S22A6_PIG
ID S22A6_PIG Reviewed; 547 AA.
AC Q8MK48; Q8MK47;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 103.
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;
DE AltName: Full=pOAT1;
GN Name=SLC22A6; Synonyms=OAT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
RC TISSUE=Kidney cortex;
RX PubMed=12628298; DOI=10.1016/s0300-9084(02)00022-6;
RA Hagos Y., Bahn A., Asif A.R., Krick W., Sendler M., Burckhardt G.;
RT "Cloning of the pig renal organic anion transporter 1 (pOAT1).";
RL Biochimie 84:1219-1222(2002).
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 2,3-dimercapto-1-
CC 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. Mediates the sodium-independent uptake of p-aminohippurate
CC (PAH). 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). PAH uptake is inhibited by
CC probenecid and alpha-ketoglutarate. {ECO:0000250,
CC ECO:0000269|PubMed:12628298}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.75 uM for PAH {ECO:0000269|PubMed:12628298};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=OAT1-1;
CC IsoId=Q8MK48-1; Sequence=Displayed;
CC Name=2; Synonyms=OAT1-2;
CC IsoId=Q8MK48-2; Sequence=VSP_032170;
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; AJ308234; CAC87128.1; -; mRNA.
DR EMBL; AJ308235; CAC87129.1; -; mRNA.
DR RefSeq; NP_001001261.1; NM_001001261.1.
DR AlphaFoldDB; Q8MK48; -.
DR SMR; Q8MK48; -.
DR STRING; 9823.ENSSSCP00000019937; -.
DR PaxDb; Q8MK48; -.
DR GeneID; 397223; -.
DR KEGG; ssc:397223; -.
DR CTD; 9356; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q8MK48; -.
DR OrthoDB; 464838at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Solute carrier family 22 member 6"
FT /id="PRO_0000324172"
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..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..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..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 511..547
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 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 VAR_SEQ 196..210
FT /note="GMSLAGISLSCMTLN -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12628298"
FT /id="VSP_032170"
FT CONFLICT 157
FT /note="N -> D (in Ref. 1; CAC87129)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="L -> V (in Ref. 1; CAC87129)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="I -> V (in Ref. 1; CAC87129)"
FT /evidence="ECO:0000305"
FT CONFLICT 427..429
FT /note="AVL -> VVV (in Ref. 1; CAC87129)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> F (in Ref. 1; CAC87129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 60063 MW; F9496D6C9C750F50 CRC64;
MAFNDLLLQV GGVGRFQQIQ VTLVVLPLLL MASHNTLQNF TAAIPAHHCR PPADTNLSRD
TELEAWLPRD GQGRPASCLR FTSPQRGPPF PNGTGTNGTG TTEPCTNGWI YDPGTFPSTI
VTEWDLVCSR RALRQLAQSL YMVGVLLGAM IFGYLANRLG RRKVLILNYL QTAVSGTCAA
FAPNFPVYCA FRLLSGMSLA GISLSCMTLN VEWMPIHTRA CVGTLIGYVY SLGQFLLAGV
AYAVPRWRHL QMLVSVPFFA FFIYSWFFIE SARWYSSSGR LDLTLKALQR VAWINGKREE
GASLSMEVLR ASLNKELTMD KGQASAMELL RCPVLRRLFL CLSLLWFATS FAYYGLVMDL
QGFGVSIYLI QVIFGAVDLP AKLVGFLVIN TMGRRPAQMA SLLLAGICIL INGVVPQDQS
IVRTALAVLG KGCLAASFNC IFLYTGELYP TMIRQTGLGM GSTLARVGSI VSPLVSMTAE
LYPSMPLFIY GAVPVAASAA TALLPETLGQ PLPDTVQDVE SRRKRQRRRQ KQQQEQQKQM
VPLQASA
