SO1A1_MOUSE
ID SO1A1_MOUSE Reviewed; 670 AA.
AC Q9QXZ6;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Solute carrier organic anion transporter family member 1A1;
DE AltName: Full=Sodium-independent organic anion-transporting polypeptide 1;
DE Short=OATP-1;
DE AltName: Full=Solute carrier family 21 member 1;
GN Name=Slco1a1; Synonyms=Oatp1a1, Slc21a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10600646; DOI=10.1042/bj3450115;
RA Hagenbuch B., Adler I.-D., Schmid T.E.;
RT "Molecular cloning and functional characterization of the mouse organic
RT anion transporting polypeptide 1 (Oatp1) and mapping of the gene to
RT chromosome X.";
RL Biochem. J. 345:115-120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11267661; DOI=10.1016/s0167-4781(01)00169-5;
RA Isern J., Hagenbuch B., Stieger B., Meier P.J., Meseguer A.;
RT "Functional analysis and androgen-regulated expression of mouse organic
RT anion transporting polypeptide 1 (Oatp1) in the kidney.";
RL Biochim. Biophys. Acta 1518:73-78(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Ogura K., Choudhuri S., Klaassen C.D.;
RT "Mouse organic anion transporting polypeptide 1 (oatp1).";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates the Na(+)-independent transport of organic anions
CC such as taurocholate, prostaglandin E2 (PGE2), dehydroepiandrosterone
CC sulfate (DHEAS), 17-beta-glucuronosyl estradiol, estrone-3-sulfate,
CC sulfobromophthalein (BSP), ouabain and gadoxetate.
CC -!- SUBUNIT: Binds to PDZK1. Interaction with PDZK1 is required for
CC expression on hepatocyte surface (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, and at lower levels in
CC kidney. Not detected in other tissues.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AF148218; AAF19351.1; -; mRNA.
DR EMBL; AF223067; AAF31457.1; -; mRNA.
DR EMBL; AB031813; BAB12444.1; -; mRNA.
DR EMBL; BC041147; AAH41147.1; -; mRNA.
DR CCDS; CCDS39691.1; -.
DR RefSeq; NP_038825.1; NM_013797.5.
DR AlphaFoldDB; Q9QXZ6; -.
DR SMR; Q9QXZ6; -.
DR STRING; 10090.ENSMUSP00000037022; -.
DR ChEMBL; CHEMBL2073696; -.
DR GlyGen; Q9QXZ6; 4 sites.
DR iPTMnet; Q9QXZ6; -.
DR PhosphoSitePlus; Q9QXZ6; -.
DR SwissPalm; Q9QXZ6; -.
DR jPOST; Q9QXZ6; -.
DR MaxQB; Q9QXZ6; -.
DR PaxDb; Q9QXZ6; -.
DR PRIDE; Q9QXZ6; -.
DR ProteomicsDB; 261100; -.
DR DNASU; 28248; -.
DR Ensembl; ENSMUST00000042119; ENSMUSP00000037022; ENSMUSG00000041698.
DR GeneID; 28248; -.
DR KEGG; mmu:28248; -.
DR UCSC; uc009eot.2; mouse.
DR CTD; 28248; -.
DR MGI; MGI:1351891; Slco1a1.
DR VEuPathDB; HostDB:ENSMUSG00000041698; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR InParanoid; Q9QXZ6; -.
DR OMA; PETASEW; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9QXZ6; -.
DR TreeFam; TF317540; -.
DR BioGRID-ORCS; 28248; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9QXZ6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QXZ6; protein.
DR Bgee; ENSMUSG00000041698; Expressed in right kidney and 20 other tissues.
DR ExpressionAtlas; Q9QXZ6; baseline and differential.
DR Genevisible; Q9QXZ6; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR GO; GO:0015711; P:organic anion transport; IDA:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..670
FT /note="Solute carrier organic anion transporter family
FT member 1A1"
FT /id="PRO_0000191040"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..377
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..405
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..536
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..571
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..623
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 433..488
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46720"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 439..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 445..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 454..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 670 AA; 74396 MW; 22199F98DDF137EA CRC64;
MEETEKKVAT QEGRFFSKMK VFLMSLTCAY LAKSLSGVYM NSMLTQIERQ FGIPTSVVGF
ITGSFEIGNL LLIVFVSYFG RKLHRPIIIG VGCVVMGLGC FLMASPHFLM GRYKYETTIS
PTSNLSSNSF LCIENRTQTL KPTQDPTECV KEIKSLMWIY VLIGNTMRGI GETPIMPLGI
SYIEDFAKSE NSPLYIGILE MGKIVGPIIG LLLGSFFARV YVDIGSVNTD DLTITPTDTR
WVGAWWIGFL VCAGVNILTS IPFFFFPKTL PKKELQDNVD VTKYEKVEKH RERAKKENLG
ITKDFLPFMK SLCCNPIYML FSLTSVLQIN GFASTFTFLP KYLEQQYGKS TSEAVFLIGV
YSLPPVCLGY LISGFIMKKF KITVKKAAYI AFGLSLSEYF IFLCNYLLTC DNFPVAGLTT
SYKGVQHPLY GEKNVLADCN TRCSCLTDTW DPVCGDNGLA YMSACLAGCE KSVGTGTNMV
FQNCSCIGSS GNSSAVLGLC KKGPECDNKL QYFLIKSVFS SFIFSLAAIP GYMVLLRCVK
SEEKSIGVGL HAFFIRLLAG IPAPVYFGAL IDRTCLHWGT LKCGQPGACR MYDINRFRHI
YLGLPAAVRG SSFLPAVFIL ILMRKFHFPG DIHSPDTELA EMKLTEKESE CTDVCRSPKV
ENDGELKTKL
