ID SO1B3_HUMAN Reviewed; 702 AA. AC Q9NPD5; E7EMT8; Q5JAR4; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=Solute carrier organic anion transporter family member 1B3; DE AltName: Full=Liver-specific organic anion transporter 2 {ECO:0000303|PubMed:17412826}; DE Short=LST-2 {ECO:0000303|PubMed:15159445, ECO:0000303|PubMed:17412826}; DE AltName: Full=OATP1B3 {ECO:0000303|PubMed:15159445, ECO:0000303|PubMed:17412826}; DE AltName: Full=Organic anion transporter 8; DE AltName: Full=Organic anion-transporting polypeptide 8 {ECO:0000303|PubMed:15159445, ECO:0000303|PubMed:17412826}; DE Short=OATP-8 {ECO:0000303|PubMed:10779507, ECO:0000303|PubMed:15159445, ECO:0000303|PubMed:17412826}; DE AltName: Full=Solute carrier family 21 member 8; GN Name=SLCO1B3; Synonyms=LST2, OATP1B3, OATP8, SLC21A8; 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 [GENOMIC DNA / MRNA] (ISOFORM SLCO1B3-1), RP GLYCOSYLATION, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RP TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Liver; RX PubMed=10779507; DOI=10.1074/jbc.m001448200; RA Koenig J., Cui Y., Nies A.T., Keppler D.; RT "Localization and genomic organization of a new hepatocellular organic RT anion transporting polypeptide."; RL J. Biol. Chem. 275:23161-23168(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SLCO1B3-1). RC TISSUE=Liver; RX PubMed=11375950; DOI=10.1053/gast.2001.24804; RA Abe T., Unno M., Onogawa T., Tokui T., Kondo T.N., Nakagomi R., Adachi H., RA Fujiwara K., Okabe M., Suzuki T., Nunoki K., Sato E., Kakyo M., Nishio T., RA Sugita J., Asano N., Tanemoto M., Seki M., Date F., Ono K., Kondo Y., RA Shiiba K., Suzuki M., Ohtani H., Shimosegawa T., Iinuma K., Nagura H., RA Ito S., Matsuno S.; RT "LST-2, a human liver-specific organic anion transporter, determines RT methotrexate sensitivity in gastrointestinal cancers."; RL Gastroenterology 120:1689-1699(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SLCO1B3-2). RA Mizutamari H., Abe T.; RT "Molecular identification of LST-3 subtype."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP FUNCTION. 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 [6] 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 [7] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=12568656; DOI=10.1042/bj20030034; RA Briz O., Serrano M.A., MacIas R.I., Gonzalez-Gallego J., Marin J.J.; RT "Role of organic anion-transporting polypeptides, OATP-A, OATP-C and OATP- RT 8, in the human placenta-maternal liver tandem excretory pathway for foetal RT bilirubin."; RL Biochem. J. 371:897-905(2003). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RX PubMed=15159445; DOI=10.1124/jpet.104.068056; RA Hirano M., Maeda K., Shitara Y., Sugiyama Y.; RT "Contribution of OATP2 (OATP1B1) and OATP8 (OATP1B3) to the hepatic uptake RT of pitavastatin in humans."; RL J. Pharmacol. Exp. Ther. 311:139-146(2004). RN [9] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16624871; DOI=10.1124/dmd.105.008938; RA Yamashiro W., Maeda K., Hirouchi M., Adachi Y., Hu Z., Sugiyama Y.; RT "Involvement of transporters in the hepatic uptake and biliary excretion of RT valsartan, a selective antagonist of the angiotensin II AT1-receptor, in RT humans."; RL Drug Metab. Dispos. 34:1247-1254(2006). RN [10] RP FUNCTION. RX PubMed=16627748; DOI=10.1124/jpet.106.103390; RA Liu L., Cui Y., Chung A.Y., Shitara Y., Sugiyama Y., Keppler D., Pang K.S.; RT "Vectorial transport of enalapril by Oatp1a1/Mrp2 and OATP1B1 and RT OATP1B3/MRP2 in rat and human livers."; RL J. Pharmacol. Exp. Ther. 318:395-402(2006). RN [11] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=17412826; DOI=10.1152/ajpgi.00075.2007; RA Mahagita C., Grassl S.M., Piyachaturawat P., Ballatori N.; RT "Human organic anion transporter 1B1 and 1B3 function as bidirectional RT carriers and do not mediate GSH-bile acid cotransport."; RL Am. J. Physiol. 