ID   SO4A1_HUMAN             Reviewed;         722 AA.
AC   Q96BD0; Q9H4T7; Q9H4T8; Q9H8P2; Q9NWX8; Q9UI35; Q9UIG7;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Solute carrier organic anion transporter family member 4A1;
DE            Short=OATP4A1 {ECO:0000303|PubMed:30343886};
DE   AltName: Full=Colon organic anion transporter;
DE   AltName: Full=Organic anion transporter polypeptide-related protein 1;
DE            Short=OATP-RP1;
DE            Short=OATPRP1;
DE            Short=POAT;
DE   AltName: Full=Organic anion-transporting polypeptide E;
DE            Short=OATP-E {ECO:0000303|PubMed:10873595};
DE   AltName: Full=Sodium-independent organic anion transporter E;
DE   AltName: Full=Solute carrier family 21 member 12;
GN   Name=SLCO4A1; Synonyms=OATP1, OATP4A1, OATPE, SLC21A12;
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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), FUNCTION, TRANSPORTER ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Hippocampus;
RX   PubMed=11316767; DOI=10.1210/endo.142.5.8115;
RA   Fujiwara K., Adachi H., Nishio T., Unno M., Tokui T., Okabe M., Onogawa T.,
RA   Suzuki T., Asano N., Tanemoto M., Seki M., Shiiba K., Suzuki M., Kondo Y.,
RA   Nunoki K., Shimosegawa T., Iinuma K., Ito S., Matsuno S., Abe T.;
RT   "Identification of thyroid hormone transporters in humans: different
RT   molecules are involved in a tissue-specific manner.";
RL   Endocrinology 142:2005-2012(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA   Itoh S., Coca-Prados M., Lu R., Chan B.S., Schuster V.L.;
RT   "Molecular cloning of a putative organic anion transporter, POAT.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
RP   ILE-78.
RC   TISSUE=Ovarian carcinoma;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; THR-37; SER-40; SER-43;
RP   SER-46 AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-43; SER-46 AND
RP   SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-40 AND SER-43, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=30343886; DOI=10.1016/j.bbrc.2018.10.074;
RA   Lofthouse E.M., Cleal J.K., O'Kelly I.M., Sengers B.G., Lewis R.M.;
RT   "Estrone sulphate uptake by the microvillous membrane of placental
RT   syncytiotrophoblast is coupled to glutamate efflux.";
RL   Biochem. Biophys. Res. Commun. 506:237-242(2018).
RN   [15]
RP   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: Organic anion antiporter with apparent broad substrate
CC       specificity. Recognizes various substrates including thyroid hormones
CC       3,3',5-triiodo-L-thyronine (T3), L-thyroxine (T4) and 3,3',5'-triiodo-
CC       L-thyronine (rT3), conjugated steroids such as estrone 3-sulfate and
CC       estradiol 17-beta glucuronide, bile acids such as taurocholate and
CC       prostanoids such as prostaglandin E2, likely operating in a tissue-
CC       specific manner (PubMed:10873595, PubMed:19129463, PubMed:30343886).
