ID   SO3A1_HUMAN             Reviewed;         710 AA.
AC   Q9UIG8; A8K4A7; B3KPY5; B3KUR7; C6G486; Q9BW73; Q9GZV2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=Solute carrier organic anion transporter family member 3A1;
DE            Short=OATP3A1 {ECO:0000303|PubMed:16971491};
DE   AltName: Full=Organic anion transporter polypeptide-related protein 3;
DE            Short=OATP-RP3;
DE            Short=OATPRP3;
DE   AltName: Full=Organic anion-transporting polypeptide D;
DE            Short=OATP-D {ECO:0000303|PubMed:14631946};
DE   AltName: Full=PGE1 transporter;
DE   AltName: Full=Sodium-independent organic anion transporter D;
DE   AltName: Full=Solute carrier family 21 member 11;
GN   Name=SLCO3A1; Synonyms=OATP3A1, OATPD, SLC21A11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY
RP   (ISOFORM 1), VARIANT ASP-294, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=10873595; DOI=10.1006/bbrc.2000.2922;
RA   Tamai I., Nezu J., Uchino H., Sai Y., Oku A., Shimane M., Tsuji A.;
RT   "Molecular identification and characterization of novel members of the
RT   human organic anion transporter (OATP) family.";
RL   Biochem. Biophys. Res. Commun. 273:251-260(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-294.
RA   Wu Y., Hsiang B.H., Zhu Y., Yang W.-P., Kirchgessner T.G.;
RT   "Identification and characterization of novel human OATP family members.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-294.
RA   Adachi H., Unno M., Matsuno S., Yawo H., Abe T.;
RT   "Molecular identification of human PGE1 transporter expressed in cancer.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP   ASP-294.
RC   TISSUE=Mesangial cell, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-294.
RC   TISSUE=Brain;
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   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=12409283; DOI=10.1152/ajpendo.00257.2002;
RA   Ugele B., St-Pierre M.V., Pihusch M., Bahn A., Hantschmann P.;
RT   "Characterization and identification of steroid sulfate transporters of
RT   human placenta.";
RL   Am. J. Physiol. 284:E390-E398(2003).
RN   [9]
RP   FUNCTION, TRANSPORTER ACTIVITY (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES
RP   (ISOFORM 1), AND TISSUE SPECIFICITY (ISOFORM 1).
RX   PubMed=14631946; DOI=10.1152/ajprenal.00402.2002;
RA   Adachi H., Suzuki T., Abe M., Asano N., Mizutamari H., Tanemoto M.,
RA   Nishio T., Onogawa T., Toyohara T., Kasai S., Satoh F., Suzuki M.,
RA   Tokui T., Unno M., Shimosegawa T., Matsuno S., Ito S., Abe T.;
RT   "Molecular characterization of human and rat organic anion transporter
RT   OATP-D.";
RL   Am. J. Physiol. 285:F1188-F1197(2003).
RN   [10]
RP   ALTERNATIVE SPLICING, FUNCTION, TRANSPORTER ACTIVITY (ISOFORMS 1 AND 2),
RP   BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION
RP   (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=16971491; DOI=10.1152/ajpcell.00597.2005;
RA   Huber R.D., Gao B., Sidler Pfaendler M.-A., Zhang-Fu W., Leuthold S.,
RA   Hagenbuch B., Folkers G., Meier P.J., Stieger B.;
RT   "Characterization of two splice variants of human organic anion
RT   transporting polypeptide 3A1 isolated from human brain.";
RL   Am. J. Physiol. 292:C795-C806(2007).
RN   [11]
RP   FUNCTION, TRANSPORTER ACTIVITY (ISOFORMS 1 AND 2), AND ACTIVITY REGULATION.
RX   PubMed=19129463; DOI=10.1152/ajpcell.00436.2008;
RA   Leuthold S., Hagenbuch B., Mohebbi N., Wagner C.A., Meier P.J., Stieger B.;
RT   "Mechanisms of pH-gradient driven transport mediated by organic anion
RT   polypeptide transporters.";
RL   Am. J. Physiol. 296:C570-C582(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   ACETYLATION AT MET-1.
RX   PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA   Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA   Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA   Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT   "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT   termini of transmembrane proteins and maintains Golgi integrity.";
RL   Cell Rep. 10:1362-1374(2015).