293:G271-G278(2007). RN [12] 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 [13] RP FUNCTION, INVOLVEMENT IN HBLRR, AND TRANSPORTER ACTIVITY. RX PubMed=22232210; DOI=10.1172/jci59526; RA van de Steeg E., Stranecky V., Hartmannova H., Noskova L., Hrebicek M., RA Wagenaar E., van Esch A., de Waart D.R., Oude Elferink R.P., RA Kenworthy K.E., Sticova E., al-Edreesi M., Knisely A.S., Kmoch S., RA Jirsa M., Schinkel A.H.; RT "Complete OATP1B1 and OATP1B3 deficiency causes human Rotor syndrome by RT interrupting conjugated bilirubin reuptake into the liver."; RL J. Clin. Invest. 122:519-528(2012). RN [14] RP FUNCTION. RX PubMed=23243220; DOI=10.1158/1078-0432.ccr-12-2080; RA van de Steeg E., van Esch A., Wagenaar E., Kenworthy K.E., Schinkel A.H.; RT "Influence of human OATP1B1, OATP1B3, and OATP1A2 on the pharmacokinetics RT of methotrexate and paclitaxel in humanized transgenic mice."; RL Clin. Cancer Res. 19:821-832(2013). RN [15] 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 [16] RP FUNCTION, 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 [17] 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 [18] RP VARIANTS [LARGE SCALE ANALYSIS] MET-292 AND LEU-647. 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 uptake of organic anions CC (PubMed:15159445, PubMed:17412826, PubMed:10779507). Shows broad CC substrate specificity, can transport both organic anions such as bile CC acid taurocholate (cholyltaurine) and conjugated steroids (17-beta- CC glucuronosyl estradiol, dehydroepiandrosterone sulfate (DHEAS), and CC estrone 3-sulfate), as well as eicosanoid leukotriene C4, prostaglandin CC E2 and L-thyroxine (T4) (PubMed:15159445, PubMed:17412826, CC PubMed:10779507, PubMed:12568656, PubMed:11159893, PubMed:19129463). CC Hydrogencarbonate/HCO3(-) acts as the probable counteranion that CC exchanges for organic anions (PubMed:19129463). Shows a pH-sensitive CC substrate specificity towards sulfated steroids, taurocholate and T4 CC which may be ascribed to the protonation state of the binding site and CC leads to a stimulation of substrate transport in an acidic CC microenvironment (PubMed:19129463). Involved in the clearance of bile CC acids and organic anions from the liver (PubMed:22232210). Can take up CC bilirubin glucuronides from plasma into the liver, contributing to the CC detoxification-enhancing liver-blood shuttling loop (PubMed:22232210). CC Transports coproporphyrin I and III, by-products of heme synthesis, and CC may be involved in their hepatic disposition (PubMed:26383540). May CC contribute to regulate the transport of organic compounds in testes CC across the blood-testis-barrier (Probable). Can transport HMG-CoA CC reductase inhibitors (also known as statins) such as pitavastatin, a CC clinically important class of hypolipidemic drugs (PubMed:15159445). CC May play an important role in plasma and tissue distribution of the CC structurally diverse chemotherapeutic drugs methotrexate and paclitaxel CC (PubMed:23243220). May also transport antihypertension agents, such as CC the angiotensin-converting enzyme (ACE) inhibitor prodrug enalapril, CC and the highly selective angiotensin II AT1-receptor antagonist CC valsartan, in the liver (PubMed:16627748, PubMed:16624871). CC {ECO:0000269|PubMed:10779507, ECO:0000269|PubMed:11159893, CC ECO:0000269|PubMed:12568656, ECO:0000269|PubMed:15159445, CC ECO:0000269|PubMed:16624871, ECO:0000269|PubMed:16627748, CC ECO:0000269|PubMed:17412826, ECO:0000269|PubMed:19129463, CC ECO:0000269|PubMed:22232210, ECO:0000269|PubMed:23243220, CC ECO:0000269|PubMed:26383540, ECO:0000305|PubMed:35307651}. 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=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:10779507, CC ECO:0000269|PubMed:12568656, ECO:0000269|PubMed:15159445}; CC -!- CATALYTIC ACTIVITY: CC Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, CC ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:17412826, CC ECO:0000305|PubMed:19129463}; 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:17412826}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone CC 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; CC Evidence={ECO:0000269|PubMed:10779507}; CC -!