CC       May be involved in uptake of metabolites from the circulation into
CC       organs such as kidney, liver or placenta. Possibly drives the selective
CC       transport of thyroid hormones and estrogens coupled to an outward
CC       glutamate gradient across the microvillous membrane of the placenta
CC       (PubMed:30343886). The transport mechanism, its electrogenicity and
CC       potential tissue-specific counterions remain to be elucidated
CC       (Probable). {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:19129463,
CC       ECO:0000269|PubMed:30343886, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,3',5-triiodo-L-thyronine(out) + L-glutamate(in) = 3,3',5-
CC         triiodo-L-thyronine(in) + L-glutamate(out); Xref=Rhea:RHEA:72299,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:533015;
CC         Evidence={ECO:0000269|PubMed:30343886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72300;
CC         Evidence={ECO:0000305|PubMed:30343886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate(in) + L-thyroxine(out) = L-glutamate(out) + L-
CC         thyroxine(in); Xref=Rhea:RHEA:72303, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:30343886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72304;
CC         Evidence={ECO:0000305|PubMed:30343886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) + L-glutamate(in) = estrone 3-
CC         sulfate(in) + L-glutamate(out); Xref=Rhea:RHEA:72239,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:30343886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72240;
CC         Evidence={ECO:0000305|PubMed:30343886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate(in) + taurocholate(out) = L-glutamate(out) +
CC         taurocholate(in); Xref=Rhea:RHEA:72307, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:30343886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72308;
CC         Evidence={ECO:0000305|PubMed:30343886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-
CC         thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015;
CC         Evidence={ECO:0000269|PubMed:11316767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812;
CC         Evidence={ECO:0000305|PubMed:11316767};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:11316767,
CC         ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820;
CC         Evidence={ECO:0000305|PubMed:11316767, ECO:0000305|PubMed:19129463};
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:0000269|PubMed:11316767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71816;
CC         Evidence={ECO:0000305|PubMed:11316767};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71836;
CC         Evidence={ECO:0000305|PubMed:10873595, ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(out) = 17beta-
CC         estradiol 17-O-(beta-D-glucuronate)(in); Xref=Rhea:RHEA:72691,
CC         ChEBI:CHEBI:82961; Evidence={ECO:0000269|PubMed:19129463};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72692;
CC         Evidence={ECO:0000305|PubMed:19129463};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC         ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:11316767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71704;
CC         Evidence={ECO:0000305|PubMed:11316767};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:10873595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50985;
CC         Evidence={ECO:0000305|PubMed:11316767};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5 with estrone 3-sulfate and L-thyroxine (T4) as
CC         substrates. {ECO:0000269|PubMed:19129463};
CC   -!- INTERACTION:
CC       Q96BD0; O00155: GPR25; NbExp=3; IntAct=EBI-2822217, EBI-10178951;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30343886};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q96BD0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96BD0-2; Sequence=VSP_006152, VSP_006156;
CC       Name=3;
CC         IsoId=Q96BD0-3; Sequence=VSP_006153, VSP_006155;
CC       Name=4;
CC         IsoId=Q96BD0-4; Sequence=VSP_006154;
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10873595,
CC       PubMed:11316767). Expressed in placental trophoblasts (PubMed:10873595,
CC       PubMed:12409283). Expressed in pancreas, kidney, skeletal muscle,
CC       liver, lung, brain, heart, colon, small intestine, ovary, testis,
CC       prostate, thymus and spleen. In testis, primarily localized to Leydig
CC       cells (PubMed:35307651). {ECO:0000269|PubMed:10873595,
CC       ECO:0000269|PubMed:11316767, ECO:0000269|PubMed:12409283,
CC       ECO:0000269|PubMed:35307651}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, heart, kidney, liver,
CC       lung, skeletal muscle, spleen and pancreas (PubMed:10873595).
CC       {ECO:0000269|PubMed:10873595}.
CC   -!- DOMAIN: A conserved histidine residue in the third TMD (His-191) may
CC       play an essential role in the pH sensitivity of SLCO4A1/OATP4A1-
CC       mediated substrate transport. {ECO:0000269|PubMed:19129463}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91247.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB031051; BAA89288.1; -; mRNA.
DR   EMBL; AF187817; AAG43447.1; -; mRNA.
DR   EMBL; AF104334; AAF15545.1; -; mRNA.
DR   EMBL; AF205072; AAG42204.1; -; mRNA.
DR   EMBL; AK023410; BAB14566.1; -; mRNA.
DR   EMBL; AK000551; BAA91247.1; ALT_INIT; mRNA.
DR   EMBL; AL357033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015727; AAH15727.1; -; mRNA.
DR   CCDS; CCDS13501.1; -. [Q96BD0-1]
DR   RefSeq; NP_057438.3; NM_016354.3. [Q96BD0-1]
DR   AlphaFoldDB; Q96BD0; -.
DR   SMR; Q96BD0; -.
DR   BioGRID; 118180; 54.
DR   IntAct; Q96BD0; 7.
DR   MINT; Q96BD0; -.
DR   STRING; 9606.ENSP00000217159; -.
DR   ChEMBL; CHEMBL2073679; -.
DR   DrugBank; DB01053; Benzylpenicillin.
