ID SO2B1_HUMAN Reviewed; 709 AA. AC O94956; A0A024R5I4; A8K2G9; B4DGA9; B4DTB0; E7ERN5; E9PPU8; Q9H2Z0; Q9UFU1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 27-MAR-2024, entry version 187. DE RecName: Full=Solute carrier organic anion transporter family member 2B1; DE AltName: Full=Organic anion transporter B {ECO:0000303|PubMed:16754786}; DE Short=OATP-B {ECO:0000303|PubMed:10873595, ECO:0000303|PubMed:16754786}; DE AltName: Full=Organic anion transporter polypeptide-related protein 2; DE Short=OATP-RP2; DE Short=OATPRP2; DE AltName: Full=Organic anion transporting polypeptide 2B1 {ECO:0000303|PubMed:16908597}; DE Short=OATP2B1 {ECO:0000303|PubMed:16908597}; DE AltName: Full=Solute carrier family 21 member 9 {ECO:0000303|PubMed:11159893}; GN Name=SLCO2B1 {ECO:0000312|HGNC:HGNC:10962}; GN Synonyms=KIAA0880, OATP2B1 {ECO:0000303|PubMed:16908597}, OATPB, GN SLC21A9 {ECO:0000303|PubMed:11159893}; 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, AND RP TISSUE SPECIFICITY. RC TISSUE=Brain; 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 3). 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT RP PHE-486. RC TISSUE=Amygdala, and Thalamus; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [9] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11159893; DOI=10.1053/gast.2001.21176; RA Kullak-Ublick G.A., Ismair M.G., Stieger B., Landmann L., Huber R., RA Pizzagalli F., Fattinger K., Meier P.J., Hagenbuch B.; RT "Organic anion-transporting polypeptide B (OATP-B) and its functional RT comparison with three other OATPs of human liver."; RL Gastroenterology 120:525-533(2001). RN [10] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11932330; DOI=10.1210/jcem.87.4.8431; RA St-Pierre M.V., Hagenbuch B., Ugele B., Meier P.J., Stallmach T.; RT "Characterization of an organic anion-transporting polypeptide (OATP-B) in RT human placenta."; RL J. Clin. Endocrinol. Metab. 87:1856-1863(2002). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND 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 [12] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=12724351; DOI=10.1124/jpet.103.051300; RA Kobayashi D., Nozawa T., Imai K., Nezu J., Tsuji A., Tamai I.; RT "Involvement of human organic anion transporting polypeptide OATP-B RT (SLC21A9) in pH-dependent transport across intestinal apical membrane."; RL J. Pharmacol. Exp. Ther. 306:703-708(2003). RN [13] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=14610227; DOI=10.1124/jpet.103.060194; RA Nozawa T., Imai K., Nezu J., Tsuji A., Tamai I.; RT "Functional characterization of pH-sensitive organic anion transporting RT polypeptide OATP-B in human."; RL J. Pharmacol. Exp. Ther. 308:438-445(2004). RN [14] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=16908597; DOI=10.1124/mol.106.026450; RA Grube M., Koeck K., Karner S., Reuther S., Ritter C.A., Jedlitschky G., RA Kroemer H.K.; RT "Modification of OATP2B1-mediated transport by steroid hormones."; RL Mol. Pharmacol. 70:1735-1741(2006). RN [15] RP PRESENCE OF DISULFIDE BONDS. RX PubMed=16754786; DOI=10.1124/mol.105.019547; RA Hanggi E., Grundschober A.F., Leuthold S., Meier P.J., St-Pierre M.V.; RT "Functional analysis of the extracellular cysteine residues in the human RT organic anion transporting polypeptide, OATP2B1."; RL Mol. Pharmacol. 70:806-817(2006). RN [16] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18501590; DOI=10.1016/j.jsbmb.2008.04.001; RA Ugele B., Bahn A., Rex-Haffner M.; RT "Functional differences in steroid sulfate uptake of organic anion RT transporter 4 (OAT4) and organic anion transporting polypeptide 2B1 RT (OATP2B1) in human placenta."; RL J. Steroid Biochem. Mol. Biol. 111:1-6(2008). RN [17] 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 [18] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=20507927; DOI=10.1124/jpet.110.166314; RA Kis O., Zastre J.A., Ramaswamy M., Bendayan R.; RT "pH dependence of organic anion-transporting polypeptide 2B1 in Caco-2 RT cells: potential role in antiretroviral drug oral bioavailability and drug- RT drug interactions."; RL J. Pharmacol. Exp. Ther. 334:1009-1022(2010). RN [19] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22201122; DOI=10.2133/dmpk.dmpk-11-sh-080; RA Shirasaka Y., Mori T., Shichiri M., Nakanishi T., Tamai I.; RT "Functional pleiotropy of organic anion transporting polypeptide OATP2B1 RT due to multiple binding sites."; RL Drug Metab. Pharmacokinet. 27:360-364(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [21] RP FUNCTION, TRANSPORTER ACTIVITY, ALTERNATIVE PROMOTER USAGE, AND TISSUE RP SPECIFICITY. RX PubMed=23531488; DOI=10.1124/mol.112.083618; RA Knauer M.J., Girdwood A.J., Kim R.B., Tirona R.G.; RT "Transport function and transcriptional regulation of a liver-enriched RT human organic anion transporting polypeptide 2B1 transcriptional start site RT variant."; RL Mol. Pharmacol. 83:1218-1228(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318 AND SER-320, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=26277985; DOI=10.1113/jp270743; RA Lofthouse E.M., Brooks S., Cleal J.K., Hanson M.A., Poore K.R., RA O'Kelly I.M., Lewis R.M.; RT "Glutamate cycling may drive organic anion transport on the basal membrane RT of human placental syncytiotrophoblast."; RL J. Physiol. (Lond.) 593:4549-4559(2015). RN [24] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=25132355; DOI=10.1007/s00424-014-1596-x; RA Gao B., Vavricka S.R., Meier P.J., Stieger B.; RT "Differential cellular expression of organic anion transporting peptides RT OATP1A2 and OATP2B1 in the human retina and brain: implications for RT carrier-mediated transport of neuropeptides and neurosteriods in the CNS."; RL Pflugers Arch. 467:1481-1493(2015). RN [25] RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF HIS-46; HIS-55; HIS-113; HIS-136; HIS-185; RP HIS-219; HIS-370; HIS-436; HIS-468; HIS-475; HIS-480; HIS-517; HIS-579; RP ARG-607; HIS-618 AND HIS-628. RX DOI=10.1039/C6MD00235H; RA Hoshino Y., Fujita D., Nakanishi T., Tamai I.; RT "Molecular localization and characterization of multiple binding sites of RT organic anion transporting polypeptide 2B1 (OATP2B1) as the mechanism for RT substrate and modulator dependent drug-drug interaction."; RL Med. Chem. Commun. 