ID   S226A_XENLA             Reviewed;         558 AA.
AC   Q66J54;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Solute carrier family 22 member 6-A;
DE   AltName: Full=Organic cation transporter 1-A;
DE   AltName: Full=Renal organic anion transporter 1-A;
DE            Short=ROAT1-A;
GN   Name=slc22a6-a; Synonyms=oat1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the renal elimination of endogenous and exogenous
CC       organic anions. Mediates the sodium-independent uptake of p-
CC       aminohippurate (PAH), 2,3-dimercapto-1-propanesulfonic acid (DMPS),
CC       cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-
CC       phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA),
CC       acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD),
CC       2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate
CC       (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-
CC       furanpropionate (CMPF) and edaravone sulfate. PAH uptake is inhibited
CC       by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate
CC       (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid,
CC       benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC),
CC       cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide,
CC       steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore
CC       A23187, benzylpenicillin, bumetamide, losartan, probenecid, phenol red,
CC       urate, glutarate and alpha-ketoglutarate (By similarity).
CC       {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; BC081055; AAH81055.1; -; mRNA.
DR   RefSeq; NP_001087661.1; NM_001094192.1.
DR   AlphaFoldDB; Q66J54; -.
DR   SMR; Q66J54; -.
DR   DNASU; 447485; -.
DR   GeneID; 447485; -.
DR   KEGG; xla:447485; -.
DR   CTD; 447485; -.
DR   Xenbase; XB-GENE-22061136; slc22a8.S.
DR   OrthoDB; 704438at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 447485; Expressed in kidney and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015075; F:ion transmembrane transporter activity; IEA:UniProt.
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   InterPro; IPR004749; Orgcat_transp/SVOP.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00898; 2A0119; 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..558
FT                   /note="Solute carrier family 22 member 6-A"
FT                   /id="PRO_0000324175"
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..140
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..253
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..369
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..400
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..428
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        450..462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        484..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..558
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          539..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  62453 MW;  7A56F314DAB130A4 CRC64;
     MSFAELLERT GGMGRFQITQ VALMCFPILL MASHNLLQNF SAAIPDHKCK ANDTWYQSNN
     TDRMGYVRLS APLDADGQPD RCLEYVEVQW MIAGTNRTWA NSSQLATRPC TEGWEYSKDE
     FNSTIITEWD LVCGHKNRRQ LAQSVYMGGV LVGAIILGGL SDRYGRRALL IWSYFQMAVS
     GLCSAFSPNY LSYCIFRFLT GMALSGIGLN TTALIVEWVP TRVRTITGTL AGFSYTVGQL
     LLAGLAYAMR DWRWLQLCVS LPFFIFFLYS WWFPESARWL VLSGKTERAV KEMKKVAKLN
     GKEEEGEKIT LESMRSDMIK ELACAKSSYT VIDLIRTSTI RRISCALSLV WFSTSFAYYG
     LAMDLQNFNV SIYLIQVIFG AVDFPAKIFS TTAMIYVGRK FTQLMSLILG GVVILANSFV
     PHEMQTVRTG MAVFGKGCLA ASFSCVFLYT TELYPTVIRQ SGLGLCSTMA RIGGIVAPLV
     KILGEYYPFL PLVIYGGAPI ISGLCVFFLP ETVNKPLPDT IEEVEKRIKA PKKENEMNEI
     VSLKKKEGMK ENPVNDVL