DR   DrugBank; DB00286; Conjugated estrogens.
DR   DrugBank; DB00509; Dextrothyroxine.
DR   DrugBank; DB00917; Dinoprostone.
DR   DrugBank; DB13952; Estradiol acetate.
DR   DrugBank; DB13953; Estradiol benzoate.
DR   DrugBank; DB13954; Estradiol cypionate.
DR   DrugBank; DB13955; Estradiol dienanthate.
DR   DrugBank; DB13956; Estradiol valerate.
DR   DrugBank; DB00451; Levothyroxine.
DR   DrugBank; DB00279; Liothyronine.
DR   DrugBank; DB01583; Liotrix.
DR   DrugBank; DB04348; Taurocholic acid.
DR   DrugBank; DB09100; Thyroid, porcine.
DR   MEROPS; I01.972; -.
DR   TCDB; 2.A.60.1.9; the organo anion transporter (oat) family.
DR   GlyCosmos; Q96BD0; 2 sites, No reported glycans.
DR   GlyGen; Q96BD0; 2 sites.
DR   iPTMnet; Q96BD0; -.
DR   PhosphoSitePlus; Q96BD0; -.
DR   SwissPalm; Q96BD0; -.
DR   BioMuta; SLCO4A1; -.
DR   DMDM; 27734555; -.
DR   EPD; Q96BD0; -.
DR   jPOST; Q96BD0; -.
DR   MassIVE; Q96BD0; -.
DR   MaxQB; Q96BD0; -.
DR   PaxDb; 9606-ENSP00000217159; -.
DR   PeptideAtlas; Q96BD0; -.
DR   ProteomicsDB; 76061; -. [Q96BD0-1]
DR   ProteomicsDB; 76062; -. [Q96BD0-2]
DR   ProteomicsDB; 76063; -. [Q96BD0-3]
DR   ProteomicsDB; 76064; -. [Q96BD0-4]
DR   Pumba; Q96BD0; -.
DR   Antibodypedia; 29551; 38 antibodies from 15 providers.
DR   DNASU; 28231; -.
DR   Ensembl; ENST00000217159.6; ENSP00000217159.1; ENSG00000101187.16. [Q96BD0-1]
DR   Ensembl; ENST00000370507.5; ENSP00000359538.1; ENSG00000101187.16. [Q96BD0-1]
DR   GeneID; 28231; -.
DR   KEGG; hsa:28231; -.
DR   MANE-Select; ENST00000217159.6; ENSP00000217159.1; NM_016354.4; NP_057438.3.
DR   UCSC; uc002ydb.1; human. [Q96BD0-1]
DR   AGR; HGNC:10953; -.
DR   CTD; 28231; -.
DR   DisGeNET; 28231; -.
DR   GeneCards; SLCO4A1; -.
DR   HGNC; HGNC:10953; SLCO4A1.
DR   HPA; ENSG00000101187; Tissue enhanced (lung).
DR   MIM; 612436; gene.
DR   neXtProt; NX_Q96BD0; -.
DR   OpenTargets; ENSG00000101187; -.
DR   PharmGKB; PA35838; -.
DR   VEuPathDB; HostDB:ENSG00000101187; -.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01080000257410; -.
DR   HOGENOM; CLU_008954_2_0_1; -.
DR   InParanoid; Q96BD0; -.
DR   OMA; WQESCDK; -.
DR   OrthoDB; 2874223at2759; -.
DR   PhylomeDB; Q96BD0; -.
DR   TreeFam; TF317540; -.
DR   PathwayCommons; Q96BD0; -.
DR   Reactome; R-HSA-879518; Transport of organic anions.
DR   SignaLink; Q96BD0; -.
DR   BioGRID-ORCS; 28231; 15 hits in 1157 CRISPR screens.
DR   ChiTaRS; SLCO4A1; human.
DR   GeneWiki; SLCO4A1; -.
DR   GenomeRNAi; 28231; -.
DR   Pharos; Q96BD0; Tbio.
DR   PRO; PR:Q96BD0; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q96BD0; Protein.
DR   Bgee; ENSG00000101187; Expressed in metanephros cortex and 169 other cell types or tissues.
