S22A6_RABIT
ID S22A6_RABIT Reviewed; 551 AA.
AC Q9TSY7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, 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 AltName: Full=rbROAT1;
GN Name=SLC22A6; Synonyms=OAT1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Bahn A., Knabe M., Hillemann A., Burckhardt G.;
RT "Molecular cloning and characterization of a renal organic anion
RT transporter of the rabbit (rbOAT1).";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=12391276; DOI=10.1124/mol.62.5.1128;
RA Bahn A., Knabe M., Hagos Y., Rodiger M., Godehardt S., Graber-Neufeld D.S.,
RA Evans K.K., Burckhardt G., Wright S.H.;
RT "Interaction of the metal chelator 2,3-dimercapto-1-propanesulfonate with
RT the rabbit multispecific organic anion transporter 1 (rbOAT1).";
RL Mol. Pharmacol. 62:1128-1136(2002).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12538807; DOI=10.1124/jpet.102.043455;
RA Groves C.E., Munoz L., Bahn A., Burckhardt G., Wright S.H.;
RT "Interaction of cysteine conjugates with human and rabbit organic anion
RT transporter 1.";
RL J. Pharmacol. Exp. Ther. 304:560-566(2003).
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 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), 3-
CC carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone
CC sulfate (By similarity). Mediates the sodium-independent uptake of p-
CC aminohippurate (PAH) and 2,3-dimercapto-1-propanesulfonic acid (DMPS).
CC PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS),
CC diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac,
CC carprofen, okadaic acid, furosemide, steviol, phorbol 12-myristate 13-
CC acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide,
CC losartan, probenecid, phenol red and glutarate (By similarity). PAH
CC uptake is inhibited by benzothiazolylcysteine (BTC), S-
CC chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-
CC dichlorovinylcysteine (DCVC), urate, alpha-ketoglutarate and
CC probenecid. {ECO:0000250, ECO:0000269|PubMed:12391276,
CC ECO:0000269|PubMed:12538807}.
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; AJ242871; CAB62587.1; -; mRNA.
DR RefSeq; NP_001075596.1; NM_001082127.1.
DR AlphaFoldDB; Q9TSY7; -.
DR SMR; Q9TSY7; -.
DR PRIDE; Q9TSY7; -.
DR GeneID; 100008851; -.
DR KEGG; ocu:100008851; -.
DR CTD; 9356; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q9TSY7; -.
DR OrthoDB; 464838at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
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 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; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..551
FT /note="Solute carrier family 22 member 6"
FT /id="PRO_0000324169"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 520..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 60589 MW; 69C25F96B154517E CRC64;
MAFNDLLKQV GGVGRFQRIQ VTLVVLPLLL MASHNTLQNF TAAIPPHHCR PPAHANLSKD
GGLQAWLPQD TQGRPKSCLR FTSPQERPPF LNGTEANGTG TTEPCTDGWI YDNSTFPSTI
VTEWDLVCSH RALRQLGQSL YMAGVLIGAM VFGYLADRLG RRKVLILNYL QTAVSGTCAA
FSPNFTVYCT FRLLSGMSLA GIALNCMTLN VEWMPIHTRA YVGTLAGYVY STGQFLLAGV
AYAVPHWRYL QLLVSVPFFA FFVYSWFFIE SARWYSTPGR LDLTLKALQK VARINGKQEE
GAKLSMEVLR TNLQKELTMS KGQASAMELL RCPALRHLFL CLSLLWFATS FAYYGLVMDL
QGFGVSIYLI QVIFGAVDLP AKLVCFLVIN SLGRRPAQMA SLLLAGICIL VNGVIPRDQS
IVRTSLAVLG KGCLASSFNC IFLYTGELYP TMIRQTGLGM GSTMARVGSI VSPLVSMTSE
LYPSLPLFIY GAVPVAASAA TALLPETLGQ PLPDTVQDLE SRRRGKPRRQ QQEQQKQMVP
LQASVQEKNG L
