ID S22A1_HUMAN Reviewed; 554 AA. AC O15245; A6NFF3; A8K1H2; C9JSU6; O15395; Q9NQD4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Solute carrier family 22 member 1 {ECO:0000303|PubMed:11388889}; DE AltName: Full=Organic cation transporter 1 {ECO:0000303|PubMed:9260930}; DE Short=hOCT1 {ECO:0000303|PubMed:9260930}; GN Name=SLC22A1 {ECO:0000312|HGNC:HGNC:10963}; Synonyms=OCT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP TISSUE SPECIFICITY, MISCELLANEOUS, AND VARIANT PHE-160. RC TISSUE=Liver; RX PubMed=9260930; DOI=10.1089/dna.1997.16.871; RA Gorboulev V., Ulzheimer J.C., Akhoundova A., Ulzheimer-Teuber I., RA Karbach U., Quester S., Baumann C., Lang F., Busch A.E., Koepsell H.; RT "Cloning and characterization of two human polyspecific organic cation RT transporters."; RL DNA Cell Biol. 16:871-881(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP MISCELLANEOUS. RX PubMed=9187257; DOI=10.1124/mol.51.6.913; RA Zhang L., Dresser M.J., Gray A.T., Yost S.C., Terashita S., Giacomini K.M.; RT "Cloning and functional expression of a human liver organic cation RT transporter."; RL Mol. Pharmacol. 51:913-921(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, TISSUE SPECIFICITY, MISCELLANEOUS, AND ALTERNATIVE SPLICING RP (ISOFORMS 1; 2; 3 AND 4). RX PubMed=11388889; DOI=10.1017/s0003480099007770; RA Hayer M., Boenisch H., Bruess M.; RT "Molecular cloning, functional characterization and genomic organization of RT four alternatively spliced isoforms of the human organic cation transporter RT 1 (hOCT1/SLC22A1)."; RL Ann. Hum. Genet. 63:473-482(1999). RN [4] RP ERRATUM OF PUBMED:11388889, AND SEQUENCE REVISION. RA Hayer M., Bonisch H., Bruss M.; RL Ann. Hum. Genet. 64:267-267(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PHE-160; RP VAL-408; MET-420 DEL AND ARG-465. RC TISSUE=Caudate nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-160. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MISCELLANEOUS. RX PubMed=9655880; RA Zhang L., Schaner M.E., Giacomini K.M.; RT "Functional characterization of an organic cation transporter (hOCT1) in a RT transiently transfected human cell line (HeLa)."; RL J. Pharmacol. Exp. Ther. 286:354-361(1998). RN [9] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11408531; RA van Montfoort J.E., Mueller M., Groothuis G.M.M., Meijer D.K.F., RA Koepsell H., Meier P.J.; RT "Comparison of 'type I' and 'type II' organic cation transport by organic RT cation transporters and organic anion-transporting polypeptides."; RL J. Pharmacol. Exp. Ther. 298:110-115(2001). RN [10] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11907186; DOI=10.1124/jpet.301.1.293; RA Kimura H., Takeda M., Narikawa S., Enomoto A., Ichida K., Endou H.; RT "Human organic anion transporters and human organic cation transporters RT mediate renal transport of prostaglandins."; RL J. Pharmacol. Exp. Ther. 301:293-298(2002). RN [11] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=15389554; DOI=10.1002/jcp.20081; RA Ciarimboli G., Struwe K., Arndt P., Gorboulev V., Koepsell H., RA Schlatter E., Hirsch J.R.; RT "Regulation of the human organic cation transporter hOCT1."; RL J. Cell. Physiol. 201:420-428(2004). RN [12] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15817714; DOI=10.1165/rcmb.2004-0363oc; RA Lips K.S., Volk C., Schmitt B.M., Pfeil U., Arndt P., Miska D., Ermert L., RA Kummer W., Koepsell H.; RT "Polyspecific cation transporters mediate luminal release of acetylcholine RT from bronchial epithelium."; RL Am. J. Respir. Cell Mol. Biol. 33:79-88(2005). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MISCELLANEOUS. RX PubMed=16263091; DOI=10.1016/j.bcp.2005.09.011; RA Mueller J., Lips K.S., Metzner L., Neubert R.H.H., Koepsell H., RA Brandsch M.; RT "Drug specificity and intestinal membrane localization of human organic RT cation transporters (OCT)."; RL Biochem. Pharmacol. 