ID S22A7_PONAB Reviewed; 548 AA.
AC Q5R540;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861035; CAH93126.1; -; mRNA.
DR RefSeq; NP_001127633.1; NM_001134161.1.
DR AlphaFoldDB; Q5R540; -.
DR SMR; Q5R540; -.
DR STRING; 9601.ENSPPYP00000018610; -.
DR Ensembl; ENSPPYT00000036745.1; ENSPPYP00000029437.1; ENSPPYG00000016637.3.
DR GeneID; 100174712; -.
DR KEGG; pon:100174712; -.
DR CTD; 10864; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154922; -.
DR HOGENOM; CLU_001265_33_3_1; -.
DR InParanoid; Q5R540; -.
DR OMA; QAFFYNA; -.
DR OrthoDB; 2088942at2759; -.
DR Proteomes; UP000001595; Chromosome 6.
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; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
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; PF07690; MFS_1; 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..548
FT /note="Solute carrier family 22 member 7"
FT /id="PRO_0000317484"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 522..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60043 MW; 21357A182FD04D57 CRC64;
MGFEELLEQV GGFGPFQLRN VALLALPRVL LPLHFLLPIF LAAVPAHRCA LPGAPANFSH
QDVWLEAHLP REPDGTLSSC LRFAYPQALP NTTLGEERQS RGELEDEPAT VPCSQGWEYD
RSEFSSTIAT ESQWDLVCEQ KGLNRAASTF FFAGVLVGAV AFGYLSDRFG RRRLLLVAYV
STLVLGLASA ASVSYVMFAI TRTLTGSALA GFTIIVMPLE LEWLDVEHRT VAGVLSSTFW
TGGMMLLALV GYLIRDWRWL LLAVTLPCAP GILSLWWVPE SARWLLTQGH VKEAHRYLLH
CARLNGRPVC EDSLSQEAVS KVAAGERVVR RPSYLDLFRT PRLRHISLCC VVVWFGVNFS
YYGLSLDVSG LGLNVYQTQL LFGAVELPSK LLVYLSVRYA GRRLTQAGTL LGTALAFGTR
LLVSSDMKSW STVLAVMGKA FSEAAFTTAY LFTSELYPTV LRQTGMGLTA LVGRLGGSLA
PLAALLDGVW LSLPKLTYGG IALLAAGTAL LLPETRQAQL PETIQDVERK SAPTSLQEEE
MPMKQVQN
//