7:1775-1782(2016). RN [26] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF TRP-272; TRP-276; TRP-277; TRP-523; ARG-607; TRP-611 AND RP TRP-629. RX PubMed=27576593; DOI=10.1021/acs.molpharmaceut.6b00648; RA Bian J., Jin M., Yue M., Wang M., Zhang H., Gui C.; RT "Tryptophan Residue Located at the Middle of Putative Transmembrane Domain RT 11 Is Critical for the Function of Organic Anion Transporting Polypeptide RT 2B1."; RL Mol. Pharm. 13:3553-3563(2016). RN [27] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=26383540; DOI=10.3109/00498254.2015.1085111; RA Bednarczyk D., Boiselle C.; RT "Organic anion transporting polypeptide (OATP)-mediated transport of RT coproporphyrins I and III."; RL Xenobiotica 46:457-466(2016). RN [28] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=28408210; DOI=10.1016/j.xphs.2017.04.001; RA Keiser M., Kaltheuner L., Wildberg C., Mueller J., Grube M., Partecke L.I., RA Heidecke C.D., Oswald S.; RT "The Organic Anion-Transporting Peptide 2B1 Is Localized in the Basolateral RT Membrane of the Human Jejunum and Caco-2 Monolayers."; RL J. Pharm. Sci. 106:2657-2663(2017). RN [29] RP FUNCTION, TRANSPORTER ACTIVITY, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF LYS-49; LEU-50; PHE-51; VAL-52; LEU-53; CYS-54; HIS-55; RP SER-56; LEU-57; LEU-58; GLN-59; LEU-60; ALA-61; GLN-62; LEU-63; MET-64; RP ILE-65; SER-66; GLY-67; TYR-68 AND LEU-69. RX PubMed=29871943; DOI=10.1124/mol.118.111914; RA Fang Z., Huang J., Chen J., Xu S., Xiang Z., Hong M.; RT "Transmembrane Domain 1 of Human Organic Anion Transporting Polypeptide 2B1 RT Is Essential for Transporter Function and Stability."; RL Mol. Pharmacol. 94:842-849(2018). RN [30] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=34628357; DOI=10.1016/j.dmpk.2021.100418; RA Hussner J., Foletti A., Seibert I., Fuchs A., Schuler E., Malagnino V., RA Grube M., Meyer Zu Schwabedissen H.E.; RT "Differences in transport function of the human and rat orthologue of the RT Organic Anion Transporting Polypeptide 2B1 (OATP2B1)."; RL Drug Metab. Pharmacokinet. 41:100418-100418(2021). RN [31] RP FUNCTION, 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). RN [32] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=35714613; DOI=10.1016/j.molcel.2022.05.024; RA Unlu G., Prizer B., Erdal R., Yeh H.W., Bayraktar E.C., Birsoy K.; RT "Metabolic-scale gene activation screens identify SLCO2B1 as a heme RT transporter that enhances cellular iron availability."; RL Mol. Cell 0:0-0(2022). RN [33] RP VARIANT [LARGE SCALE ANALYSIS] LYS-77. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Mediates the Na(+)-independent transport of steroid sulfate CC conjugates and other specific organic anions (PubMed:10873595, CC PubMed:11159893, PubMed:11932330, PubMed:12724351, PubMed:14610227, CC PubMed:16908597, PubMed:18501590, PubMed:20507927, PubMed:22201122, CC PubMed:23531488, PubMed:25132355, PubMed:27576593, PubMed:26383540, CC PubMed:28408210, PubMed:29871943, PubMed:34628357). Responsible for the CC transport of estrone 3-sulfate (E1S) through the basal membrane of CC syncytiotrophoblast, highlighting a potential role in the placental CC absorption of fetal-derived sulfated steroids including the steroid CC hormone precursor dehydroepiandrosterone sulfate (DHEA-S) CC (PubMed:11932330, PubMed:12409283). Also facilitates the uptake of CC sulfated steroids at the basal/sinusoidal membrane of hepatocytes, CC therefore accounting for the major part of organic anions clearance of CC liver (PubMed:11159893). Mediates the intestinal uptake of sulfated CC steroids (PubMed:12724351, PubMed:28408210). Mediates the uptake of the CC neurosteroids DHEA-S and pregnenolone sulfate (PregS) into the CC endothelial cells of the blood-brain barrier as the first step to enter CC the brain (PubMed:16908597, PubMed:25132355). Also plays a role in the CC reuptake of neuropeptides such as substance P/TAC1 and vasoactive CC intestinal peptide/VIP released from retinal neurons (PubMed:25132355). CC May act as a heme transporter that promotes cellular iron availability CC via heme oxygenase/HMOX2 and independently of TFRC (PubMed:35714613). CC Also transports heme by-product coproporphyrin III (CPIII), and may be CC involved in their hepatic disposition (PubMed:26383540). Mediates the CC uptake of other substrates such as prostaglandins D2 (PGD2), E1 (PGE1) CC and E2 (PGE2), taurocholate, L-thyroxine, leukotriene C4 and CC thromboxane B2 (PubMed:10873595, PubMed:14610227, PubMed:19129463, CC Ref.25, PubMed:29871943). May contribute to regulate the transport of CC organic compounds in testis across the blood-testis-barrier (Probable). CC Shows a pH-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 (PubMed:14610227, CC PubMed:19129463, PubMed:22201122). The exact transport mechanism has CC not been yet deciphered but most likely involves an anion exchange, CC coupling the cellular uptake of organic substrate with the efflux of an CC anionic compound (PubMed:19129463, PubMed:20507927, PubMed:26277985). CC Hydrogencarbonate/HCO3(-) acts