- CATALYTIC ACTIVITY: CC Reaction=leukotriene C4(out) = leukotriene C4(in); CC Xref=Rhea:RHEA:72743, ChEBI:CHEBI:57973; CC Evidence={ECO:0000269|PubMed:10779507}; 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 -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin E2(out) = prostaglandin E2(in); CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; CC Evidence={ECO:0000305|PubMed:19129463}; CC -!- CATALYTIC ACTIVITY: CC Reaction=bilirubin-glucuronoside(out) = bilirubin-glucuronoside(in); CC Xref=Rhea:RHEA:72791, ChEBI:CHEBI:57767; CC Evidence={ECO:0000269|PubMed:22232210}; CC -!- CATALYTIC ACTIVITY: CC Reaction=bilirubin-bisglucuronoside(out) = bilirubin- CC bisglucuronoside(in); Xref=Rhea:RHEA:72795, ChEBI:CHEBI:58471; CC Evidence={ECO:0000269|PubMed:22232210}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.25 uM for pitavastatin {ECO:0000269|PubMed:15159445}; CC KM=5.4 uM for 17beta-estradiol 17-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:10779507}; CC KM=3.3 uM for sulfobromophthalein {ECO:0000269|PubMed:10779507}; CC KM=24.6 uM for 17beta-estradiol 17-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:15159445}; CC KM=18.2 uM for valsartan {ECO:0000269|PubMed:16624871}; CC KM=3.95 uM for coproporphyrin I {ECO:0000269|PubMed:26383540}; CC KM=1.55 uM for coproporphyrin III {ECO:0000269|PubMed:26383540}; CC KM=54.6 uM for estrone 3-sulfate (at pH 6.5) CC {ECO:0000269|PubMed:19129463}; CC KM=73 uM for estrone 3-sulfate (at pH 8.0) CC {ECO:0000269|PubMed:19129463}; CC Vmax=100 pmol/min/mg protein with pitavastatin CC {ECO:0000269|PubMed:15159445}; CC Vmax=56.8 pmol/min/mg protein with 17beta-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15159445}; CC Vmax=135 pmol/min/mg protein with valsartan CC {ECO:0000269|PubMed:16624871}; CC Vmax=17 pmol/min/mg enzyme with coproporphyrin I as substrate CC {ECO:0000269|PubMed:26383540}; CC Vmax=14.9 pmol/min/mg enzyme with coproporphyrin III as substrate CC {ECO:0000269|PubMed:26383540}; CC Vmax=1798 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 6.5) {ECO:0000269|PubMed:19129463}; CC Vmax=1776 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at CC pH 8.0) {ECO:0000269|PubMed:19129463}; CC pH dependence: CC Optimum pH is 6.5 with estrone 3-sulfate, taurocholate and CC L-thyroxine (T4) as substrates. {ECO:0000269|PubMed:19129463}; CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane CC {ECO:0000269|PubMed:10779507}; Multi-pass membrane protein CC {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:35307651}; CC Multi-pass membrane protein {ECO:0000305}. Note=Localized to the CC basolateral membrane of hepatocytes (PubMed:10779507). Localized to the CC basal membrane of Sertoli cells (PubMed:35307651). CC {ECO:0000269|PubMed:10779507, ECO:0000269|PubMed:35307651}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=SLCO1B3-1; CC IsoId=Q9NPD5-1; Sequence=Displayed; CC Name=SLCO1B3-2; CC IsoId=Q9NPD5-2; Sequence=VSP_056615, VSP_056616, VSP_056617; CC Name=SLCO1B3-SLCO1B7-1; CC IsoId=F5H094-1; Sequence=External; CC -!- TISSUE SPECIFICITY: Highly expressed in liver, in particular at the CC basolateral membrane of hepatocytes near the central vein CC (PubMed:10779507, PubMed:15159445). Expressed in the placenta CC (PubMed:12409283). In testis, primarily localized to the basal membrane CC of Sertoli cells and weakly expressed in Leydig cells and within the CC tubules (PubMed:35307651). {ECO:0000269|PubMed:10779507, CC ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:15159445, CC ECO:0000269|PubMed:35307651}. CC -!- DOMAIN: A conserved histidine residue in the third TMD (His-115) may CC play an essential role in the pH sensitivity of SLCO1B3/OATP1B3- CC mediated substrate transport. {ECO:0000305|PubMed:19129463}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10779507}. CC -!