RN   [14]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND INDUCTION BY FGF19.
RX   PubMed=30063921; DOI=10.1053/j.gastro.2018.07.031;
RA   Pan Q., Zhang X., Zhang L., Cheng Y., Zhao N., Li F., Zhou X., Chen S.,
RA   Li J., Xu S., Huang D., Chen Y., Li L., Wang H., Chen W., Cai S.Y.,
RA   Boyer J.L., Chai J.;
RT   "Solute Carrier Organic Anion Transporter Family Member 3A1 Is a Bile Acid
RT   Efflux Transporter in Cholestasis.";
RL   Gastroenterology 155:1578-1592(2018).
RN   [15]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=35307651; DOI=10.1124/dmd.121.000748;
RA   Hau R.K., Klein R.R., Wright S.H., Cherrington N.J.;
RT   "Localization of Xenobiotic Transporters Expressed at the Human Blood-
RT   Testis Barrier.";
RL   Drug Metab. Dispos. 50:770-780(2022).
CC   -!- FUNCTION: Putative organic anion antiporter with apparent broad
CC       substrate specificity. Recognizes various substrates including thyroid
CC       hormone L-thyroxine, prostanoids such as prostaglandin E1 and E2, bile
CC       acids such as taurocholate, glycolate and glycochenodeoxycholate and
CC       peptide hormones such as L-arginine vasopressin, likely operating in a
CC       tissue-specific manner (PubMed:10873595, PubMed:14631946,
CC       PubMed:16971491, PubMed:19129463, PubMed:30063921). The transport
CC       mechanism, its electrogenicity and potential tissue-specific
CC       counterions remain to be elucidated (Probable).
CC       {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:14631946,
CC       ECO:0000269|PubMed:16971491, ECO:0000269|PubMed:19129463,
CC       ECO:0000269|PubMed:30063921, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:16971491,
CC         ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820;
CC         Evidence={ECO:0000305|PubMed:16971491, ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:16971491,
CC         ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820;
CC         Evidence={ECO:0000305|PubMed:16971491, ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=prostaglandin E1(out) = prostaglandin E1(in);
CC         Xref=Rhea:RHEA:50980, ChEBI:CHEBI:57397;
CC         Evidence={ECO:0000269|PubMed:14631946, ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50981;
CC         Evidence={ECO:0000305|PubMed:14631946, ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=prostaglandin E1(out) = prostaglandin E1(in);
CC         Xref=Rhea:RHEA:50980, ChEBI:CHEBI:57397;
CC         Evidence={ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50981;
CC         Evidence={ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:14631946,
CC         ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50985;
CC         Evidence={ECO:0000305|PubMed:10873595, ECO:0000305|PubMed:14631946,
CC         ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50985;
CC         Evidence={ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in);
CC         Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404;
CC         Evidence={ECO:0000269|PubMed:14631946};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50989;
CC         Evidence={ECO:0000305|PubMed:14631946};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate(out) = (5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate(in); Xref=Rhea:RHEA:71395, ChEBI:CHEBI:32395;
CC         Evidence={ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71396;
CC         Evidence={ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC         ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:30063921};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71705;
CC         Evidence={ECO:0000305|PubMed:30063921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851,
CC         ChEBI:CHEBI:29746; Evidence={ECO:0000269|PubMed:30063921};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71853;
CC         Evidence={ECO:0000305|PubMed:30063921};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71836;
CC         Evidence={ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71836;
CC         Evidence={ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=argipressin(out) = argipressin(in); Xref=Rhea:RHEA:75979,
CC         ChEBI:CHEBI:194507; Evidence={ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75980;
CC         Evidence={ECO:0000305|PubMed:16971491};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=argipressin(out) = argipressin(in); Xref=Rhea:RHEA:75979,
CC         ChEBI:CHEBI:194507; Evidence={ECO:0000269|PubMed:16971491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75980;
CC         Evidence={ECO:0000305|PubMed:16971491};
CC   -!- ACTIVITY REGULATION: Stimulated by extracellular acidic pH.
