ID   S22A6_MOUSE             Reviewed;         545 AA.
AC   Q8VC69; Q61185;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Solute carrier family 22 member 6 {ECO:0000250|UniProtKB:Q4U2R8};
DE   AltName: Full=Kidney-specific transport protein;
DE   AltName: Full=Novel kidney transcript {ECO:0000303|PubMed:9045672};
DE            Short=mNKT {ECO:0000303|PubMed:9045672};
DE   AltName: Full=Organic anion transporter 1 {ECO:0000303|PubMed:14979872};
DE            Short=mOAT1 {ECO:0000303|PubMed:14979872};
DE   AltName: Full=Renal organic anion transporter 1;
DE            Short=mROAT1;
GN   Name=Slc22a6 {ECO:0000312|MGI:MGI:892001}; Synonyms=Nkt, Oat1;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   MISCELLANEOUS.
RC   STRAIN=BALB/cJ; TISSUE=Kidney;
RX   PubMed=9045672; DOI=10.1074/jbc.272.10.6471;
RA   Lopez-Nieto C.E., You G., Bush K.T., Barros E.J., Beier D.R., Nigam S.K.;
RT   "Molecular cloning and characterization of NKT, a gene product related to
RT   the organic cation transporter family that is almost exclusively expressed
RT   in the kidney.";
RL   J. Biol. Chem. 272:6471-6478(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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=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, AND MISCELLANEOUS.
RX   PubMed=9880528; DOI=10.1074/jbc.274.3.1519;
RA   Kuze K., Graves P., Leahy A., Wilson P., Stuhlmann H., You G.;
RT   "Heterologous expression and functional characterization of a mouse renal
RT   organic anion transporter in mammalian cells.";
RL   J. Biol. Chem. 274:1519-1524(1999).
RN   [5]
RP   SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX   PubMed=10744714; DOI=10.1074/jbc.275.14.10278;
RA   You G., Kuze K., Kohanski R.A., Amsler K., Henderson S.;
RT   "Regulation of mOAT-mediated organic anion transport by okadaic acid and
RT   protein kinase C in LLC-PK(1) cells.";
RL   J. Biol. Chem. 275:10278-10284(2000).
RN   [6]
RP   SUBCELLULAR LOCATION, DOMAIN, MISCELLANEOUS, AND MUTAGENESIS OF CYS-49;
RP   CYS-78; CYS-99; CYS-122; CYS-172; CYS-183; CYS-200; CYS-326; CYS-335;
RP   CYS-379; CYS-402; CYS-427 AND CYS-434.
RX   PubMed=14979872; DOI=10.1042/bj20031724;
RA   Tanaka K., Zhou F., Kuze K., You G.;
RT   "Cysteine residues in the organic anion transporter mOAT1.";
RL   Biochem. J. 380:283-287(2004).
RN   [7]
RP   MUTAGENESIS OF ASN-39, GLYCOSYLATION AT ASN-56; ASN-86; ASN-91 AND ASN-107,
RP   AND MISCELLANEOUS.
RX   PubMed=14749323; DOI=10.1074/jbc.m400197200;
RA   Tanaka K., Xu W., Zhou F., You G.;
RT   "Role of glycosylation in the organic anion transporter OAT1.";
RL   J. Biol. Chem. 279:14961-14966(2004).
RN   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15944205; DOI=10.1152/ajpcell.00619.2004;
RA   Bahn A., Ljubojevic M., Lorenz H., Schultz C., Ghebremedhin E., Ugele B.,
RA   Sabolic I., Burckhardt G., Hagos Y.;
RT   "Murine renal organic anion transporters mOAT1 and mOAT3 facilitate the
RT   transport of neuroactive tryptophan metabolites.";
RL   Am. J. Physiol. 289:C1075-C1084(2005).