70:1851-1860(2005). RN [14] RP FUNCTION, AND MISCELLANEOUS. RX PubMed=16272756; DOI=10.2133/dmpk.20.379; RA Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T., Inui K.; RT "Metformin is a superior substrate for renal organic cation transporter RT OCT2 rather than hepatic OCT1."; RL Drug Metab. Pharmacokinet. 20:379-386(2005). RN [15] RP MISCELLANEOUS. RX PubMed=16951202; DOI=10.1158/0008-5472.can-06-0769; RA Zhang S., Lovejoy K.S., Shima J.E., Lagpacan L.L., Shu Y., Lapuk A., RA Chen Y., Komori T., Gray J.W., Chen X., Lippard S.J., Giacomini K.M.; RT "Organic cation transporters are determinants of oxaliplatin RT cytotoxicity."; RL Cancer Res. 66:8847-8857(2006). RN [16] RP INDUCTION. RX PubMed=16436500; DOI=10.1124/jpet.105.099929; RA Saborowski M., Kullak-Ublick G.A., Eloranta J.J.; RT "The human organic cation transporter-1 gene is transactivated by RT hepatocyte nuclear factor-4alpha."; RL J. Pharmacol. Exp. Ther. 317:778-785(2006). RN [17] RP MISCELLANEOUS. RX PubMed=16914559; DOI=10.1124/jpet.106.110346; RA Yonezawa A., Masuda S., Yokoo S., Katsura T., Inui K.; RT "Cisplatin and oxaliplatin, but not carboplatin and nedaplatin, are RT substrates for human organic cation transporters (SLC22A1-3 and multidrug RT and toxin extrusion family)."; RL J. Pharmacol. Exp. Ther. 319:879-886(2006). RN [18] RP FUNCTION, AND MISCELLANEOUS. RX PubMed=16581093; DOI=10.1016/j.neuropharm.2006.01.005; RA Amphoux A., Vialou V., Drescher E., Bruess M., Mannoury La Cour C., RA Rochat C., Millan M.J., Giros B., Boenisch H., Gautron S.; RT "Differential pharmacological in vitro properties of organic cation RT transporters and regional distribution in rat brain."; RL Neuropharmacology 50:941-952(2006). RN [19] RP INDUCTION. RX PubMed=17635184; DOI=10.1111/j.1472-8206.2007.00517.x; RA Dias V., Ribeiro V.; RT "The expression of the solute carriers NTCP and OCT-1 is regulated by RT cholesterol in HepG2 cells."; RL Fundam. Clin. Pharmacol. 21:445-450(2007). RN [20] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RX PubMed=17460754; DOI=10.1371/journal.pone.0000385; RA Taubert D., Grimberg G., Stenzel W., Schoemig E.; RT "Identification of the endogenous key substrates of the human organic RT cation transporter OCT2 and their implication in function of dopaminergic RT neurons."; RL PLoS ONE 2:e385-e385(2007). RN [21] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MISCELLANEOUS. RX PubMed=19536068; DOI=10.1038/clpt.2009.92; RA Tzvetkov M.V., Vormfelde S.V., Balen D., Meineke I., Schmidt T., Sehrt D., RA Sabolic I., Koepsell H., Brockmoeller J.; RT "The effects of genetic polymorphisms in the organic cation transporters RT OCT1, OCT2, and OCT3 on the renal clearance of metformin."; RL Clin. Pharmacol. Ther. 86:299-306(2009). RN [22] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21128598; DOI=10.1021/mp100180a; RA Winter T.N., Elmquist W.F., Fairbanks C.A.; RT "OCT2 and MATE1 provide bidirectional agmatine transport."; RL Mol. Pharm. 8:133-142(2011). RN [23] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND MISCELLANEOUS. RX PubMed=23680637; DOI=10.1124/mol.112.084517; RA Han T.K., Everett R.S., Proctor W.R., Ng C.M., Costales C.L., Brouwer K.L., RA Thakker D.R.; RT "Organic cation transporter 1 (OCT1/mOct1) is localized in the apical RT membrane of Caco-2 cell monolayers and enterocytes."; RL Mol. Pharmacol. 84:182-189(2013). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-541, AND IDENTIFICATION BY RP 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 [25] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RX PubMed=24961373; DOI=10.1073/pnas.1314939111; RA Chen L., Shu Y., Liang X., Chen E.C., Yee S.W., Zur A.A., Li S., Xu L., RA Keshari K.R., Lin M.J., Chien H.C., Zhang Y., Morrissey K.M., Liu J., RA Ostrem J., Younger N.S., Kurhanewicz J., Shokat K.M., Ashrafi K., RA Giacomini K.M.; RT "OCT1 is a high-capacity thiamine transporter that regulates hepatic RT steatosis and is a target of metformin."; RL Proc. Natl. Acad. Sci. U.S.A. 111:9983-9988(2014). RN [26] RP MUTAGENESIS OF TYR-240; PRO-283; TYR-361 AND TYR-376, AND DOMAIN. RX PubMed=26979622; DOI=10.1038/ncomms10880; RA Sprowl J.A., Ong S.S., Gibson A.A., Hu S., Du G., Lin W., Li L., RA Bharill S., Ness R.A., Stecula A., Offer S.M., Diasio R.B., Nies A.T., RA Schwab M., Cavaletti G., Schlatter E., Ciarimboli G., Schellens J.H.M., RA Isacoff E.Y., Sali A., Chen T., Baker S.D., Sparreboom A., Pabla N.; RT "A phosphotyrosine switch regulates organic cation transporters."; RL Nat. Commun. 7:10880-10880(2016). RN [27] RP FUNCTION, AND MISCELLANEOUS. RX PubMed=34040533; DOI=10.3389/fphar.2021.674559; RA Jensen O., Matthaei J., Klemp H.G., Meyer M.J., Brockmoeller J., RA Tzvetkov M.V.; RT "Isobutyrylcarnitine as a Biomarker of OCT1 Activity and Interspecies RT Differences in its Membrane Transport."; RL Front. Pharmacol. 12:674559-674559(2021). RN [28] 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 [29] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, DOMAIN, MISCELLANEOUS, AND MUTAGENESIS OF ILE-24; LEU-28; ALA-31; RP PHE-32 AND CYS-36. RX PubMed=35469921; DOI=10.1016/j.jbc.2022.101974; RA Meyer M.J., Schreier P.C.F., Basaran M., Vlasova S., Seitz T., RA Brockmoeller J., Zdrazil B., Tzvetkov M.V.; RT "Amino acids in transmembrane helix 1 confer major functional differences RT between human and mouse orthologs of the polyspecific membrane transporter RT OCT1."; RL J. Biol. Chem. 298:101974-101974(2022). RN [30] RP VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND MET-420 DEL, CHARACTERIZATION RP OF VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND MET-420 DEL, FUNCTION, RP TRANSPORTER ACTIVITY, AND MISCELLANEOUS. RX PubMed=12439218; DOI=10.1097/00008571-200211000-00002; RA Kerb R., Brinkmann U., Chatskaia N., Gorbunov D., Gorboulev V., RA Mornhinweg E., Keil A., Eichelbaum M., Koepsell H.; RT "Identification of genetic variations of the human organic cation RT transporter hOCT1 and their functional consequences."; RL Pharmacogenetics 12:591-595(2002). RN [31] RP VARIANTS PHE-14; CYS-61; PHE-85; PHE-160; LEU-189; VAL-220; LEU-341; RP HIS-342; SER-401; VAL-408; MET-420 DEL; ILE-440; ILE-461; ARG-465 AND RP MET-488, CHARACTERIZATION OF VARIANTS PHE-14; CYS-61; PHE-85; PHE-160; RP LEU-189; VAL-220; LEU-341; HIS-342; SER-401; VAL-408; MET-420 DEL; ILE-440; RP ILE-461; ARG-465 AND MET-488, MUTAGENESIS OF GLY-465, FUNCTION, SUBCELLULAR RP LOCATION, AND MISCELLANEOUS. RX PubMed=12719534; DOI=10.1073/pnas.0730858100; RA Shu Y., Leabman M.K., Feng B., Mangravite L.M., Huang C.C., Stryke D., RA Kawamoto M., Johns S.J., DeYoung J., Carlson E., Ferrin T.E., RA Herskowitz I., Giacomini K.M.; RT "Evolutionary conservation predicts function of variants of the human RT organic cation transporter, OCT1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5902-5907(2003). RN [32] RP VARIANTS PHE-160; LEU-283; GLY-287 AND LEU-341. RX PubMed=14697261; DOI=10.1016/j.bbrc.2003.11.175; RA Sakata T., Anzai N., Shin H.J., Noshiro R., Hirata T., Yokoyama H., RA Kanai Y., Endou H.; RT "Novel single nucleotide polymorphisms of organic cation transporter 1 RT (SLC22A1) affecting transport functions."; RL Biochem. Biophys. Res. Commun. 313:789-793(2004). RN [33] RP VARIANTS LEU-41; PHE-160; LEU-341 AND VAL-408. RX PubMed=15499200; DOI=10.2133/dmpk.19.308; RA Itoda M., Saito Y., Maekawa K., Hichiya H., Komamura K., Kamakura S., RA Kitakaze M., Tomoike H., Ueno K., Ozawa S., Sawada J.; RT "Seven novel single nucleotide polymorphisms in the human SLC22A1 gene RT encoding organic cation transporter 1 (OCT1)."; RL Drug Metab. Pharmacokinet. 