CC       {ECO:0000269|PubMed:19129463}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       Kinetic parameters:
CC         KM=101 nM for prostaglandin E1 {ECO:0000269|PubMed:16971491};
CC         KM=48.5 nM for prostaglandin E1 {ECO:0000269|PubMed:14631946};
CC         KM=219 nM for prostaglandin E2 {ECO:0000269|PubMed:16971491};
CC         KM=55.5 nM for prostaglandin E2 {ECO:0000269|PubMed:14631946};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC       Kinetic parameters:
CC         KM=218 nM for prostaglandin E1 {ECO:0000269|PubMed:16971491};
CC         KM=371 nM for prostaglandin E2 {ECO:0000269|PubMed:16971491};
CC   -!- INTERACTION:
CC       Q9UIG8-2; Q13520: AQP6; NbExp=3; IntAct=EBI-13041931, EBI-13059134;
CC       Q9UIG8-2; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-13041931, EBI-12003442;
CC       Q9UIG8-2; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-13041931, EBI-712073;
CC       Q9UIG8-2; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-13041931, EBI-11988865;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Basolateral cell membrane
CC       {ECO:0000269|PubMed:16971491}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized to the basolateral membrane of choroid
CC       plexus epithelium. {ECO:0000269|PubMed:16971491}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Apical cell membrane
CC       {ECO:0000269|PubMed:16971491}; Multi-pass membrane protein
CC       {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Localized to the basal
CC       membrane of Sertoli cells (PubMed:35307651). Localized to the apical
CC       membrane of choroid plexus epithelium (PubMed:16971491).
CC       {ECO:0000269|PubMed:16971491, ECO:0000269|PubMed:35307651}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=OATP3A1-v1;
CC         IsoId=Q9UIG8-1; Sequence=Displayed;
CC       Name=2; Synonyms=OATP3A1-v2;
CC         IsoId=Q9UIG8-2; Sequence=VSP_036837, VSP_036838;
CC       Name=3;
CC         IsoId=Q9UIG8-3; Sequence=VSP_036834, VSP_036835, VSP_036836;
CC       Name=4;
CC         IsoId=Q9UIG8-4; Sequence=VSP_036833;
CC   -!- TISSUE SPECIFICITY: Generally the expression of isoform 1 is higher
CC       than that of isoform 2. {ECO:0000269|PubMed:16971491}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in placental trophoblasts
CC       (PubMed:10873595, PubMed:12409283). Expressed in pancreas, kidney,
CC       liver, lung, brain, heart, cerebellum, peripheral blood leukocyte,
CC       colon, small intestine, ovary, testis, prostate, thyroid, thymus and
CC       spleen (PubMed:10873595, PubMed:16971491, PubMed:14631946). Expressed
CC       in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and
CC       pancreas (PubMed:10873595). In testis, detected in spermatogonia at
CC       different stages and absent from Sertoli cells. Expressed in the
CC       choroid plexus epithelium, at the basolateral membrane. In brain, also
CC       very abundant in the gray matter of the frontal cortex, but not
CC       associated with neuronal cell bodies. Not detected in the white matter
CC       (PubMed:16971491). {ECO:0000269|PubMed:10873595,
CC       ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:14631946,
CC       ECO:0000269|PubMed:16971491}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in heart, brain, cerebellum,
CC       testis, lung, thyroid, spoleen and liver (PubMed:16971491). In testis,
CC       primarily localized to the basal membrane of Sertoli cells and weakly
CC       expressed within the tubules (PubMed:35307651, PubMed:16971491). In
CC       testis, also present in spermatogonia at different stages. In brain,
CC       expressed in the choroid plexus epithelium, at the apical membrane as
CC       well as in the subapical intracellular vesicular compartments. In
CC       brain, also associated with neuronal bodies and axons in both the gray
CC       and the white matters of the frontal cortex (PubMed:16971491).
CC       {ECO:0000269|PubMed:16971491, ECO:0000269|PubMed:35307651}.
CC   -!- INDUCTION: Transcriptionally up-regulated by SP1 and RELA in response
CC       to FGF19. {ECO:0000269|PubMed:30063921}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; AB031050; BAA89287.1; -; mRNA.
DR   EMBL; AF205074; AAG42206.1; -; mRNA.
DR   EMBL; AF187816; AAG43446.1; -; mRNA.
DR   EMBL; AK290872; BAF83561.1; -; mRNA.
DR   EMBL; AK057031; BAG51847.1; -; mRNA.
