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S22A6_DANRE
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   03-AUG-2022, entry version 107.
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:0000305}; Multi-pass membrane
CC       protein {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}.
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DR   EMBL; BC066519; AAH66519.1; -; mRNA.
DR   AlphaFoldDB; Q6NYN7; -.
DR   SMR; Q6NYN7; -.
DR   STRING; 7955.ENSDARP00000072353; -.
DR   PaxDb; Q6NYN7; -.
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   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:ZFIN.
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   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 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
 
 
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