ID   SO1A5_MOUSE             Reviewed;         670 AA.
AC   Q91YY5; Q91XS2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Solute carrier organic anion transporter family member 1A5;
DE   AltName: Full=Organic anion-transporting polypeptide 3;
DE            Short=OATP-3;
DE   AltName: Full=Sodium-independent organic anion transporter 3;
DE   AltName: Full=Solute carrier family 21 member 7;
GN   Name=Slco1a5; Synonyms=Oatp1a5, Oatp3, Slc21a7;
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=Brain;
RX   PubMed=11093941; DOI=10.1152/ajpgi.2000.279.6.g1188;
RA   Walters H.C., Craddock A.L., Fusegawa H., Willingham M.C., Dawson P.A.;
RT   "Expression, transport properties, and chromosomal location of organic
RT   anion transporter subtype 3.";
RL   Am. J. Physiol. 279:G1188-G1200(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=15255953; DOI=10.1111/j.1471-4159.2004.02549.x;
RA   Ohtsuki S., Takizawa T., Takanaga H., Hori S., Hosoya K., Terasaki T.;
RT   "Localization of organic anion transporting polypeptide 3 (oatp3) in mouse
RT   brain parenchymal and capillary endothelial cells.";
RL   J. Neurochem. 90:743-749(2004).
CC   -!- FUNCTION: Na(+)-independent transporter that mediates the cellular
CC       uptake of a broad range of organic anions such as the endogenous bile
CC       salts cholate and deoxycholate, either in their unconjugated or
CC       conjugated forms (taurocholate and glycocholate), estrone 3-sulfate and
CC       prostaglandin E2, at the plasma membrane. Responsible for intestinal
CC       absorption of bile acids. Capable of thyroid hormone transport (both T3
CC       or 3,3',5'-triiodo-L-thyronine, and T4 or L-tyroxine) (By similarity).
CC       Plays roles in blood-brain and -cerebrospinal fluid barrier transport
CC       of organic anions and signal mediators, and in hormone uptake by neural
CC       cells (PubMed:15255953). May also play a role in the reuptake of
CC       neuropeptides such as substance P/TAC1 and vasoactive intestinal
CC       peptide/VIP released from retinal neurons (By similarity). Shows a pH-
CC       sensitive substrate specificity which may be ascribed to the
CC       protonation state of the binding site and leads to a stimulation of
CC       substrate transport in an acidic microenvironment.
CC       Hydrogencarbonate/HCO3(-) acts as the probable counteranion that
CC       exchanges for organic anions (By similarity). May contribute to
CC       regulate the transport of organic compounds in testis across the blood-
CC       testis-barrier (By similarity). {ECO:0000250|UniProtKB:O88397,
CC       ECO:0000250|UniProtKB:P46721, ECO:0000303|PubMed:15255953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC         ChEBI:CHEBI:36257; Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851,
CC         ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in);
CC         Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in);
CC         Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,3',5'-triiodo-L-thyronine(out) = 3,3',5'-triiodo-L-
CC         thyronine(in); Xref=Rhea:RHEA:71815, ChEBI:CHEBI:57261;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurodeoxycholate(out) = taurodeoxycholate(in);
CC         Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycodeoxycholate(out) = glycodeoxycholate(in);
CC         Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in);
CC         Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in);
CC         Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:O88397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=substance P(out) = substance P(in); Xref=Rhea:RHEA:74367,
CC         ChEBI:CHEBI:190692; Evidence={ECO:0000250|UniProtKB:P46721};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46721};
CC       Multi-pass membrane protein {ECO:0000305}. Basal cell membrane
CC       {ECO:0000250|UniProtKB:P46721}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, choroid plexus and lung, but
CC       not in liver or kidney. {ECO:0000269|PubMed:15255953}.
CC   -!- DOMAIN: A conserved histidine residue in the third TMD (His-107) may
CC       play an essential role in the pH sensitivity of SLCO1A5/OATP1A5-
CC       mediated substrate transport. {ECO:0000250|UniProtKB:O88397}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; AF240694; AAK39416.1; -; mRNA.
DR   EMBL; BC013594; AAH13594.1; -; mRNA.