DR   EMBL; AK097797; BAG53529.1; -; mRNA.
DR   EMBL; FJ515841; ACS13734.1; -; Genomic_DNA.
DR   EMBL; AC104020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000585; AAH00585.1; -; mRNA.
DR   CCDS; CCDS10371.1; -. [Q9UIG8-1]
DR   CCDS; CCDS45354.1; -. [Q9UIG8-2]
DR   RefSeq; NP_001138516.1; NM_001145044.1. [Q9UIG8-2]
DR   RefSeq; NP_037404.2; NM_013272.3. [Q9UIG8-1]
DR   AlphaFoldDB; Q9UIG8; -.
DR   SMR; Q9UIG8; -.
DR   BioGRID; 118181; 14.
DR   IntAct; Q9UIG8; 5.
DR   STRING; 9606.ENSP00000320634; -.
DR   ChEMBL; CHEMBL2073685; -.
DR   DrugBank; DB00770; Alprostadil.
DR   DrugBank; DB00345; Aminohippuric acid.
DR   DrugBank; DB01053; Benzylpenicillin.
DR   DrugBank; DB00286; Conjugated estrogens.
DR   DrugBank; DB01160; Dinoprost tromethamine.
DR   DrugBank; DB00917; Dinoprostone.
DR   DrugBank; DB01088; Iloprost.
DR   DrugBank; DB09198; Lobeglitazone.
DR   DrugBank; DB00563; Methotrexate.
DR   DrugBank; DB06654; Safinamide.
DR   DrugBank; DB04348; Taurocholic acid.
DR   DrugBank; DB09100; Thyroid, porcine.
DR   TCDB; 2.A.60.1.18; the organo anion transporter (oat) family.
DR   GlyCosmos; Q9UIG8; 7 sites, No reported glycans.
DR   GlyGen; Q9UIG8; 7 sites.
DR   iPTMnet; Q9UIG8; -.
DR   PhosphoSitePlus; Q9UIG8; -.
DR   SwissPalm; Q9UIG8; -.
DR   BioMuta; SLCO3A1; -.
DR   DMDM; 296452954; -.
DR   jPOST; Q9UIG8; -.
DR   MassIVE; Q9UIG8; -.
DR   MaxQB; Q9UIG8; -.
DR   PaxDb; 9606-ENSP00000320634; -.
DR   PeptideAtlas; Q9UIG8; -.
DR   ProteomicsDB; 84519; -. [Q9UIG8-1]
DR   ProteomicsDB; 84520; -. [Q9UIG8-2]
DR   ProteomicsDB; 84521; -. [Q9UIG8-3]
DR   ProteomicsDB; 84522; -. [Q9UIG8-4]
DR   Pumba; Q9UIG8; -.
DR   Antibodypedia; 29012; 93 antibodies from 16 providers.
DR   DNASU; 28232; -.
DR   Ensembl; ENST00000318445.11; ENSP00000320634.6; ENSG00000176463.14. [Q9UIG8-1]
DR   Ensembl; ENST00000424469.2; ENSP00000387846.2; ENSG00000176463.14. [Q9UIG8-2]
DR   GeneID; 28232; -.
DR   KEGG; hsa:28232; -.
DR   MANE-Select; ENST00000318445.11; ENSP00000320634.6; NM_013272.4; NP_037404.2.
DR   UCSC; uc002bqx.3; human. [Q9UIG8-1]
DR   AGR; HGNC:10952; -.
DR   CTD; 28232; -.
DR   DisGeNET; 28232; -.
DR   GeneCards; SLCO3A1; -.
DR   HGNC; HGNC:10952; SLCO3A1.
DR   HPA; ENSG00000176463; Tissue enhanced (brain).
DR   MIM; 612435; gene.
DR   neXtProt; NX_Q9UIG8; -.
DR   OpenTargets; ENSG00000176463; -.
DR   PharmGKB; PA35837; -.
DR   VEuPathDB; HostDB:ENSG00000176463; -.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01080000257410; -.
DR   HOGENOM; CLU_008954_3_0_1; -.
DR   InParanoid; Q9UIG8; -.
DR   OMA; NINCECQ; -.
DR   OrthoDB; 2874223at2759; -.