19:308-312(2004). RN [34] RP VARIANTS CYS-61 AND MET-420 DEL, AND CHARACTERIZATION OF VARIANTS CYS-61 RP AND MET-420 DEL. RX PubMed=28942964; DOI=10.1016/j.ajhg.2017.08.008; RA Kim H.I., Raffler J., Lu W., Lee J.J., Abbey D., Saleheen D., RA Rabinowitz J.D., Bennett M.J., Hand N.J., Brown C., Rader D.J.; RT "Fine Mapping and Functional Analysis Reveal a Role of SLC22A1 in RT Acylcarnitine Transport."; RL Am. J. Hum. Genet. 101:489-502(2017). CC -!- FUNCTION: Electrogenic voltage-dependent transporter that mediates the CC transport of a variety of organic cations such as endogenous bioactive CC amines, cationic drugs and xenobiotics (PubMed:9260930, PubMed:9187257, CC PubMed:11388889, PubMed:9655880, PubMed:11408531, PubMed:15389554, CC PubMed:16263091, PubMed:16272756, PubMed:16581093, PubMed:19536068, CC PubMed:21128598, PubMed:23680637, PubMed:24961373, PubMed:34040533, CC PubMed:12439218, PubMed:12719534). Functions as a pH- and Na(+)- CC independent, bidirectional transporter (By similarity). Cation cellular CC uptake or release is driven by the electrochemical potential (i.e. CC membrane potential and concentration gradient) and substrate CC selectivity (By similarity). Hydrophobicity is a major requirement for CC recognition in polyvalent substrates and inhibitors (By similarity). CC Primarily expressed at the basolateral membrane of hepatocytes and CC proximal tubules and involved in the uptake and disposition of cationic CC compounds by hepatic and renal clearance from the blood flow (By CC similarity). Most likely functions as an uptake carrier in enterocytes CC contributing to the intestinal elimination of organic cations from the CC systemic circulation (PubMed:16263091). Transports endogenous CC monoamines such as N-1-methylnicotinamide (NMN), guanidine, histamine, CC neurotransmitters dopamine, serotonin and adrenaline (PubMed:9260930, CC PubMed:24961373, PubMed:35469921, PubMed:12439218). Also transports CC natural polyamines such as spermidine, agmatine and putrescine at low CC affinity, but relatively high turnover (PubMed:21128598). Involved in CC the hepatic uptake of vitamin B1/thiamine, hence regulating hepatic CC lipid and energy metabolism (PubMed:24961373). Mediates the CC bidirectional transport of acetylcholine (ACh) at the apical membrane CC of ciliated cell in airway epithelium, thereby playing a role in CC luminal release of ACh from bronchial epithelium (PubMed:15817714). CC Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol CC with lower efficency (PubMed:17460754). Also capable of transporting CC non-amine endogenous compounds such as prostaglandin E2 (PGE2) and CC prostaglandin F2-alpha (PGF2-alpha) (PubMed:11907186). May contribute CC to the transport of cationic compounds in testes across the blood- CC testis-barrier (Probable). Also involved in the uptake of xenobiotics CC tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N- CC methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), CC azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21- CC deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N- CC methylpyridinium (ASP) (PubMed:9260930, PubMed:11408531, CC PubMed:15389554, PubMed:35469921). {ECO:0000250|UniProtKB:O08966, CC ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:11388889, CC ECO:0000269|PubMed:11408531, ECO:0000269|PubMed:11907186, CC ECO:0000269|PubMed:12439218, ECO:0000269|PubMed:12719534, CC ECO:0000269|PubMed:15389554, ECO:0000269|PubMed:15817714, CC ECO:0000269|PubMed:16263091, ECO:0000269|PubMed:16272756, CC ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17460754, CC ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:21128598, CC ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:24961373, CC ECO:0000269|PubMed:34040533, ECO:0000269|PubMed:35469921, CC ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9260930, CC ECO:0000269|PubMed:9655880, ECO:0000305|PubMed:35307651}. CC -!