as a probable counteranion that CC exchanges for organic anions (PubMed:19129463). Cytoplasmic glutamate CC may also act as counteranion in the placenta (PubMed:26277985). An CC inwardly directed proton gradient has also been proposed as the driving CC force of E1S uptake with a (H(+):E1S) stoichiometry of (1:1) CC (PubMed:20507927). {ECO:0000269|PubMed:10873595, CC ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, CC ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:12724351, CC ECO:0000269|PubMed:14610227, ECO:0000269|PubMed:16908597, CC ECO:0000269|PubMed:18501590, ECO:0000269|PubMed:19129463, CC ECO:0000269|PubMed:20507927, ECO:0000269|PubMed:22201122, CC ECO:0000269|PubMed:23531488, ECO:0000269|PubMed:25132355, CC ECO:0000269|PubMed:26277985, ECO:0000269|PubMed:26383540, CC ECO:0000269|PubMed:27576593, ECO:0000269|PubMed:29871943, CC ECO:0000269|PubMed:34628357, ECO:0000269|PubMed:35714613, CC ECO:0000269|Ref.25, ECO:0000305|PubMed:35307651}. CC -!- FUNCTION: [Isoform 3]: Has estrone 3-sulfate (E1S) transport activity CC comparable with the full-length isoform 1. CC {ECO:0000269|PubMed:23531488}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone CC 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; CC Evidence={ECO:0000305|PubMed:11159893, ECO:0000305|PubMed:14610227, CC ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:18501590, CC ECO:0000305|PubMed:23531488, ECO:0000305|PubMed:26277985, CC ECO:0000305|PubMed:34628357}; 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:28408210, ECO:0000305|PubMed:10873595, CC ECO:0000305|PubMed:11159893, ECO:0000305|PubMed:11932330, CC ECO:0000305|PubMed:12724351, ECO:0000305|PubMed:14610227, CC ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:18501590, CC ECO:0000305|PubMed:19129463, ECO:0000305|PubMed:20507927, CC ECO:0000305|PubMed:22201122, ECO:0000305|PubMed:23531488, CC ECO:0000305|PubMed:26277985, ECO:0000305|PubMed:26383540, CC ECO:0000305|PubMed:27576593, ECO:0000305|PubMed:29871943, CC ECO:0000305|PubMed:34628357, ECO:0000305|Ref.25}; CC -!- CATALYTIC ACTIVITY: CC Reaction=estrone 3-sulfate(out) + hydrogencarbonate(in) = estrone 3- CC sulfate(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:73055, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:60050; CC Evidence={ECO:0000269|PubMed:19129463}; CC -!- CATALYTIC ACTIVITY: CC Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, CC ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:14610227, CC ECO:0000305|PubMed:29871943}; CC -!- CATALYTIC ACTIVITY: CC Reaction=coproporphyrin III(out) = coproporphyrin III(in); CC Xref=Rhea:RHEA:74363, ChEBI:CHEBI:131725; CC Evidence={ECO:0000305|PubMed:26383540}; CC -!- CATALYTIC ACTIVITY: CC Reaction=substance P(out) = substance P(in); Xref=Rhea:RHEA:74367, CC ChEBI:CHEBI:190692; Evidence={ECO:0000305|PubMed:25132355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=pregnenolone sulfate(out) = pregnenolone sulfate(in); CC Xref=Rhea:RHEA:73023, ChEBI:CHEBI:133000; CC Evidence={ECO:0000305|PubMed:16908597, ECO:0000305|PubMed:34628357}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin E2(out) = prostaglandin E2(in); CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; CC Evidence={ECO:0000305|PubMed:10873595, ECO:0000305|Ref.25}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin D2(out) = prostaglandin D2(in); CC Xref=Rhea:RHEA:50976, ChEBI:CHEBI:57406; CC Evidence={ECO:0000250|UniProtKB:Q9JHI3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, CC ChEBI:CHEBI:58448; Evidence={ECO:0000305|PubMed:19129463}; CC -!- ACTIVITY REGULATION: E1S, DHEA-S and PregS transports are regulated by CC steroid hormones. In the case of testosterone, transport of E1S and CC DHEA-S was inhibited, whereas progesterone stimulated E1S, DHEA-S and CC PregS uptake (PubMed:16908597). Progesterone stimulates high-affinity CC uptake of E1S whereas it inhibits low-affinity uptake of E1S (Ref.25). CC Progesterone doesn't affect the uptake of PGE2 (Ref.25). CC {ECO:0000269|PubMed:16908597, ECO:0000269|Ref.25}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=13.1 uM for estrone 3-sulfate (at pH 5.0) CC {ECO:0000269|PubMed:14610227}; CC KM=9.36 uM for estrone-3-sulfate (at pH 6.5) CC {ECO:0000269|PubMed:19129463}; CC KM=35 uM for estrone 3-sulfate (at pH 7.2) CC {ECO:0000269|PubMed:11932330}; CC KM=14 uM for estrone 3-sulfate (at pH 7.3) CC {ECO:0000269|PubMed:16908597}; CC KM=6.4 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:29871943}; CC KM=19.1 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:18501590}; CC KM=8.09 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:14610227}; CC KM=7.1 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:27576593}; CC KM=6.76 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:27576593}; CC KM=16 uM for estrone 3-sulfate (at pH 7.4) CC {ECO:0000269|PubMed:20507927}; CC KM=6.3 uM for estrone 3-sulfate (at pH 7.5) CC {ECO:0000269|PubMed:11159893}; CC KM=17.7 uM for estrone-3-sulfate (at pH 8.0) CC {ECO:0000269|PubMed:19129463}; CC KM=29.9 uM for estrone 3-sulfate for the low-affinity site (at pH CC 6.5) {ECO:0000269|PubMed:22201122}; CC KM=51.4 uM for estrone 3-sulfate for the low-affinity site (at pH CC 6.5) {ECO:0000269|Ref.25}; CC KM=0.1 uM for estrone 3-sulfate for the high-affinity site (at pH CC 6.5) {ECO:0000269|PubMed:22201122}; CC KM=0.463 uM for estrone 3-sulfate for the high-affinity site (at pH CC 6.5) {ECO:0000269|Ref.25}; CC KM=201.8 uM for dehydroepiandrosterone sulfate (at pH 7.4) CC {ECO:0000269|PubMed:18501590}; CC KM=0.31 uM for L-thyroxine (at pH 6.5) {ECO:0000269|PubMed:19129463}; CC KM=0.77 uM for L-thyroxine (at pH 8.0) {ECO:0000269|PubMed:19129463}; CC KM=71.8 uM for taurocholate (at pH 5.0) CC {ECO:0000269|PubMed:14610227}; CC KM=84 uM for substance P/TAC1 (at pH 7.5) CC {ECO:0000269|PubMed:25132355}; CC KM=94 uM for vasoactive intestinal peptide/VIP (at pH 7.5) CC {ECO:0000269|PubMed:25132355}; CC KM=0.31 uM for coproporphyrin III (at pH 7.4) CC {ECO:0000269|PubMed:26383540}; CC Vmax=2135 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 5.0) {ECO:0000269|PubMed:14610227}; CC Vmax=1293 pmol/min/mg enzyme with estrone-3-sulfate as substrate (at CC pH 6.5) {ECO:0000269|PubMed:19129463}; CC Vmax=12300 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.2) {ECO:0000269|PubMed:11932330}; CC Vmax=169 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.3) {ECO:0000269|PubMed:16908597}; CC Vmax=585 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.4) {ECO:0000269|PubMed:18501590}; CC Vmax=351 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.4) {ECO:0000269|PubMed:29871943}; CC Vmax=300 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.4) {ECO:0000269|PubMed:14610227}; CC Vmax=182 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.4) {ECO:0000269|PubMed:27576593}; CC Vmax=209 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 7.4) {ECO:0000269|PubMed:20507927}; CC Vmax=1400 pmol/min/mg enzyme with estrone-3-sulfate as substrate (at CC pH 8.0) {ECO:0000269|PubMed:19129463}; CC Vmax=602 pmol/min/mg enzyme with dehydroepiandrosterone sulfate as CC substrate (at pH 7.4) {ECO:0000269|PubMed:18501590}; CC Vmax=5.76 pmol/min/mg enzyme with L-thyroxine as substrate (at pH CC 6.5) {ECO:0000269|PubMed:19129463}; CC Vmax=7.28 pmol/min/mg enzyme with L-thyroxine as substrate (at pH CC 8.0) {ECO:0000269|PubMed:19129463}; CC Vmax=546 pmol/min/mg enzyme with taurocholate as substrate (at pH CC 5.0) {ECO:0000269|PubMed:14610227}; CC Vmax=19 pmol/min/mg enzyme with coproporphyrin III as substrate (at CC pH 7.4) {ECO:0000269|PubMed:26383540}; CC Note=Estrone 3-sulfate transport exhibits a biphasic saturation CC kinetics, with Km and Vmax values of high- and low-affinity sites due CC to the presence of multiple binding sites. CC {ECO:0000269|PubMed:22201122, ECO:0000269|Ref.25}; CC pH dependence: CC Optimum pH is around 5.0 with estrone 3-sulfate, CC dehydroepiandrosterone sulfate and taurocholate as substrates CC (PubMed:12724351, PubMed:14610227, PubMed:20507927, PubMed:22201122). CC The high-affinity site for estrone 3-sulfate binding is pH-dependent CC with increased transport at lower pH, while the low-affinity site is CC pH-independent (PubMed:22201122). Taurocholate is only transported at CC acidic pH (PubMed:14610227). {ECO:0000269|PubMed:12724351, CC ECO:0000269|PubMed:14610227, ECO:0000269|PubMed:20507927, CC ECO:0000269|PubMed:22201122}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius with estrone 3-sulfate as CC substrate. {ECO:0000269|PubMed:11932330}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25132355}; CC Multi-pass membrane protein {ECO:0000305}. Basal cell membrane CC {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, CC ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:35307651}; Multi-pass CC membrane protein {ECO:0000305}. Basolateral cell membrane CC {ECO:0000269|PubMed:28408210}; Multi-pass membrane protein CC {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12724351, CC ECO:0000269|PubMed:28408210}; Multi-pass membrane protein CC {ECO:0000305}. Note=Expressed at the basal membrane of hepatocytes, CC syncytiotrophoblast and Sertoli cells (PubMed:11159893, CC PubMed:11932330, PubMed:12409283, PubMed:35307651). Localized to the CC basolateral membrane of enterocytes (PubMed:28408210). Also found at CC the apical membrane of enterocytes (PubMed:12724351, PubMed:28408210). CC {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, CC ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:12724351, CC ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=1b, FL; CC IsoId=O94956-1; Sequence=Displayed; CC Name=2; CC IsoId=O94956-2; Sequence=VSP_006147, VSP_006148; CC Name=3; Synonyms=1e, Short; CC IsoId=O94956-3; Sequence=VSP_054109; CC Name=4; CC IsoId=O94956-4; Sequence=VSP_054110; CC -!- TISSUE SPECIFICITY: Strongly expressed in the liver, at the sinusoidal CC membrane of the hepatocytes (PubMed:10873595, PubMed:11159893, CC PubMed:23531488). Expressed in the kidney (PubMed:11159893). Expressed CC in placental trophoblasts and syncytiotrophoblast (PubMed:11159893, CC PubMed:11932330, PubMed:12409283, PubMed:26277985). Expressed in the CC small intestine (PubMed:10873595, PubMed:11159893, PubMed:12724351, CC PubMed:23531488, PubMed:28408210). Expressed in the blood-brain CC barrier, in endothelial cells of brain capillaries (PubMed:11159893, CC PubMed:25132355). Expressed in the retina, in the inner nuclear layer CC and the inner plexiform layer (PubMed:25132355). Expressed in skelettal CC muscles (PubMed:23531488). In testis, primarily localized to the basal CC membrane of Sertoli cells and weakly expressed within the tubules CC (PubMed:10873595, PubMed:11159893, PubMed:35307651). Also expressed in CC pancreas, lung, heart, colon, ovary and spleen (PubMed:10873595, CC PubMed:11159893). Expressed in fetal brain, heart, kidney, liver, lung, CC skeletal muscle, spleen and pancreas (PubMed:10873595). CC {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:11159893, CC ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, CC ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:23531488, CC ECO:0000269|PubMed:25132355, ECO:0000269|PubMed:26277985, CC ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highest expression in brain. CC Predominant isoform compared to isoform 3 in small intestine duodenum, CC kidney, placenta, and skeletal muscle. {ECO:0000269|PubMed:23531488}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Predominant isoform compared to CC isoform 1 in liver. Also expressed in small intestine duodenum, kidney, CC brain, placenta, and skeletal muscle. {ECO:0000269|PubMed:23531488}. CC -!