S22A8_MACFA
ID S22A8_MACFA Reviewed; 542 AA.
AC Q4W8A2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Solute carrier family 22 member 8;
DE AltName: Full=Organic anion transporter 3;
DE AltName: Full=mkOAT3;
GN Name=SLC22A8; Synonyms=OAT3;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=15846473; DOI=10.1007/s11095-005-2503-0;
RA Tahara H., Shono M., Kusuhara H., Kinoshita H., Fuse E., Takadate A.,
RA Otagiri M., Sugiyama Y.;
RT "Molecular cloning and functional analyses of OAT1 and OAT3 from cynomolgus
RT monkey kidney.";
RL Pharm. Res. 22:647-660(2005).
CC -!- FUNCTION: Plays an important role in the excretion/detoxification of
CC endogenous and exogenous organic anions, especially from the brain and
CC kidney. Transports specifically estrone-3-sulfate (E1S),
CC benzylpenicillin (PCG), methotrexate and estradiol-17-beta-glucuromide.
CC Also transports 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), p-
CC amino-hippurate (PAH) and indoxyl sulfate (IS).
CC {ECO:0000269|PubMed:15846473}.
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. Localized on the abluminal and
CC possibly, luminal membrane of the brain capillary endothelial cells
CC (BCEC). {ECO:0000269|PubMed:15846473}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB182993; BAD99108.1; -; mRNA.
DR RefSeq; NP_001306519.1; NM_001319590.1.
DR AlphaFoldDB; Q4W8A2; -.
DR SMR; Q4W8A2; -.
DR STRING; 9541.XP_005577590.1; -.
DR GeneID; 102122319; -.
DR eggNOG; KOG0255; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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:0015075; F:ion transmembrane transporter activity; IEA:UniProt.
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 InterPro; IPR005829; Sugar_transporter_CS.
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_0000273440"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..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..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..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 514..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"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 542 AA; 59785 MW; 98733DF97C6FE599 CRC64;
MTFSEILDRV GSMGRFQFLH VAILGLPILN MANHNLLQIF TAATPVHHCR LPPNASAGPW
VIPMGPNGKP ERCLRFVHPS NASLPNDTQR SMEPCLDGWV YNSTKDSIVT EWNLVCNSNK
LKEMAQSIFM AGILIGGLVL GDLSDRFGRR PILTCSYLLL AASGSGAAFS PTFPVYVVFR
FLCGCGISGI TLSTVILNVE WVPTRMRAIM STALGYCYTV GQFILPGLAY AIPQWRWLQL
TVSIPFFIFF LSSWWTPESI RWLVLTGKSS KALKILRRVA AFNGKKEEGE RLSLEELKLN
LQKEISLAKA KYTAADLFRI PMLRRMTFCL SLAWFATGFA YYSLAMGVEE FGVNLYILQI
IFGGVDIPAK FITILSLSYL GRHTTQAAAL LLAGGAILAL TFVPLDLQTV RTVLAVFGKG
CLSSSFSCLF LYTSELYPTV IRQTGMGVSN LWTRVGSMLS PLVKITGEVQ PFIPNIIYGI
TALLGGSAAL FLPETLNQPL PETIEDLENW SLRAKEPKQE PEVEKASQRI PLQPYGPDLG
SS