- FUNCTION: [Isoform 1]: Mediates the uptake of 1-methyl-4- CC phenylpyridinium (MPP(+)). {ECO:0000269|PubMed:11388889}. CC -!- FUNCTION: [Isoform 2]: Not able to uptake 1-methyl-4-phenylpyridinium CC (MPP(+)). {ECO:0000269|PubMed:11388889}. CC -!- FUNCTION: [Isoform 3]: Not able to uptake 1-methyl-4-phenylpyridinium CC (MPP(+)). {ECO:0000269|PubMed:11388889}. CC -!- FUNCTION: [Isoform 4]: Not able to uptake 1-methyl-4-phenylpyridinium CC (MPP(+)). {ECO:0000269|PubMed:11388889}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); CC Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; CC Evidence={ECO:0000269|PubMed:9260930}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:35469921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, CC ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:12439218, CC ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:35469921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); CC Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; CC Evidence={ECO:0000269|PubMed:35469921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, CC ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:35469921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, CC ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:Q63089}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, CC ChEBI:CHEBI:15355; Evidence={ECO:0000269|PubMed:15817714}; CC -!- CATALYTIC ACTIVITY: CC Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, CC ChEBI:CHEBI:18385; Evidence={ECO:0000269|PubMed:24961373, CC ECO:0000269|PubMed:35469921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, CC ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:21128598}; CC -!- CATALYTIC ACTIVITY: CC Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, CC ChEBI:CHEBI:326268; Evidence={ECO:0000269|PubMed:21128598}; CC -!- CATALYTIC ACTIVITY: CC Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, CC ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:Q63089}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L- CC proline diketopiperazine(out); Xref=Rhea:RHEA:74787, CC ChEBI:CHEBI:90039; Evidence={ECO:0000269|PubMed:17460754}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); CC Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; CC Evidence={ECO:0000269|PubMed:17460754}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); CC Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; CC Evidence={ECO:0000269|PubMed:11907186}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin E2(out) = prostaglandin E2(in); CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; CC Evidence={ECO:0000269|PubMed:11907186}; CC -!- ACTIVITY REGULATION: Phosphorylation of the transporter leads to CC changes in its substrate affinity, resulting in a regulation of the CC transport activity (PubMed:15389554). In contrast with rat ortholog, CC ASP uptake is inhibited by protein kinase A (PKA) and C (PKC) CC activation (PubMed:15389554). ASP uptake is also endogenously activated CC by calmodulin, the calmodulin-dependent kinase II and LCK tyrosine CC kinase (PubMed:15389554). Inhibited by cGMP, most likely through a CC cGMP-binding protein that interacts with OCT1 (By similarity). CC {ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:15389554}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=440 uM for salsolinol {ECO:0000269|PubMed:17460754}; CC KM=558 uM for adrenaline {ECO:0000269|PubMed:35469921}; CC