DR   ExpressionAtlas; Q96BD0; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0015349; F:thyroid hormone transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   CDD; cd17462; MFS_SLCO4A_OATP4A; 1.
DR   Gene3D; 3.30.60.30; -; 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; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   InterPro; IPR046329; SO4A1-like.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF100; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 4A1; 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.
DR   Genevisible; Q96BD0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..722
FT                   /note="Solute carrier organic anion transporter family
FT                   member 4A1"
FT                   /id="PRO_0000191067"
FT   TOPO_DOM        1..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..143
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..195
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..222
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..253
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..332
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..400
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..420
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..444
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..448
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..471
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        472..580
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..603
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        604..612
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        613..638
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        639..671
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        672..689
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        690..722
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          498..555
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        504..534
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        510..530
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        519..553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   VAR_SEQ         250..410
FT                   /note="TYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELTT
FT                   ESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEA
FT                   SNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFL -> LFFAI
FT                   ACFLYKPLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_006152"
FT   VAR_SEQ         548..661
FT                   /note="YRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPAL
FT                   TATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVY
FT                   QNS -> SGAAAYRPCPPLDPGKGPPCLPLVIGAIVGLPRCTETVAVSLRIFPLVLAMH
FT                   CREMHFNLSEKAPPSGFHIRCNFLYIPQQHSCTNGNSTVSWGRVCACPELSLQHPEAEL
FT                   CRS (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006153"
FT   VAR_SEQ         572..603
FT                   /note="STCQRKPLLLVFIFVVIFFTFLSSIPALTATL -> TTALCAARTASCTSHC
FT                   ATQGALQPRRRMWTAR (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_006154"
FT   VAR_SEQ         662..722
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006155"
FT   VAR_SEQ         686..722
FT                   /note="CFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQSSV -> SSRAASDHRPR
FT                   PPGHGGHSAFPDDRTVPLGDAITRELLFDLQPST (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_006156"
FT   VARIANT         70
FT                   /note="R -> Q (in dbSNP:rs34419428)"
FT                   /id="VAR_053678"
FT   VARIANT         78
FT                   /note="V -> I (in dbSNP:rs1047099)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_053679"
FT   CONFLICT        246
FT                   /note="T -> M (in Ref. 5; BAB14566)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   722 AA;  77193 MW;  DD8F0C10E4BCD255 CRC64;
     MPLHQLGDKP LTFPSPNSAM ENGLDHTPPS RRASPGTPLS PGSLRSAAHS PLDTSKQPLC
     QLWAEKHGAR GTHEVRYVSA GQSVACGWWA FAPPCLQVLN TPKGILFFLC AAAFLQGMTV
     NGFINTVITS LERRYDLHSY QSGLIASSYD IAACLCLTFV SYFGGSGHKP RWLGWGVLLM
     GTGSLVFALP HFTAGRYEVE LDAGVRTCPA NPGAVCADST SGLSRYQLVF MLGQFLHGVG
     ATPLYTLGVT YLDENVKSSC SPVYIAIFYT AAILGPAAGY LIGGALLNIY TEMGRRTELT
     TESPLWVGAW WVGFLGSGAA AFFTAVPILG YPRQLPGSQR YAVMRAAEMH QLKDSSRGEA
     SNPDFGKTIR DLPLSIWLLL KNPTFILLCL AGATEATLIT GMSTFSPKFL ESQFSLSASE
     AATLFGYLVV PAGGGGTFLG GFFVNKLRLR GSAVIKFCLF CTVVSLLGIL VFSLHCPSVP
     MAGVTASYGG SLLPEGHLNL TAPCNAACSC QPEHYSPVCG SDGLMYFSLC HAGCPAATET
     NVDGQKVYRD CSCIPQNLSS GFGHATAGKC TSTCQRKPLL LVFIFVVIFF TFLSSIPALT
     ATLRCVRDPQ RSFALGIQWI VVRILGGIPG PIAFGWVIDK ACLLWQDQCG QQGSCLVYQN
     SAMSRYILIM GLLYKVLGVL FFAIACFLYK PLSESSDGLE TCLPSQSSAP DSATDSQLQS
     SV
//