DR   PhylomeDB; Q9UIG8; -.
DR   TreeFam; TF317540; -.
DR   PathwayCommons; Q9UIG8; -.
DR   Reactome; R-HSA-879518; Transport of organic anions. [Q9UIG8-1]
DR   SignaLink; Q9UIG8; -.
DR   BioGRID-ORCS; 28232; 7 hits in 1143 CRISPR screens.
DR   ChiTaRS; SLCO3A1; human.
DR   GeneWiki; SLCO3A1; -.
DR   GenomeRNAi; 28232; -.
DR   Pharos; Q9UIG8; Tbio.
DR   PRO; PR:Q9UIG8; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9UIG8; Protein.
DR   Bgee; ENSG00000176463; Expressed in buccal mucosa cell and 190 other cell types or tissues.
DR   ExpressionAtlas; Q9UIG8; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR   GO; GO:0015732; P:prostaglandin transport; IDA:ARUK-UCL.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   CDD; cd17402; MFS_SLCO3_OATP3; 1.
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; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF86; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 3A1; 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   Genevisible; Q9UIG8; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..710
FT                   /note="Solute carrier organic anion transporter family
FT                   member 3A1"
FT                   /id="PRO_0000191064"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..60
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..106
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..203
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..261
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..286
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..344
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..366
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..386
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..410
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..438
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..539
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        540..562
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..571
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        572..597
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..630
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..648
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        649..705
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          465..513
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:25732826"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        471..501
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        477..497
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        486..511
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   VAR_SEQ         1..281
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036833"
FT   VAR_SEQ         1..58
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036834"
FT   VAR_SEQ         59..60
FT                   /note="YL -> MN (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036835"
FT   VAR_SEQ         641..710
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036836"
FT   VAR_SEQ         667..692
FT                   /note="EFFASTLTLDNLGRDPVPANQTHRTK -> TEYQDIETEKTCPESHSPSEDS
FT                   FVRS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036837"
FT   VAR_SEQ         693..710
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036838"
FT   VARIANT         294
FT                   /note="E -> D (in dbSNP:rs1517618)"
FT                   /evidence="ECO:0000269|PubMed:10873595,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT                   /id="VAR_054853"
FT   CONFLICT        40
FT                   /note="K -> R (in Ref. 4; BAF83561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="R -> L (in Ref. 7; AAH00585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="G -> D (in Ref. 4; BAF83561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="I -> Y (in Ref. 1; BAA89287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   710 AA;  76553 MW;  ED56724BA0998553 CRC64;
     MQGKKPGGSS GGGRSGELQG DEAQRNKKKK KKVSCFSNIK IFLVSECALM LAQGTVGAYL
     VSVLTTLERR FNLQSADVGV IASSFEIGNL ALILFVSYFG ARGHRPRLIG CGGIVMALGA
     LLSALPEFLT HQYKYEAGEI RWGAEGRDVC AANGSGGDEG PDPDLICRNR TATNMMYLLL
     IGAQVLLGIG ATPVQPLGVS YIDDHVRRKD SSLYIGILFT MLVFGPACGF ILGSFCTKIY
     VDAVFIDTSN LDITPDDPRW IGAWWGGFLL CGALLFFSSL LMFGFPQSLP PHSEPAMESE
     QAMLSEREYE RPKPSNGVLR HPLEPDSSAS CFQQLRVIPK VTKHLLSNPV FTCIILAACM
     EIAVVAGFAA FLGKYLEQQF NLTTSSANQL LGMTAIPCAC LGIFLGGLLV KKLSLSALGA
     IRMAMLVNLV STACYVSFLF LGCDTGPVAG VTVPYGNSTA PGSALDPYSP CNNNCECQTD
     SFTPVCGADG ITYLSACFAG CNSTNLTGCA CLTTVPAENA TVVPGKCPSP GCQEAFLTFL
     CVMCICSLIG AMAQTPSVII LIRTVSPELK SYALGVLFLL LRLLGFIPPP LIFGAGIDST
     CLFWSTFCGE QGACVLYDNV VYRYLYVSIA IALKSFAFIL YTTTWQCLRK NYKRYIKNHE
     GGLSTSEFFA STLTLDNLGR DPVPANQTHR TKFIYNLEDH EWCENMESVL
//