- DISEASE: Hyperbilirubinemia, Rotor type (HBLRR) [MIM:237450]: An CC autosomal recessive form of primary conjugated hyperbilirubinemia. CC Affected individuals develop mild jaundice not associated with CC hemolysis shortly after birth or in childhood. They have delayed plasma CC clearance of the unconjugated anionic dye bromsulphthalein and CC prominent urinary excretion of coproporphyrin I. Hepatic pigmentation CC is normal. {ECO:0000269|PubMed:22232210}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family. CC {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; AJ400763; CAB97008.1; -; Genomic_DNA. DR EMBL; AJ400764; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400765; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400766; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400767; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400768; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400769; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400770; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400771; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400772; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400773; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400774; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400775; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ400776; CAB97008.1; JOINED; Genomic_DNA. DR EMBL; AJ251506; CAB96997.1; -; mRNA. DR EMBL; AF187815; AAG43445.1; -; mRNA. DR EMBL; AY257471; AAP81212.1; -; mRNA. DR EMBL; AY442326; AAS01768.1; -; mRNA. DR EMBL; AC011604; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS8684.1; -. [Q9NPD5-1] DR RefSeq; NP_062818.1; NM_019844.3. [Q9NPD5-1] DR PDB; 8PG0; EM; 2.97 A; A=1-702. DR PDBsum; 8PG0; -. DR AlphaFoldDB; Q9NPD5; -. DR EMDB; EMD-17655; -. DR SMR; Q9NPD5; -. DR BioGRID; 118182; 9. DR STRING; 9606.ENSP00000261196; -. DR BindingDB; Q9NPD5; -. DR ChEMBL; CHEMBL1743121; -. DR DrugBank; DB06403; Ambrisentan. DR DrugBank; DB12597; Asciminib. DR DrugBank; DB11586; Asunaprevir. DR DrugBank; DB05016; Ataluren. DR DrugBank; DB01072; Atazanavir. DR DrugBank; DB16098; Atogepant. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB11817; Baricitinib. DR DrugBank; DB00394; Beclomethasone dipropionate. DR DrugBank; DB15719; Belantamab mafodotin. DR DrugBank; DB15463; Belzutifan. DR DrugBank; DB11936; Bempedoic acid. DR DrugBank; DB00188; Bortezomib. DR DrugBank; DB12151; Brincidofovir. DR DrugBank; DB06772; Cabazitaxel. DR DrugBank; DB00520; Caspofungin. DR DrugBank; DB08862; Cholecystokinin. DR DrugBank; DB02659; Cholic Acid. DR DrugBank; DB01211; Clarithromycin. DR DrugBank; DB00257; Clotrimazole. DR DrugBank; DB09065; Cobicistat. DR DrugBank; DB05239; Cobimetinib. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB00091; Cyclosporine. DR DrugBank; DB08912; Dabrafenib. DR DrugBank; DB09102; Daclatasvir. DR DrugBank; DB12941; Darolutamide. DR DrugBank; DB16650; Deucravacitinib. DR DrugBank; DB08995; Diosmin. DR DrugBank; DB00975; Dipyridamole. DR DrugBank; DB01248; Docetaxel. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB08861; DPDPE. DR DrugBank; DB04855; Dronedarone. DR DrugBank; DB15444; Elexacaftor. DR DrugBank; DB09038; Empagliflozin. DR DrugBank; DB13874; Enasidenib. DR DrugBank; DB00199; Erythromycin. DR DrugBank; DB00783; Estradiol. 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; DB01590; Everolimus. DR DrugBank; DB12500; Fedratinib. DR DrugBank; DB12265; Fexinidazole. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB01095; Fluvastatin. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB08884; Gadoxetic acid. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB06749; Ginsenoside Rb1. DR DrugBank; DB06750; Ginsenoside Rg1. DR DrugBank; DB13879; Glecaprevir. DR DrugBank; DB02691; Glycocholic acid. DR DrugBank; DB11575; Grazoprevir. DR DrugBank; DB12471; Ibrexafungerp. DR DrugBank; DB09054; Idelalisib. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB00602; Ivermectin. DR DrugBank; DB09078; Lenvatinib. DR DrugBank; DB12070; Letermovir. DR DrugBank; DB08855; Leukotriene C4. DR DrugBank; DB13153; Levomenol. DR DrugBank; DB13139; Levosalbutamol. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB17083; Linzagolix. DR DrugBank; DB00279; Liothyronine. DR DrugBank; DB01583; Liotrix. DR DrugBank; DB06448; Lonafarnib. DR DrugBank; DB01601; Lopinavir. DR DrugBank; DB00227; Lovastatin. DR DrugBank; DB12674; Lurbinectedin. DR DrugBank; DB00244; Mesalazine. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB00834; Mifepristone. DR DrugBank; DB00688; Mycophenolate mofetil. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB01051; Novobiocin. DR DrugBank; DB00646; Nystatin. DR DrugBank; DB00275; Olmesartan. DR DrugBank; DB16267; Olutasidenib. DR DrugBank; DB11632; Opicapone. DR DrugBank; DB01092; Ouabain. DR DrugBank; DB01229; Paclitaxel. DR DrugBank; DB15575; Padeliporfin. DR DrugBank; DB15413; Pafolacianine. DR DrugBank; DB13154; Parachlorophenol. DR DrugBank; DB09297; Paritaprevir. DR DrugBank; DB12978; Pexidartinib. DR DrugBank; DB13878; Pibrentasvir. DR DrugBank; DB01132; Pioglitazone. DR DrugBank; DB08860; Pitavastatin. DR DrugBank; DB06813; Pralatrexate. DR DrugBank; DB15822; Pralsetinib. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB05804; Prasterone sulfate. DR DrugBank; DB00175; Pravastatin. DR DrugBank; DB00396; Progesterone. DR DrugBank; DB00481; Raloxifene. DR DrugBank; DB14761; Remdesivir. DR DrugBank; DB11855; Revefenacin. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB11753; Rifamycin. DR DrugBank; DB08864; Rilpivirine. DR DrugBank; DB12457; Rimegepant. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB06176; Romidepsin. DR DrugBank; DB01098; Rosuvastatin. DR DrugBank; DB12332; Rucaparib. DR DrugBank; DB09292; Sacubitril. DR DrugBank; DB11362; Selexipag. DR DrugBank; DB11942; Selinexor. DR DrugBank; DB09298; Silibinin. DR DrugBank; DB06290; Simeprevir. DR DrugBank; DB00641; Simvastatin. DR DrugBank; DB09142; Sincalide. DR DrugBank; DB12713; Sotagliflozin. DR DrugBank; DB00795; Sulfasalazine. DR DrugBank; DB04348; Taurocholic acid. DR DrugBank; DB09137; Technetium Tc-99m mebrofenin. DR DrugBank; DB00976; Telithromycin. DR DrugBank; DB09299; Tenofovir alafenamide. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB13946; Testosterone undecanoate. DR DrugBank; DB00932; Tipranavir. DR DrugBank; DB06137; Tirbanibulin. DR DrugBank; DB14962; Trastuzumab deruxtecan. DR DrugBank; DB15328; Ubrogepant. DR DrugBank; DB00177; Valsartan. DR DrugBank; DB11869; Valspodar. DR DrugBank; DB11613; Velpatasvir. DR DrugBank; DB00541; Vincristine. DR DrugBank; DB12026; Voxilaprevir. DR DrugCentral; Q9NPD5; -. DR GuidetoPHARMACOLOGY; 1221; -. DR TCDB; 2.A.60.1.12; the organo anion transporter (oat) family. DR GlyCosmos; Q9NPD5; 8 sites, 1 glycan. DR GlyGen; Q9NPD5; 8 sites, 1 N-linked glycan (2 sites). DR iPTMnet; Q9NPD5; -. DR PhosphoSitePlus; Q9NPD5; -. DR BioMuta; SLCO1B3; -. DR DMDM; 27734563; -. DR MassIVE; Q9NPD5; -. DR PaxDb; 9606-ENSP00000261196; -. DR PeptideAtlas; Q9NPD5; -. DR ProteomicsDB; 62988; -. DR ProteomicsDB; 81974; -. [Q9NPD5-1] DR Antibodypedia; 12268; 241 antibodies from 22 providers. DR DNASU; 28234; -. DR Ensembl; ENST00000261196.6; ENSP00000261196.2; ENSG00000111700.13. [Q9NPD5-1] DR Ensembl; ENST00000381545.8; ENSP00000370956.4; ENSG00000111700.13. [Q9NPD5-1] DR GeneID; 28234; -. DR KEGG; hsa:28234; -. DR MANE-Select; ENST00000381545.8; ENSP00000370956.4; NM_019844.4; NP_062818.1. DR UCSC; uc001rel.5; human. [Q9NPD5-1] DR AGR; HGNC:10961; -. DR CTD; 28234; -. DR DisGeNET; 28234; -. DR GeneCards; SLCO1B3; -. DR GeneReviews; SLCO1B3; -. DR HGNC; HGNC:10961; SLCO1B3. DR HPA; ENSG00000111700; Tissue enriched (liver). DR MalaCards; SLCO1B3; -. DR MIM; 237450; phenotype. DR MIM; 605495; gene. DR neXtProt; NX_Q9NPD5; -. DR