KM=655 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; CC KM=663 uM for serotonin {ECO:0000269|PubMed:35469921}; CC KM=674 uM for dopamine {ECO:0000269|PubMed:35469921}; CC KM=647 nM for prostaglandin E2 {ECO:0000269|PubMed:11907186}; CC KM=477 nM for prostaglandin F2-alpha {ECO:0000269|PubMed:11907186}; CC KM=780 uM for thiamine {ECO:0000269|PubMed:24961373}; CC KM=1057 uM for thiamine {ECO:0000269|PubMed:35469921}; CC KM=4675 uM for histamine {ECO:0000269|PubMed:35469921}; CC KM=18730 uM for agmatine {ECO:0000269|PubMed:21128598}; CC KM=19.5 uM for NMQ {ECO:0000269|PubMed:11408531}; CC KM=11.5 uM for NMQD {ECO:0000269|PubMed:11408531}; CC KM=53 uM for TBuMA {ECO:0000269|PubMed:11408531}; CC KM=100.9 uM for APM {ECO:0000269|PubMed:11408531}; CC Vmax=1 nmol/min/mg enzyme for salsolinol uptake CC {ECO:0000269|PubMed:17460754}; CC Vmax=1.123 nmol/min/mg enzyme with adrenaline as substrate CC {ECO:0000269|PubMed:35469921}; CC Vmax=6.9 nmol/min/mg enzyme for cyclo(his-pro) uptake CC {ECO:0000269|PubMed:17460754}; CC Vmax=6.183 nmol/min/mg enzyme with serotonin as substrate CC {ECO:0000269|PubMed:35469921}; CC Vmax=0.718 nmol/min/mg enzyme with dopamine as substrate CC {ECO:0000269|PubMed:35469921}; CC Vmax=2.77 nmol/min/mg enzyme with thiamine as substrate CC {ECO:0000269|PubMed:24961373}; CC Vmax=8.261 nmol/min/mg enzyme with thiamine as substrate CC {ECO:0000269|PubMed:35469921}; CC Vmax=5.124 nmol/min/mg enzyme with histamine as substrate CC {ECO:0000269|PubMed:35469921}; CC pH dependence: CC Optimum pH is 8.5 for the transport of MPP (PubMed:11388889). While CC optimum pH is 6.0 for the transport of the drug quinidine, no CC transport activity is observed at pH 7.5, possibly due to the CC protonation of quininide at pH6.0 (PubMed:11408531). CC {ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:11408531}; CC Temperature dependence: CC Optimum temperature is 22 degrees Celsius for the transport of TEA. CC Doesn't show any transport activity of TEA at 4 degrees Celsius. CC {ECO:0000269|PubMed:9655880}; CC -!- INTERACTION: CC O15245; Q96G23: CERS2; NbExp=3; IntAct=EBI-1172714, EBI-1057080; CC O15245; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-1172714, EBI-741850; CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane CC {ECO:0000269|PubMed:12719534}; Multi-pass membrane protein CC {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, CC ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637}; Multi-pass CC membrane protein {ECO:0000305}. Lateral cell membrane CC {ECO:0000269|PubMed:16263091}; Multi-pass membrane protein CC {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:35307651}; CC Multi-pass membrane protein {ECO:0000305}. Cell membrane CC {ECO:0000269|PubMed:35469921}; Multi-pass membrane protein CC {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of CC hepatocytes (By similarity). Mainly localized to the basolateral CC membrane of renal proximal tubular cells (By similarity). However, also CC identified at the apical side of proximal tubular cells CC (PubMed:19536068). Mainly expressed at the lateral membrane of CC enterocytes (PubMed:16263091). Also observed at the apical side of CC enterocytes (PubMed:23680637). Localized to the luminal/apical membrane CC of ciliated epithelial cells in bronchi (PubMed:15817714). Localized to CC the basal membrane of Sertoli cells (PubMed:35307651). CC {ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:15817714, CC ECO:0000269|PubMed:16263091, ECO:0000269|PubMed:19536068, CC ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:35307651}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=hOCT1G/L554; CC IsoId=O15245-1; Sequence=Displayed; CC Name=2; Synonyms=hOCT1G/L506; CC IsoId=O15245-2; Sequence=VSP_033589, VSP_033590; CC Name=3; Synonyms=hOCT1G483; CC IsoId=O15245-3; Sequence=VSP_033588; CC Name=4; Synonyms=hOCT1G353; CC IsoId=O15245-4; Sequence=VSP_033587; CC -!