ID S22A6_DANRE Reviewed; 560 AA. AC Q6NYN7; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Solute carrier family 22 member 6; DE AltName: Full=Organic anion transporter 1; DE AltName: Full=Renal organic anion transporter 1; DE Short=ROAT1; GN Name=slc22a6; Synonyms=oat; ORFNames=zgc:77073; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the renal elimination of endogenous and exogenous CC organic anions. Functions as organic anion exchanger when the uptake of CC one molecule of organic anion is coupled with an efflux of one molecule CC of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). CC Mediates the sodium-independent uptake of p-aminohippurate (PAH), 2,3- CC dimercapto-1-propanesulfonic acid (DMPS), cidofovir, adefovir, 9-(2- CC phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) CC diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido- CC 3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro-phenoxyacetate CC (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and CC 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone CC sulfate. PAH uptake is inhibited by p-chloromercuribenzenesulphonate CC (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, CC diclofenac, carprofen, okadaic acid, benzothiazolylcysteine (BTC), S- CC chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S- CC dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate CC 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, CC bumetamide, losartan, probenecid, phenol red, urate, glutarate and CC alpha-ketoglutarate (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VC69}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VC69}. Basolateral CC cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane CC protein {ECO:0000305}. Basal cell membrane CC {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein CC {ECO:0000305}. CC -!- DOMAIN: Multiple cysteine residues are necessary for proper targeting CC to the plasma membrane. {ECO:0000250}. CC -!- PTM: Glycosylated. Glycosylation is necessary for proper targeting of CC the transporter to the plasma membrane (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC066519; AAH66519.1; -; mRNA. DR AlphaFoldDB; Q6NYN7; -. DR SMR; Q6NYN7; -. DR STRING; 7955.ENSDARP00000072353; -. DR PaxDb; 7955-ENSDARP00000072353; -. DR AGR; ZFIN:ZDB-GENE-040426-2249; -. DR ZFIN; ZDB-GENE-040426-2249; slc22a6l. DR eggNOG; KOG0255; Eukaryota. DR InParanoid; Q6NYN7; -. DR PhylomeDB; Q6NYN7; -. DR Reactome; R-DRE-561048; Organic anion transport. DR PRO; PR:Q6NYN7; -. DR Proteomes; UP000000437; Genome assembly. DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN. DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:ZFIN. DR CDD; cd17446; MFS_SLC22A6_OAT1_like; 1. 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 PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1. DR PANTHER; PTHR24064:SF439; SOLUTE CARRIER FAMILY 22 MEMBER 8; 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; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..560 FT /note="Solute carrier family 22 member 6" FT /id="PRO_0000324173" FT TOPO_DOM 1..15 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 16..36 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 37..143 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 144..164 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 165..170 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 171..191 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 192..201 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 202..222 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 223..228 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 229..249 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 250..256 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 257..277 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 278..345 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 367..374 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 375..395 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 396..406 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 407..427 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 428..433 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 434..454 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 455..465 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 466..486 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 487..491 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 492..512 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 513..560 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 560 AA; 61972 MW; 14D3F32AB9771D45 CRC64; MAFSDLLEQV GSTGRFQVLH VTLLSMPILM MASHNLLQNF VAAVPPHHCQ PHANLSMSST DAVDVLRATV PLGLNGKLER CKRYTTPQWQ ILSLNTSESL WDESMAETET QSCEDGWFYN MTEMSSTIIT EWDLVCDYRA LKQMSQTTYM GGVLVGAIVF GGLSDRFGRR VLLLISNLMM AIGGTCVAFS TSFTMFCVFR VCCGMALSGL VLNSFSLIVE WIPTRVRTVV GTGTGYCYTT GQLILAAVAY CIRDWRWLTL AVSLPFYVSF LYSWWFLESA RWLVLTKNPE QAVKNLKTVA RINGRSAEGD KIDLEMLQES MKKEMACSKG SYSALDLLRT STMRTITICL SAVWFSTSFA YYGLSMDLQK FGVSIYLIQI IFGAVDIPAK IIVTICMSML GRRPSQCGAL VLAGIMILIN LLVPSDLQML RTSLAVIGKG CLAASFNCCY LYAGELYPTV IRQSGMGWVS MMARFGAMVA PMVLLLGDDY PWIPGFIYGG APIVSGIFAF FLPETLSQPL PDTIQDIDDR GLARTNSKRL PEKLDLAMKD PSCVLLKESV //