OpenTargets; ENSG00000111700; -. DR OpenTargets; ENSG00000257046; -. DR Orphanet; 3111; Rotor syndrome. DR PharmGKB; PA35844; -. DR VEuPathDB; HostDB:ENSG00000111700; -. DR eggNOG; KOG3626; Eukaryota. DR GeneTree; ENSGT01080000257336; -. DR HOGENOM; CLU_008954_4_0_1; -. DR InParanoid; Q9NPD5; -. DR OMA; RGPSYLV; -. DR PhylomeDB; Q9NPD5; -. DR TreeFam; TF317540; -. DR PathwayCommons; Q9NPD5; -. DR Reactome; R-HSA-159418; Recycling of bile acids and salts. DR Reactome; R-HSA-189483; Heme degradation. DR Reactome; R-HSA-5619058; Defective SLCO1B3 causes hyperbilirubinemia, Rotor type (HBLRR). DR Reactome; R-HSA-879518; Transport of organic anions. DR Reactome; R-HSA-9754706; Atorvastatin ADME. DR SIGNOR; Q9NPD5; -. DR BioGRID-ORCS; 28234; 8 hits in 1143 CRISPR screens. DR ChiTaRS; SLCO1B3; human. DR GeneWiki; SLCO1B3; -. DR GenomeRNAi; 28234; -. DR Pharos; Q9NPD5; Tchem. DR PRO; PR:Q9NPD5; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9NPD5; Protein. DR Bgee; ENSG00000111700; Expressed in right lobe of liver and 91 other cell types or tissues. DR ExpressionAtlas; Q9NPD5; baseline and differential. 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:HPA. DR GO; GO:0015125; F:bile acid transmembrane transporter activity; TAS:Reactome. DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome. 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; TAS:ProtInc. DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 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 NCBIfam; TIGR00805; oat; 1. DR PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1. DR PANTHER; PTHR11388:SF89; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 1B3; 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; Q9NPD5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Glycoprotein; Ion transport; Lipid transport; Membrane; Phosphoprotein; KW Protease inhibitor; Reference proteome; Serine protease inhibitor; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..702 FT /note="Solute carrier organic anion transporter family FT member 1B3" FT /id="PRO_0000191053" FT TOPO_DOM 1..28 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 29..48 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 49..67 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 68..88 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 89..94 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 95..119 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 120..168 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 169..197 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 198..216 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 217..237 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 238..255 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 256..280 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 281..331 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 332..353 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 354..373 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 374..397 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 398..401 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 402..425 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 426..537 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 538..560 FT /note="Helical; Name=10" FT /evidence="ECO:0000255" FT TOPO_DOM 561..569 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 570..595 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 596..629 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 630..647 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 648..695 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 453..508 FT /note="Kazal-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT MOD_RES 293 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6L6" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6L6" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6L6" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 