- INDUCTION: [Isoform 3]: Its expression is regulated by HNF4A. CC {ECO:0000305|PubMed:23531488}. CC -!- DOMAIN: A conserved histidine residue in the third transmembrane domain CC (His-136) might play an essential role in the pH sensitivity of CC SLCO2B1/OATP2B1-mediated substrate transport (PubMed:19129463). CC Transmembrane domain 1 (TM1) may be localized within the substrate CC binding pocket (PubMed:29871943). {ECO:0000269|PubMed:19129463, CC ECO:0000269|PubMed:29871943}. CC -!- MISCELLANEOUS: Most likely contributes to the oral absorption and the CC disposition of a wide range of drugs in the intestine and the liver CC (PubMed:10873595, PubMed:11159893, PubMed:12724351, PubMed:14610227, CC PubMed:23531488, PubMed:26277985, Ref.25, PubMed:27576593). CC {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:11159893, CC ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:14610227, CC ECO:0000269|PubMed:23531488, ECO:0000269|PubMed:26277985, CC ECO:0000269|PubMed:27576593, ECO:0000269|Ref.25}. CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family. CC {ECO:0000305}. CC -!- CAUTION: While some reports have shown that E1S transport exhibited CC single-saturation kinetics (PubMed:11932330, PubMed:14610227), other CC studies demonstrated a biphasic saturation kinetics (PubMed:22201122, CC Ref.25, PubMed:11932330, PubMed:14610227). Despite a previous report CC that demonstrated a pH-dependent substrate uptake and a transport CC stimulation at low pH (PubMed:14610227), another study did not observe CC any pH-dependent E1S and taurocholate transport (PubMed:23531488, CC PubMed:14610227). Was shown to mediate bile acid taurocholate transport CC at low pH in some studies (PubMed:14610227, PubMed:29871943), but not CC others (PubMed:23531488, PubMed:11159893, PubMed:29871943). The CC enterocyte localization of SLCO2B1/OATP2B1 remains uncertain. While CC some authors found it in the apical membrane (PubMed:12724351), CC consistent with a function as uptake carrier contributing to the CC intestinal absorption of drugs, other studies demonstrated a CC basolateral membrane expression, supporting a physiological role in CC substrate uptake from the blood flow and intestinal clearance CC (PubMed:28408210, PubMed:12724351). {ECO:0000269|PubMed:11159893, CC ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12724351, CC ECO:0000269|PubMed:14610227, ECO:0000269|PubMed:22201122, CC ECO:0000269|PubMed:23531488, ECO:0000269|PubMed:28408210, CC ECO:0000269|PubMed:29871943, ECO:0000269|Ref.25}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74903.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB026256; BAA78638.1; -; mRNA. DR EMBL; AF205073; AAG42205.1; -; mRNA. DR EMBL; AB020687; BAA74903.2; ALT_INIT; mRNA. DR EMBL; AK290234; BAF82923.1; -; mRNA. DR EMBL; AK294503; BAG57720.1; -; mRNA. DR EMBL; AK300134; BAG61922.1; -; mRNA. DR EMBL; AL117465; CAB55940.1; -; mRNA. DR EMBL; AP001972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455415; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74957.1; -; Genomic_DNA. DR EMBL; CH471076; EAW74956.1; -; Genomic_DNA. DR EMBL; BC041095; AAH41095.1; -; mRNA. DR CCDS; CCDS44683.1; -. [O94956-3] DR CCDS; CCDS53679.1; -. [O94956-4] DR CCDS; CCDS8235.1; -. [O94956-1] DR PIR; T17250; T17250. DR RefSeq; NP_001138683.1; NM_001145211.2. [O94956-3] DR RefSeq; NP_001138684.1; NM_001145212.2. [O94956-4] DR RefSeq; NP_009187.1; NM_007256.4. [O94956-1] DR AlphaFoldDB; O94956; -. DR SMR; O94956; -. DR BioGRID; 116442; 2. DR STRING; 9606.ENSP00000289575; -. DR BindingDB; O94956; -. DR ChEMBL; CHEMBL1743124; -. DR DrugBank; DB03166; Acetic acid. DR DrugBank; DB00770; Alprostadil. DR DrugBank; DB11586; Asunaprevir. DR DrugBank; DB01072; Atazanavir. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB12319; Benzbromarone. DR DrugBank; DB03793; Benzoic acid. DR DrugBank; DB01053; Benzylpenicillin. DR DrugBank; DB11591; Bilastine. DR DrugBank; DB08862; Cholecystokinin. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB09213; Dexibuprofen. DR DrugBank; DB00255; Diethylstilbestrol. DR DrugBank; DB00917; Dinoprostone. DR DrugBank; DB08995; Diosmin. DR DrugBank; DB00975; Dipyridamole. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB00530; Erlotinib. 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; DB00655; Estrone. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB01095; Fluvastatin. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB01645; Genistein. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB01050; Ibuprofen. DR DrugBank; DB01088; Iloprost. DR DrugBank; DB00224; Indinavir. DR DrugBank; DB01167; Itraconazole. DR DrugBank; DB04398; Lactic acid. DR DrugBank; DB11660; Latanoprostene bunod. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB11611; Lifitegrast. DR DrugBank; DB00227; Lovastatin. DR DrugBank; DB16226; Maralixibat. DR DrugBank; DB00244; Mesalazine. DR DrugBank; DB00471; Montelukast. DR DrugBank; DB03467; Naringenin. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB00627; Niacin. DR DrugBank; DB01051; Novobiocin. DR DrugBank; DB11632; Opicapone. DR DrugBank; DB03902; Oxalic Acid. DR DrugBank; DB12978; Pexidartinib. DR DrugBank; DB02746; Phthalic Acid. DR DrugBank; DB00554; Piroxicam. DR DrugBank; DB08860; Pitavastatin. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB05804; Prasterone sulfate. DR DrugBank; DB00175; Pravastatin. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB00206; Reserpine. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB11753; Rifamycin. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB01098; Rosuvastatin. DR DrugBank; DB00936; Salicylic acid. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB09298; Silibinin. DR DrugBank; DB06290; Simeprevir. DR DrugBank; DB00641; Simvastatin. DR DrugBank; DB00795; Sulfasalazine. DR DrugBank; DB04348; Taurocholic acid. DR DrugBank; DB05521; Telaprevir. DR DrugBank; DB11761; Tenapanor. DR DrugBank; DB00759; Tetracycline. DR DrugBank; DB00932; Tipranavir. DR DrugBank; DB01124; Tolbutamide. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB11613; Velpatasvir. DR DrugCentral; O94956; -. DR GuidetoPHARMACOLOGY; 1224; -. DR TCDB; 2.A.60.1.20; the organo anion transporter (oat) family. DR GlyCosmos; O94956; 2 sites, No reported glycans. DR GlyGen; O94956; 2 sites. DR iPTMnet; O94956; -. DR PhosphoSitePlus; O94956; -. DR BioMuta; SLCO2B1; -. DR jPOST; O94956; -. DR MassIVE; O94956; -. DR MaxQB; O94956; -. DR PaxDb; 9606-ENSP00000289575; -. DR PeptideAtlas; O94956; -. DR ProteomicsDB; 17820; -. DR ProteomicsDB; 22826; -. DR ProteomicsDB; 50577; -. [O94956-1] DR ProteomicsDB; 50578; -. [O94956-2] DR Antibodypedia; 17309; 133 antibodies from 18 providers. DR DNASU; 11309; -. DR Ensembl; ENST00000289575.10; ENSP00000289575.5; ENSG00000137491.15. [O94956-1] DR Ensembl; ENST00000428359.6; ENSP00000388912.2; ENSG00000137491.15. [O94956-3] DR Ensembl; ENST00000454962.6; ENSP00000389653.2; ENSG00000137491.15. [O94956-2] DR Ensembl; ENST00000525650.5; ENSP00000436324.1; ENSG00000137491.15. [O94956-4] DR GeneID; 11309; -. DR KEGG; hsa:11309; -. DR MANE-Select; ENST00000289575.10; ENSP00000289575.5; NM_007256.5; NP_009187.1. DR UCSC; uc001owc.4; human. [O94956-1] DR AGR; HGNC:10962; -. DR CTD; 11309; -. DR DisGeNET; 11309; -. DR GeneCards; SLCO2B1; -. DR HGNC; HGNC:10962; SLCO2B1. DR HPA; ENSG00000137491; Tissue enhanced (liver). DR MIM; 604988; gene. DR neXtProt; NX_O94956; -. DR OpenTargets; ENSG00000137491; -. DR PharmGKB; PA35845; -. DR VEuPathDB; HostDB:ENSG00000137491; -. DR eggNOG; KOG3626; Eukaryota. DR GeneTree; ENSGT01080000257336; -. DR HOGENOM; CLU_008954_4_2_1; -. DR InParanoid; O94956; -. DR OMA; FMLGSAM; -. DR OrthoDB; 2874223at2759; -. DR PhylomeDB; O94956; -. DR TreeFam; TF317540; -. DR PathwayCommons; O94956; -. DR Reactome; R-HSA-189483; Heme degradation. [O94956-3] DR Reactome; R-HSA-879518; Transport of organic anions. DR Reactome; R-HSA-9749641; Aspirin ADME. [O94956-1] DR Reactome; R-HSA-9754706; Atorvastatin ADME. [O94956-3] DR BioGRID-ORCS; 11309; 8 hits in 1163 CRISPR screens. DR ChiTaRS; SLCO2B1; human. DR GeneWiki; SLCO2B1; -. DR GenomeRNAi; 11309; -. DR Pharos; O94956; Tchem. DR PRO; PR:O94956; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O94956; Protein. DR Bgee; ENSG00000137491; Expressed in right lobe of liver and 172 other cell types or tissues. DR ExpressionAtlas; O94956; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL. 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; IDA:UniProtKB. DR GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0042167; P:heme catabolic process; TAS:Reactome. DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW. DR GO; GO:0015711; P:organic anion transport; IDA:ARUK-UCL. DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IDA:ARUK-UCL. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR CDD; cd17460; MFS_SLCO2B_OATP2B; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR002350; Kazal_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:SF87; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 2B1; 1. DR Pfam; PF03137; OATP; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS51465; KAZAL_2; 1. DR Genevisible; O94956; HS. PE 1: Evidence at protein level; KW Alternative promoter usage; Alternative splicing; Cell membrane; KW Disulfide bond; Glycoprotein; Ion transport; Membrane; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..709 FT /note="Solute carrier organic anion transporter family FT member 2B1" FT /id="PRO_0000191061" FT TOPO_DOM 1..49 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 50..69 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 70..88 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 89..109 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 110..115 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 116..140 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 141..185 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 186..215 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 216..234 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 256..273 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 274..298 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 299..366 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 367..388 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 389..408 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 409..432 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 433..436 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 437..460 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 461..564 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 565..587 FT /note="Helical; Name=10" FT /evidence="ECO:0000255" FT TOPO_DOM 588..596 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 597..622 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 623..655 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 656..673 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 674..709 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 483..543 FT /note="Kazal-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 51..69 FT /note="Required for E1S and taurocholate transport; FT required for transporter stability" FT /evidence="ECO:0000269|PubMed:29871943" FT REGION 319..