S22A8_RABIT
ID S22A8_RABIT Reviewed; 542 AA.
AC Q8HY24;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Solute carrier family 22 member 8;
DE AltName: Full=Organic anion transporter 3;
DE AltName: Full=rbOAT3;
GN Name=SLC22A8; Synonyms=OAT3;
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., Roediger M., Lorenz H., Hagos Y., Burckhardt G.;
RT "Molecular cloning and characterization of rabbit organic anion transporter
RT 3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X., Wright S.H.;
RT "Molecular cloning of rabbit organic anion transporter rabbit OAT3 and
RT functional comparisons with rabbit OAT1.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the excretion/detoxification of
CC endogenous and exogenous organic anions, especially from the brain and
CC kidney. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Note=Localizes on the brush border
CC membrane of the choroid epithelial cells. Localizes to the basolateral
CC membrane of the proximal tubular cells. Localizes on the abluminal and
CC possibly, luminal membrane of the brain capillary endothelial cells
CC (BCEC) (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; AJ489526; CAD34035.1; -; mRNA.
DR EMBL; AF533644; AAQ10307.1; -; mRNA.
DR RefSeq; NP_001075590.1; NM_001082121.2.
DR RefSeq; XP_008272547.1; XM_008274325.2.
DR AlphaFoldDB; Q8HY24; -.
DR SMR; Q8HY24; -.
DR STRING; 9986.ENSOCUP00000022206; -.
DR Ensembl; ENSOCUT00000023266; ENSOCUP00000022206; ENSOCUG00000024091.
DR GeneID; 100008845; -.
DR KEGG; ocu:100008845; -.
DR CTD; 9376; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000157004; -.
DR HOGENOM; CLU_001265_33_3_1; -.
DR InParanoid; Q8HY24; -.
DR OMA; RIPLQPC; -.
DR OrthoDB; 464838at2759; -.
DR TreeFam; TF315847; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000024091; Expressed in kidney and 15 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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; Detoxification; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..542
FT /note="Solute carrier family 22 member 8"
FT /id="PRO_0000273444"
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..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 518..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1U7"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 542 AA; 59584 MW; 90AECA4DAC87ED86 CRC64;
MTFSEILDRV GSMGPFQFLH VALLGFPILG MANHNLLQIF TATTPSHHCR PPPNASAGPW
VLPVNQNGQT ERCLRFVHPP NASLPNDTQG ATEPCLDGWV YNSTRDTIVT EWDLVCSSNK
LKEMAQSIFM AGILIGGLVL GDLSDRFGRK PILTCCYLLL AASGSSTAFS PTLPIYMVFR
FLCGFSISGI SLSTVILNVE WVPTKMRAIT STAIGYCYTI GQFILPGLAY AIPQWRWLQL
TVSVPYFIFS LLSWWIPESI RWLVLAGKSS KALKILRRVA TFNGKKEEGE KLSLEELKLS
LQKDISLAKA KYSTADLFRT PILRRVTLCL SLAWFATGFA YYSLAMGVEE FGVNIYILQI
IFGGVDIPAK FITILSLSYL GRHITQGAAL ILAGAAILSL IFVPMDMSLL RTILAVFGKG
CLSGSFSCLF LYTSELFPTV IRQTGMGISN VWARVGSMIS PLVKITGEIQ PFIPNIIYGT
VALLGGSAAL FLPETLNQPL PETLEDMENW FLQSKKLKQE PEAEKASQRI PLQPSGPGVD
RS