RN   [9]
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: Secondary active transporter that functions as a Na(+)-
CC       independent organic anion (OA)/dicarboxylate antiporter where the
CC       uptake of one molecule of OA into the cell is coupled with an efflux of
CC       one molecule of intracellular dicarboxylate such as 2-oxoglutarate or
CC       glutarate (PubMed:15944205). Mediates the uptake of OA across the
CC       basolateral side of proximal tubule epithelial cells, thereby
CC       contributing to the renal elimination of endogenous OA from the
CC       systemic circulation into the urine (By similarity). Functions as a
CC       biopterin transporters involved in the uptake and the secretion of
CC       coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and
CC       sepiapterin to urine, thereby determining baseline levels of blood
CC       biopterins (By similarity). Transports prostaglandin E2 (PGE2) and
CC       prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal
CC       excretion (By similarity). Involved in the transport of neuroactive
CC       tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA)
CC       (PubMed:15944205). May transport glutamate. Also involved in the
CC       disposition of uremic toxins and potentially toxic xenobiotics by the
CC       renal organic anion secretory pathway, helping reduce their undesired
CC       toxicological effects on the body (By similarity). Uremic toxins
CC       include the indoxyl sulfate (IS), hippurate/N-benzoylglycine (HA),
CC       indole acetate (IA) and 3-carboxy-4- methyl-5-propyl-2-
CC       furanpropionate(CMPF) and urate (By similarity). Xenobiotics include
CC       the mycotoxin ochratoxin (OTA) (By similarity). May also contribute to
CC       the transport of organic compounds in testes across the blood-testis-
CC       barrier (By similarity). {ECO:0000250|UniProtKB:Q4U2R8,
CC       ECO:0000269|PubMed:15944205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(out) + a
CC         dicarboxylate(in) = (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(in) +
CC         a dicarboxylate(out); Xref=Rhea:RHEA:76071, ChEBI:CHEBI:28965,
CC         ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + L-erythro-7,8-dihydrobiopterin(out) = a
CC         dicarboxylate(out) + L-erythro-7,8-dihydrobiopterin(in);
CC         Xref=Rhea:RHEA:76075, ChEBI:CHEBI:28965, ChEBI:CHEBI:43029;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + L-sepiapterin(out) = a
CC         dicarboxylate(out) + L-sepiapterin(in); Xref=Rhea:RHEA:76079,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:194527;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + prostaglandin F2alpha(out) = a
CC         dicarboxylate(out) + prostaglandin F2alpha(in); Xref=Rhea:RHEA:76119,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:57404;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + prostaglandin E2(out) = a
CC         dicarboxylate(out) + prostaglandin E2(in); Xref=Rhea:RHEA:76123,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP(out) + a dicarboxylate(in) = 3',5'-cyclic
CC         AMP(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76127,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:58165;
CC         Evidence={ECO:0000250|UniProtKB:O35956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP(out) + a dicarboxylate(in) = 3',5'-cyclic
CC         GMP(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76131,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:57746;
CC         Evidence={ECO:0000250|UniProtKB:O35956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + urate(out) = a dicarboxylate(out) +
CC         urate(in); Xref=Rhea:RHEA:76135, ChEBI:CHEBI:17775,
CC         ChEBI:CHEBI:28965; Evidence={ECO:0000250|UniProtKB:O35956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutarate(in) + kynurenate(out) = glutarate(out) +
CC         kynurenate(in); Xref=Rhea:RHEA:75999, ChEBI:CHEBI:30921,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15944205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetate(out) + a dicarboxylate(in) = (indol-3-
CC         yl)acetate(in) + a dicarboxylate(out); Xref=Rhea:RHEA:75983,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:30854;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + indoxyl sulfate(out) = a
CC         dicarboxylate(out) + indoxyl sulfate(in); Xref=Rhea:RHEA:75987,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:144643;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + N-benzoylglycine(out) = a
CC         dicarboxylate(out) + N-benzoylglycine(in); Xref=Rhea:RHEA:75991,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:606565;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-carboxy-4-methyl-5-propyl-2-furanpropanoate(out) + a
CC         dicarboxylate(in) = 3-carboxy-4-methyl-5-propyl-2-furanpropanoate(in)
CC         + a dicarboxylate(out); Xref=Rhea:RHEA:75995, ChEBI:CHEBI:28965,
CC         ChEBI:CHEBI:194524; Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:10744714, ECO:0000269|PubMed:14979872,
CC       ECO:0000269|PubMed:15944205}; Multi-pass membrane protein
CC       {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:Q4U2R8};
CC       Multi-pass membrane protein {ECO:0000305}. Note=Localized to the
CC       basolateral side of proximal convoluted tubules corresponding to tubule
CC       segments S1 and S2. {ECO:0000269|PubMed:15944205}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney (PubMed:9045672,
CC       PubMed:9880528, PubMed:15944205). In kidney, restricted to the proximal
CC       convoluted tubule (representing S1 and S2 segments) (PubMed:9045672,
CC       PubMed:15944205). In brain, expressed in neurons of the cortex cerebri
CC       and hippocampus as well as in the ependymal cell layer of the choroid
CC       plexus (PubMed:9045672, PubMed:15944205). {ECO:0000269|PubMed:15944205,
CC       ECO:0000269|PubMed:9045672, ECO:0000269|PubMed:9880528}.