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 679..709 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 579 FT /note="Implicated in low-affinity site for E1S transport" FT /evidence="ECO:0000269|Ref.25" FT SITE 607 FT /note="Essential for E1S and PGE2 transport activity and FT may interact with these substrates" FT /evidence="ECO:0000269|PubMed:27576593, ECO:0000269|Ref.25" FT SITE 611 FT /note="Essential for E1S transport activity and may FT interact with this substrate" FT /evidence="ECO:0000269|PubMed:27576593" FT SITE 618 FT /note="Implicated in high-affinity site for E1S transport" FT /evidence="ECO:0000269|Ref.25" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BXB6" FT MOD_RES 318 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CARBOHYD 176 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 538 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 489..520 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 495..516 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 504..541 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT VAR_SEQ 1..116 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_006147" FT VAR_SEQ 1..22 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_054109" FT VAR_SEQ 6..149 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054110" FT VAR_SEQ 150..260 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_006148" FT VARIANT 77 FT /note="E -> K (in a breast cancer sample; somatic mutation; FT dbSNP:rs865987804)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036412" FT VARIANT 201 FT /note="V -> M (in dbSNP:rs35199625)" FT /id="VAR_053675" FT VARIANT 312 FT /note="R -> Q (in dbSNP:rs12422149)" FT /id="VAR_053676" FT VARIANT 392 FT /note="T -> I (in dbSNP:rs1621378)" FT /id="VAR_053677" FT VARIANT 486 FT /note="S -> F (in dbSNP:rs2306168)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_020294" FT MUTAGEN 46 FT /note="H->Q: No change in low- and high-affinity transport FT of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 49 FT /note="K->A: Decreased E1S transport, no change in cell FT surface expression." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 50 FT /note="L->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 51 FT /note="F->A: Decreased E1S transport; decreased cell FT surface expression; no change in Km and Vmax values. FT Decreased taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 51 FT /note="F->Y: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 52 FT /note="V->A: Decreased E1S transport, decreased cell FT surface expression; no change in Km value and decreased FT Vmax value. Decreased taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 52 FT /note="V->I: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 53 FT /note="L->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 54 FT /note="C->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 55 FT /note="H->A: Decreased E1S transport, decreased cell FT surface expression; no change in Km value and decreased FT Vmax value for E1S transport activity. Decreased FT taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 55 FT /note="H->K: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 55 FT /note="H->Q: Decreased low- and high-affinity transport of FT E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 56 FT /note="S->A: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 57 FT /note="L->A: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 58 FT /note="L->A: Decreased E1S transport, no change in cell FT surface expression; increased Km value and decreased Vmax FT value for E1S transport activity. Decreased taurocholate FT transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 58 FT /note="L->I: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 59 FT /note="Q->A: Decreased E1S transport, no change in cell FT surface expression; no change in Km value and decreased FT Vmax value for E1S transport activity. Decreased FT taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 59 FT /note="Q->N: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 60 FT /note="L->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 61 FT /note="A->V: Decreased E1S transport, no change in cell FT surface expression, increased Km value and decreased Vmax FT value for E1S transport activity. Decreased taurocholate FT transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 62 FT /note="Q->A: Decreased E1S transport, no change in cell FT surface expression; no change in Km value and decreased FT Vmax value for E1S transport activity. Decreased FT taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 62 FT /note="Q->N: Decreased E1S transport; no change in cell FT surface expression." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 63 FT /note="L->A: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 64 FT /note="M->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 65 FT /note="I->A: Decreased E1S transport, no change in cell FT surface expression." