S22A6_PONAB
ID S22A6_PONAB Reviewed; 550 AA.
AC Q5RCH6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=OAT1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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 -!- 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; CR858294; CAH90531.1; -; mRNA.
DR AlphaFoldDB; Q5RCH6; -.
DR SMR; Q5RCH6; -.
DR STRING; 9601.ENSPPYP00000003625; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q5RCH6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
DR GO; GO:0015711; P:organic anion transport; ISS:UniProtKB.
DR GO; GO:0097254; P:renal tubular secretion; ISS:UniProtKB.
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..550
FT /note="Solute carrier family 22 member 6"
FT /id="PRO_0000324170"
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..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..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 514..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
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 550 AA; 60306 MW; CF4B2A1B2673EB30 CRC64;
MAFNDLLQQV GGVGRFQQIQ VTLVVLPLLL MASHNTLQNF TAAIPTHHCR PPADANLSKN
GGLEVWLPRD RKGQPESCLR FTSPQWGPPF PNGTEANGTG ATEPCTDGWI YDNSTFPSTI
VTEWDLVCSH RALRQLAQSL YMVGVLLGAM VFGYLADRLG RRKVLILNYL QTAVSGTCTA
FAPNFSIYCA FRLLSGMSLA GISLNCMTLN VEWMPIHTRA CVGTLIGYVY SLGQFLLAGV
AYAVPHWRHL QLLVSAPFFA FFIYSWFFIE SARWHSSSGR LDLTLRALQR VARINGKREE
GAKLSMEVLR ASLQKELTMG KGQASAMELL RCPTLRHLFL CLSMLWFATS FAYYGLVMDL
QGFGVSIYLI QVIFGAVDLP AKLVGFLVIN SLGRRPAQMA ALLLAGICIL LNGVIPQDQS
IVRTSLAVPG KGCLAASFNC IFLYTGELYP TMIRQTGMGM GSTMARVGSI VSPLVSMTAE
LYPSMPLFIY GAVPVAASAV TVLLPETLGQ PLPDTVQDLE SRKGKQTRQQ QEHQKYMVPL
QASAQEKNGL