145 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 151 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 503 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 516 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 459..489 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 465..485 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 474..506 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT VAR_SEQ 622..664 FT /note="GRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASDNERK -> GIVQP FT ELKALAIGFHSMIMRSLGGILVPIYFGALIDTTCMKWSTNSCGARGACRIYNSTYLGRA FT FFGLKVALIFPVLVLLTVFIFVVRKKSHGKDTKVLENERQ (in isoform FT SLCO1B3-2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_056615" FT VAR_SEQ 676..677 FT /note="NG -> DS (in isoform SLCO1B3-2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_056616" FT VAR_SEQ 685..702 FT /note="GTDSKTCNLDMQDNAAAN -> EEQ (in isoform SLCO1B3-2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_056617" FT VARIANT 112 FT /note="S -> A (in dbSNP:rs4149117)" FT /id="VAR_024645" FT VARIANT 233 FT /note="M -> I (in dbSNP:rs7311358)" FT /id="VAR_053672" FT VARIANT 256 FT /note="G -> A (in dbSNP:rs60140950)" FT /id="VAR_062150" FT VARIANT 292 FT /note="I -> M (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036410" FT VARIANT 560 FT /note="V -> A (in dbSNP:rs12299012)" FT /id="VAR_053673" FT VARIANT 647 FT /note="M -> L (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs556554798)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036411" FT HELIX 27..50 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 52..59 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 63..84 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 93..112 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 171..185 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 188..199 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 208..216 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 218..230 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 258..273 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 325..334 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 336..357 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 359..367 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 371..400 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 404..424 FT /evidence="ECO:0007829|PDB:8PG0" FT TURN 425..427 FT /evidence="ECO:0007829|PDB:8PG0" FT TURN 437..439 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 444..447 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 458..461 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 484..487 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 505..507 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 528..560 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 568..584 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 587..597 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 599..602 FT /evidence="ECO:0007829|PDB:8PG0" FT STRAND 612..616 FT /evidence="ECO:0007829|PDB:8PG0" FT HELIX 618..648 FT /evidence="ECO:0007829|PDB:8PG0" SQ SEQUENCE 702 AA; 77403 MW; 6D2AE371D782C7FB CRC64; MDQHQHLNKT AESASSEKKK TRRCNGFKMF LAALSFSYIA KALGGIIMKI SITQIERRFD ISSSLAGLID GSFEIGNLLV IVFVSYFGSK LHRPKLIGIG CLLMGTGSIL TSLPHFFMGY YRYSKETHIN PSENSTSSLS TCLINQTLSF NGTSPEIVEK DCVKESGSHM WIYVFMGNML RGIGETPIVP LGISYIDDFA KEGHSSLYLG SLNAIGMIGP VIGFALGSLF AKMYVDIGYV DLSTIRITPK DSRWVGAWWL GFLVSGLFSI ISSIPFFFLP KNPNKPQKER KISLSLHVLK TNDDRNQTAN LTNQGKNVTK NVTGFFQSLK SILTNPLYVI FLLLTLLQVS SFIGSFTYVF KYMEQQYGQS ASHANFLLGI ITIPTVATGM FLGGFIIKKF KLSLVGIAKF SFLTSMISFL FQLLYFPLIC ESKSVAGLTL TYDGNNSVAS HVDVPLSYCN SECNCDESQW EPVCGNNGIT YLSPCLAGCK SSSGIKKHTV FYNCSCVEVT GLQNRNYSAH LGECPRDNTC TRKFFIYVAI QVINSLFSAT GGTTFILLTV KIVQPELKAL AMGFQSMVIR TLGGILAPIY FGALIDKTCM KWSTNSCGAQ GACRIYNSVF FGRVYLGLSI ALRFPALVLY IVFIFAMKKK FQGKDTKASD NERKVMDEAN LEFLNNGEHF VPSAGTDSKT CNLDMQDNAA AN //