHPQALP NSTLWGEGQN SGEQPEGEPS TVPCPQGWEY
NHSEFSSTIA TEWDLVCEQK GLNKAISTFF FAGVLVGAEV YGYLSDRFGR RRLLLVAYVS
SLALGLASAA SVSYIMFAIT RTLTGMALAG FTIIVMPLEL EWLDVRHRTV AGVLSSTFWT
GGVMLLALIG YLIRDWRWLL LTVTLPCVPG ILTLWWVPES ARWLLTQGRV EEAHRYLLRC
ARLNGPPVGE DSLSREALNK VAAAERMVRR PSYLDLFRTP RLRYISLCCM VVWFGVNFSY
YGVSLDLSGL GLNVYLTQLV FGAVELPSKL LVYLSVRHAG RRLTMAGTLL GAALAVGLRI
LVSPEMKSWS TALAVMGKAF SEAAFTTAYL FTSELYPTVL RQTGMGLTAL VGRLGGSLAP
LAALLDGVWL SLPKLAYGGI ALLAACTALL LPETKQAQLP ETIQDVERKS APSSLQEEEM
PMKQVQD
//