- TISSUE SPECIFICITY: Widely expressed with high level in liver CC (PubMed:9260930, PubMed:9187257, PubMed:11388889, PubMed:23680637). In CC liver, expressed around the central vein (PubMed:16263091). Expressed CC in kidney (PubMed:9260930, PubMed:9187257). Expressed in small CC intestine enterocytes (PubMed:16263091, PubMed:23680637). Localized to CC peritubular myoid cells, Leydig cells and moderately to the basal CC membrane of Sertoli cells in testes (PubMed:35307651). Expressed in CC tracheal and bronchial ciliated epithelium in the respiratory tract CC (PubMed:15817714). Also expressed in skeletal muscle, stomach, spleen, CC heart, placentacolon, brain, granulycytes and lympohocytes CC (PubMed:9260930, PubMed:9187257). {ECO:0000269|PubMed:11388889, CC ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091, CC ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:35307651, CC ECO:0000269|PubMed:9187257, ECO:0000269|PubMed:9260930}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in liver and in glial cell CC lines. {ECO:0000269|PubMed:11388889}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in liver and in glial cell CC lines. {ECO:0000269|PubMed:11388889}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in glial cell lines. Not CC expressed in liver. {ECO:0000269|PubMed:11388889}. CC -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in glial cell lines. Not CC expressed in liver. {ECO:0000269|PubMed:11388889}. CC -!- INDUCTION: In the liver activated by HNF4A and suppressed by bile acids CC via NR0B2. Increased by cholesterol treatment in hepatocyte cells. CC {ECO:0000269|PubMed:16436500, ECO:0000269|PubMed:17635184}. CC -!- DOMAIN: A large substrate binding region with partially overlapping CC binding domains for structurally different substrates is formed by CC several transmembrane helix domains (TMH) including TMH 2, 4, 10 and CC 11, and it is alternatingly exposed to the extracellular or CC intracellular side during substrate transport (By similarity). Amino CC acids in TMH 1 confer major functional differences between human and CC mouse orthologs (PubMed:35469921). {ECO:0000250|UniProtKB:Q63089, CC ECO:0000269|PubMed:35469921}. CC -!- DOMAIN: Contains one proline-rich sequence (Pro-Glu-Ser-Pro-Arg) that CC is required for transport activity. {ECO:0000305|PubMed:26979622}. CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}. CC -!- MISCELLANEOUS: Involved in the uptake of clinically used drugs CC including diabetes treatment medicine metformin, neurotoxins 1-methyl- CC 4-phenylpyridinium (MPP(+)) and iobenguane and platinum-based drug CC cisplatin (PubMed:9260930, PubMed:9187257, PubMed:11388889, CC PubMed:9655880, PubMed:16263091, PubMed:16272756, PubMed:16951202, CC PubMed:16914559, PubMed:16581093, PubMed:19536068, PubMed:23680637, CC PubMed:24961373, PubMed:35469921, PubMed:12439218, PubMed:12719534). CC Also involved in metformin efflux transport (PubMed:34040533). CC Metformin competitively inhibits OCT1-mediated thiamine uptake, leading CC to a decrease in hepatic steatosis (PubMed:24961373). Plays a role in CC the anticancer activity of cisplatin and may contribute to antitumor CC specificity (PubMed:16951202, PubMed:16914559). CC {ECO:0000269|PubMed:11388889, ECO:0000269|PubMed:12439218, CC ECO:0000269|PubMed:12719534, ECO:0000269|PubMed:16263091, CC ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093, CC ECO:0000269|PubMed:16914559, ECO:0000269|PubMed:16951202, CC ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637, CC ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:34040533, CC ECO:0000269|PubMed:35469921, ECO:0000269|PubMed:9187257, CC ECO:0000269|PubMed:9260930, ECO:0000269|PubMed:9655880}. CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}. CC -!