DR   CCDS; CCDS57464.1; -.
DR   RefSeq; NP_001254636.1; NM_001267707.1.
DR   RefSeq; NP_570931.1; NM_130861.3.
DR   AlphaFoldDB; Q91YY5; -.
DR   SMR; Q91YY5; -.
DR   STRING; 10090.ENSMUSP00000137607; -.
DR   GlyCosmos; Q91YY5; 4 sites, No reported glycans.
DR   GlyGen; Q91YY5; 4 sites.
DR   iPTMnet; Q91YY5; -.
DR   PhosphoSitePlus; Q91YY5; -.
DR   SwissPalm; Q91YY5; -.
DR   jPOST; Q91YY5; -.
DR   MaxQB; Q91YY5; -.
DR   PaxDb; 10090-ENSMUSP00000080116; -.
DR   ProteomicsDB; 261308; -.
DR   DNASU; 108096; -.
DR   GeneID; 108096; -.
DR   KEGG; mmu:108096; -.
DR   UCSC; uc009epa.2; mouse.
DR   AGR; MGI:1351865; -.
DR   CTD; 108096; -.
DR   MGI; MGI:1351865; Slco1a5.
DR   eggNOG; KOG3626; Eukaryota.
DR   InParanoid; Q91YY5; -.
DR   OrthoDB; 2874223at2759; -.
DR   PhylomeDB; Q91YY5; -.
DR   TreeFam; TF317540; -.
DR   BioGRID-ORCS; 108096; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Slco1a5; mouse.
DR   PRO; PR:Q91YY5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q91YY5; Protein.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; ISO:MGI.
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:0015349; F:thyroid hormone transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR   GO; GO:0050892; P:intestinal absorption; ISO:MGI.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015718; P:monocarboxylic acid transport; ISO:MGI.
DR   GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF148; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER-RELATED; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport;
KW   Lipid transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..670
FT                   /note="Solute carrier organic anion transporter family
FT                   member 1A5"
FT                   /id="PRO_0000191043"
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   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"
FT   CONFLICT        280
FT                   /note="A -> D (in Ref. 1; AAK39416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        591
FT                   /note="I -> M (in Ref. 1; AAK39416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        644
FT                   /note="Q -> L (in Ref. 1; AAK39416)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        656
FT                   /note="G -> R (in Ref. 1; AAK39416)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   670 AA;  74663 MW;  AF802A903FCD457D CRC64;
     MGETEKRIAT HGVRCFSKIK MFLLALTCAY VSKSLSGIYM NSMLTQIERQ FDIPTSIVGL
     INGSFEIGNL LLIILVSYFG TKLHRPIMIG IGCVIMGLGC FLMSLPHFLM GRYEYETTIS
     PTSNLSSNSF LCMENRTQTL KPTQDPAECV KEMKSLMWIY VLVGNIIRGI GETPIMPLGI
     SYIEDFAKSE NSPLYIGILE SGKMIGPIVG LLLGSFCARI YVDTGSVNTD DLTITPTDTR
     WVGAWWIGFL VCAGVNILTS IPFFFFPKTL PKEGLQDNVA RTENDKEEKH REKAKEENRG
     ITKDFLPFMK SLSCNPIYML LILTSVLQIN AFINMFTFLP KYLEQQYGKS TSEVVLLIGV
     CNLPPICIGY LLIGFIMKKF RITVKKAAYM AFCLSLFEYL LSYFHFMISC DNFQVAGLTT
     SYEGVQHPLY VENKVLADCN TRCSCLTNTW DPVCGDNGLS YMSACLAGCE KSVGMGTHMV
     FQNCSCIQSS GNSSAVLGLC KKGPECANKL QYFLIMSVIG SFIYSITAIP GYMVLLRCIK
     SEEKSLGIGL HAFCTRIFAG IPAPIYFGAL IDRTCLHWGT LKCGEPGACR IYNINNFRRI
     YLVLPAALRG SSYLPAFFIL ILMRKFQLPG EMYSSETELA DMKQTVKKSE CTDVHGIPKV
     ENDGELKTKL
//