S22A6_BOVIN
ID S22A6_BOVIN Reviewed; 549 AA.
AC Q864Z3; A7E342;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 113.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Geyer J., Petzinger E.;
RT "Cloning of the organic anion transporter 1 from bovine kidney.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q864Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q864Z3-2; Sequence=VSP_032167;
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; AJ549816; CAD71145.1; -; mRNA.
DR EMBL; BT021760; AAX46607.1; -; mRNA.
DR EMBL; BC151704; AAI51705.1; -; mRNA.
DR RefSeq; NP_001001143.1; NM_001001143.2.
DR AlphaFoldDB; Q864Z3; -.
DR SMR; Q864Z3; -.
DR STRING; 9913.ENSBTAP00000018132; -.
DR PaxDb; Q864Z3; -.
DR GeneID; 407180; -.
DR KEGG; bta:407180; -.
DR CTD; 9356; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q864Z3; -.
DR OrthoDB; 464838at2759; -.
DR Proteomes; UP000009136; 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..549
FT /note="Solute carrier family 22 member 6"
FT /id="PRO_0000324165"
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..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..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..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..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 521..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
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"
FT VAR_SEQ 1..130
FT /note="MAFNDLLLQLGGVGRFQKIQVTLVILPLILLASHNTLQNFTAAIPTHHCRPP
FT ADTNLSEDGDLEAWLPRDGQGRPESCLLFTSPQRGPPFPNGTETNGTGATEPCPHGWIY
FT DNSTFPSTIVTEWDLVCSH -> MGRGGPSPASSSPPPSGDRPFPMAQRPTAQGPQSPV
FT PTAGSTTTAPSLPPSSL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032167"
FT CONFLICT 162
FT /note="R -> Q (in Ref. 1; CAD71145 and 2; AAX46607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 60184 MW; 8D4793CC3C408B69 CRC64;
MAFNDLLLQL GGVGRFQKIQ VTLVILPLIL LASHNTLQNF TAAIPTHHCR PPADTNLSED
GDLEAWLPRD GQGRPESCLL FTSPQRGPPF PNGTETNGTG ATEPCPHGWI YDNSTFPSTI
VTEWDLVCSH RALRQLAQSL YMMGVLLGAM TFGCLADRLG RRKVLIFNYL QTAVSGTCAA
FAPNFPAYCA FRFLSGMSTA GVVLNCMTLN VEWMPIHTRA YVGTLTGYVY SLGQFLLAGM
AYAVPHWRYL QLLVSAPFFA FFIYSWFFIE SARWYASSGR LDLTLRNLQR VAWINGKQEE
GANLSMEALQ ASLKKELTTG KSQASALELI RCPALRRLFL CLSMLWFATS FAYYGLVMDL
QGFGVSIYLI QVIFGAVDLP AKLVSFLVIN NVGRRPAQMA SLLLAGICIL INGVVPKDKS
IVRTSLAVLG KGCLASSFNC IFLYTGEVYP TMIRQTGLGM GSTLARVGSI VSPLVSMTAE
LYPSVPLFIY GAVPVAASAA IALLPETLGQ PLPDTVQDVE NRRRGKTRKQ QEELQKQMVP
LQASAQVKN