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 66 FT /note="S->A: Decreased E1S transport, no change in cell FT surface expression, increased Km value and decreased Vmax FT value for E1S transport activity. Decreased taurocholate FT transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 66 FT /note="S->T: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 67 FT /note="G->A: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 68 FT /note="Y->A: No change in E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 69 FT /note="L->A: Decreased E1S transport, no change in cell FT surface expression; no change in Km value and decreased FT Vmax value for E1S transport activity. Decreased FT taurocholate transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 69 FT /note="L->I: Decreased E1S transport." FT /evidence="ECO:0000269|PubMed:29871943" FT MUTAGEN 113 FT /note="H->Q: Decreased low-affinity transport of E1S; no FT change in high-affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 136 FT /note="H->Q: Decreased low-affinity transport of E1S; no FT change in high-affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 185 FT /note="H->Q: Increased low- and high-affinity transport of FT E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 219 FT /note="H->Q: Decreased low- and high-affinity transport of FT E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 272 FT /note="W->A: Decreased E1S transport; decreased cell FT surface expression. Strong decrease in cell surface FT expression; when associated with A-276 and A-277." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 272 FT /note="W->F: No change in E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 276 FT /note="W->A: Decreased E1S transport; decreased cell FT surface expression. Strong decrease in cell surface FT expression; when associated with A-272 and A-277." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 276 FT /note="W->F: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 277 FT /note="W->A: Decreased E1S transport; decreased cell FT surface expression. Strong decrease in cell surface FT expression; when associated with A-272 and A-276." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 277 FT /note="W->F: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 370 FT /note="H->Q: No change in low- and high-affinity transport FT of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 436 FT /note="H->Q: Decreased low-affinity transport of E1S; no FT change in high affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 468 FT /note="H->Q: Decreased high-affinity transport of E1S; no FT change in low-affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 475 FT /note="H->Q: Increased high-affinity transport of E1S; FT decreased low-affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 480 FT /note="H->Q: No change in low- and high-affinity transport FT of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 517 FT /note="H->Q: Decreased low-affinity transport of E1S; no FT change in high-affinity transport of E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 523 FT /note="W->A: No change in E1S transport; no change in cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 579 FT /note="H->Q: Strong decrease in low-affinity and decreased FT in high-affinity transport of E1S; undetectable kinetic FT parameter for low-affinity and no change in Vmax/Km value FT for high-affinity transort. Increased PGE2 transport. FT Decreased in low- and high-affinity transport of E1S and FT lower Vmax/Km values; when associated with Q-618." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 607 FT /note="R->A: Loss of E1S transport; small decrease in cell FT surface expression. Strong decrease in low-affinity FT transport of E1S and loss of high-affinity transport of FT E1S. Decreased PGE2 transport." FT /evidence="ECO:0000269|PubMed:27576593, ECO:0000269|Ref.25" FT MUTAGEN 611 FT /note="W->A: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 611 FT /note="W->F: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 611 FT /note="W->H: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 611 FT /note="W->S: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 611 FT /note="W->Y: Decreased E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT MUTAGEN 618 FT /note="H->Q: Strong decrease in high-affinity transport of FT E1S and lower Vmax/Km value; no change in low-affinity FT transport of E1S and higher Vmax/Km value. No change in FT PGE2 transport. Decreased in low- and high-affinity FT transport of E1S and lower Vmax/Km values; when associated FT with Q-579." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 628 FT /note="H->Q: Decreased low- and high-affinity transport of FT E1S." FT /evidence="ECO:0000269|Ref.25" FT MUTAGEN 629 FT /note="W->A: No change in E1S transport; decreased cell FT surface expression." FT /evidence="ECO:0000269|PubMed:27576593" FT CONFLICT 94 FT /note="N -> D (in Ref. 4; BAF82923)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="D -> V (in Ref. 2; AAG42205)" FT /evidence="ECO:0000305" SQ SEQUENCE 709 AA; 76699 MW; 61087C5E00F86D04 CRC64; MGPRIGPAGE VPQVPDKETK ATMGTENTPG GKASPDPQDV RPSVFHNIKL FVLCHSLLQL AQLMISGYLK SSISTVEKRF GLSSQTSGLL ASFNEVGNTA LIVFVSYFGS RVHRPRMIGY GAILVALAGL LMTLPHFISE PYRYDNTSPE DMPQDFKASL CLPTTSAPAS APSNGNCSSY TETQHLSVVG IMFVAQTLLG VGGVPIQPFG ISYIDDFAHN SNSPLYLGIL FAVTMMGPGL AFGLGSLMLR LYVDINQMPE GGISLTIKDP RWVGAWWLGF LIAAGAVALA AIPYFFFPKE MPKEKRELQF RRKVLAVTDS PARKGKDSPS KQSPGESTKK QDGLVQIAPN LTVIQFIKVF PRVLLQTLRH PIFLLVVLSQ VCLSSMAAGM ATFLPKFLER QFSITASYAN LLIGCLSFPS VIVGIVVGGV LVKRLHLGPV GCGALCLLGM LLCLFFSLPL FFIGCSSHQI AGITHQTSAH PGLELSPSCM EACSCPLDGF NPVCDPSTRV EYITPCHAGC SSWVVQDALD NSQVFYTNCS CVVEGNPVLA GSCDSTCSHL VVPFLLLVSL GSALACLTHT PSFMLILRGV KKEDKTLAVG IQFMFLRILA WMPSPVIHGS AIDTTCVHWA LSCGRRAVCR YYNNDLLRNR FIGLQFFFKT GSVICFALVL AVLRQQDKEA RTKESRSSPA VEQQLLVSGP GKKPEDSRV //