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated with significant
CC       expression beginning at 18 dpc and rising just before birth.
CC       {ECO:0000269|PubMed:9045672}.
CC   -!- DOMAIN: Multiple cysteine residues are necessary for proper targeting
CC       to the plasma membrane. {ECO:0000269|PubMed:14979872}.
CC   -!- PTM: Glycosylated. Glycosylation is necessary for proper targeting of
CC       the transporter to the plasma membrane. {ECO:0000269|PubMed:14749323}.
CC   -!- MISCELLANEOUS: Involved in the renal transport of a variety of drugs
CC       with well-known nephrotoxic potential, therefore may play a role in the
CC       etiology of the drug-associated nephrotoxicity (By similarity). Uptakes
CC       the diagnostic agent PAH/para-aminohippurate and clinically used drugs
CC       (PubMed:9045672, PubMed:9880528, PubMed:10744714, PubMed:14979872,
CC       PubMed:14749323). Mediates the bidirectional transport of PAH/para-
CC       aminohippurate (By similarity). {ECO:0000250|UniProtKB:Q4U2R8,
CC       ECO:0000269|PubMed:10744714, ECO:0000269|PubMed:14749323,
CC       ECO:0000269|PubMed:14979872, ECO:0000269|PubMed:9045672,
CC       ECO:0000269|PubMed:9880528}.
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; U52842; AAC53112.1; -; mRNA.
DR   EMBL; AK035971; BAC29261.1; -; mRNA.
DR   EMBL; BC021647; AAH21647.1; -; mRNA.
DR   CCDS; CCDS29538.1; -.
DR   RefSeq; NP_032792.2; NM_008766.3.
DR   AlphaFoldDB; Q8VC69; -.
DR   SMR; Q8VC69; -.
DR   BioGRID; 201976; 1.
DR   STRING; 10090.ENSMUSP00000010250; -.
DR   BindingDB; Q8VC69; -.
DR   ChEMBL; CHEMBL5653; -.
DR   DrugCentral; Q8VC69; -.
DR   GlyCosmos; Q8VC69; 6 sites, No reported glycans.
DR   GlyGen; Q8VC69; 6 sites.
DR   iPTMnet; Q8VC69; -.
DR   PhosphoSitePlus; Q8VC69; -.
DR   jPOST; Q8VC69; -.
DR   MaxQB; Q8VC69; -.
DR   PaxDb; 10090-ENSMUSP00000010250; -.
DR   ProteomicsDB; 260886; -.
DR   Antibodypedia; 28866; 330 antibodies from 32 providers.
DR   DNASU; 18399; -.
DR   Ensembl; ENSMUST00000010250.4; ENSMUSP00000010250.3; ENSMUSG00000024650.6.
DR   GeneID; 18399; -.
DR   KEGG; mmu:18399; -.
DR   UCSC; uc008gme.2; mouse.
DR   AGR; MGI:892001; -.
DR   CTD; 9356; -.
DR   MGI; MGI:892001; Slc22a6.
DR   VEuPathDB; HostDB:ENSMUSG00000024650; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000157004; -.
DR   HOGENOM; CLU_001265_33_3_1; -.
DR   InParanoid; Q8VC69; -.
DR   OMA; MEAYMGA; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; Q8VC69; -.
DR   TreeFam; TF315847; -.
DR   Reactome; R-MMU-561048; Organic anion transport.
DR   SABIO-RK; Q8VC69; -.
DR   BioGRID-ORCS; 18399; 9 hits in 78 CRISPR screens.
DR   ChiTaRS; Slc22a6; mouse.
DR   PRO; PR:Q8VC69; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8VC69; Protein.
DR   Bgee; ENSMUSG00000024650; Expressed in right kidney and 75 other cell types or tissues.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR   GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA: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:0005452; F:solute:inorganic anion antiporter activity; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
DR   GO; GO:0072237; P:metanephric proximal tubule development; IEA:Ensembl.
DR   GO; GO:0006820; P:monoatomic anion transport; IDA:MGI.
DR   GO; GO:0015711; P:organic anion transport; IMP:UniProtKB.
DR   GO; GO:0015732; P:prostaglandin transport; ISS:UniProtKB.
DR   GO; GO:0097254; P:renal tubular secretion; IMP:UniProtKB.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; ISO:MGI.
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:SF294; SOLUTE CARRIER FAMILY 22 MEMBER 6; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q8VC69; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..545
FT                   /note="Solute carrier family 22 member 6"
FT                   /id="PRO_0000324168"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..419
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        472..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        500..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          515..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14749323"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14749323"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14749323"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14749323"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         39
FT                   /note="N->Q: Complete loss of PAH transport activity."
FT                   /evidence="ECO:0000269|PubMed:14749323"
FT   MUTAGEN         49
FT                   /note="C->A: Decreased cell surface expression level and
FT                   PAH transport activity. Complete loss of PAH transport
FT                   activity; when associated with A-78; A-99; A-122; A-172;
FT                   A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434."
FT                   /evidence="ECO:0000269|PubMed:14979872"
FT   MUTAGEN         122
FT                   /note="C->A: Decreased cell surface expression level and
FT                   PAH transport activity. Complete loss of PAH transport
FT                   activity; when associated with A-49; A-78; A-99; A-172;
FT                   A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434."
FT                   /evidence="ECO:0000269|PubMed:14979872"
FT   MUTAGEN         183
FT                   /note="C->A: Decreased cell surface expression level and
FT                   PAH transport activity. Complete loss of PAH transport
FT                   activity; when associated with A-49; A-78; A-99; A-122;
FT                   A-172; A-200; A-362; A-335; A-379; A-402; A-427 and A-434."
FT                   /evidence="ECO:0000269|PubMed:14979872"
FT   MUTAGEN         434
FT                   /note="C->A: Decreased cell surface expression level and
FT                   PAH transport activity. 80% decrease of PAH transport
FT                   activity; when associated with A-49; A-122 and A-183.
FT                   Complete loss of PAH transport activity; when associated
FT                   with A-49; A-78; A-99; A-122; A-172; A-183; A-200; A-362;
FT                   A-335; A-379; A-402 and A-427."
FT                   /evidence="ECO:0000269|PubMed:14979872"
FT   CONFLICT        66
FT                   /note="W -> R (in Ref. 1; AAC53112)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   545 AA;  60013 MW;  827782E115705C77 CRC64;
     MAFNDLLKQV GGVGRFQLIQ VTMVVAPLLL MASHNTLQNF TAAIPAHHCR PPANANLSKD
     GGLEAWLPLD KQGRPESCLR FPFPHNGTEA NGTGVTEPCL DGWVYDNSTF PSTIVTEWNL
     VCSHRAFRQL AQSLFMVGVL LGAMMFGYLA DRLGRRKVLI LNYLQTAVSG TCAAYAPNYT
     VYCIFRLLSG MSLASIAINC MTLNMEWMPI HTRAYVGTLI GYVYSLGQFL LAGIAYAVPH
     WRHLQLAVSV PFFVAFIYSW FFIESARWYS SSGRLDLTLR ALQRVARING KQEEGAKLSI
     EVLQTSLQKE LTLNKGQASA MELLRCPTLR RLFLCLSMLW FATSFAYYGL VMDLQGFGVS
     MYLIQVIFGA VDLPAKFVCF LVINSMGRRP AQLASLLLAG ICILVNGIIP RGHTIIRTSL
     AVLGKGCLAS SFNCIFLYTG ELYPTMIRQT GLGMGSTMAR VGSIVSPLIS MTAEFYPSIP
     LFIFGAVPVA ASAVTALLPE TLGQPLPDTV QDLKSRSRGK QKQQQLEQQK QMIPLQVSTQ
     EKNGL
//