- CAUTION: Cellular localization of OCT1 in the intestine and the kidney CC remains to be finally defined. While most authors have deduced a CC localization at the basolateral side of enterocytes consistent with a CC physiological role in organic anions uptake from the blood flow and CC intestinal excretion (PubMed:16263091), other studies demonstrated an CC apical localization (PubMed:23680637), supporting a function in CC intestinal absorption of organic anions and drugs (PubMed:16263091, CC PubMed:23680637). Similarly, contradictory results localized the CC transporter to the basolateral side (By similarity) or to the apical CC side (PubMed:19536068) of proximal tubules (By similarity) CC (PubMed:19536068). Although initially reported to transport carnitine CC across the hepatocyte membrane (PubMed:28942964), another study was CC unable to verify this finding (PubMed:34040533, PubMed:28942964). CC Affinity and capacity of the transporter for endogenous substrates vary CC among orthologs (PubMed:16581093, PubMed:34040533, PubMed:35469921). CC For endogenous compounds such as dopamine, histamine, serotonin and CC thiamine, mouse ortholog display higher affinity and capacity compared CC with human OCT1 (PubMed:35469921). In contrast with mouse ortholog, not CC able to transport carnitine, noradrenaline and choline CC (PubMed:34040533). {ECO:0000250|UniProtKB:Q63089, CC ECO:0000269|PubMed:16263091, ECO:0000269|PubMed:16581093, CC ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637, CC ECO:0000269|PubMed:28942964, ECO:0000269|PubMed:34040533, CC ECO:0000269|PubMed:35469921}. 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; X98332; CAA66977.1; -; mRNA. DR EMBL; U77086; AAB67703.1; -; mRNA. DR EMBL; AJ243995; CAB95971.1; -; Genomic_DNA. DR EMBL; AJ243996; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ243998; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ243999; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ244000; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ245460; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ276051; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ276052; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AJ276053; CAB95971.1; JOINED; Genomic_DNA. DR EMBL; AK289887; BAF82576.1; -; mRNA. DR EMBL; AL353625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126364; AAI26365.1; -; mRNA. DR CCDS; CCDS5274.1; -. [O15245-1] DR CCDS; CCDS5275.1; -. [O15245-2] DR RefSeq; NP_003048.1; NM_003057.2. [O15245-1] DR RefSeq; NP_694857.1; NM_153187.1. [O15245-2] DR RefSeq; XP_006715615.1; XM_006715552.1. [O15245-3] DR PDB; 8ET6; EM; 3.57 A; A=1-554. DR PDB; 8ET7; EM; 3.77 A; A=1-554. DR PDB; 8ET8; EM; 3.45 A; A=1-554. DR PDB; 8SC1; EM; 2.92 A; A=1-554. DR PDB; 8SC2; EM; 3.36 A; A=19-554. DR PDB; 8SC3; EM; 3.24 A; A=1-554. DR PDB; 8SC4; EM; 3.46 A; A=1-554. DR PDB; 8SC6; EM; 3.13 A; A=1-554. DR PDBsum; 8ET6; -. DR PDBsum; 8ET7; -. DR PDBsum; 8ET8; -. DR PDBsum; 8SC1; -. DR PDBsum; 8SC2; -. DR PDBsum; 8SC3; -. DR PDBsum; 8SC4; -. DR PDBsum; 8SC6; -. DR AlphaFoldDB; O15245; -. DR EMDB; EMD-28586; -. DR EMDB; EMD-28587; -. DR EMDB; EMD-28588; -. DR EMDB; EMD-40334; -. DR EMDB; EMD-40335; -. DR EMDB; EMD-40336; -. DR EMDB; EMD-40337; -. DR EMDB; EMD-40339; -. DR SMR; O15245; -. DR BioGRID; 112467; 93. DR IntAct; O15245; 2. DR STRING; 9606.ENSP00000355930; -. DR BindingDB; O15245; -. DR ChEMBL; CHEMBL5685; -. DR DrugBank; DB14973; Abrocitinib. DR DrugBank; DB03128; Acetylcholine. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB08838; Agmatine. DR DrugBank; DB00915; Amantadine. DR DrugBank; DB06288; Amisulpride. DR DrugBank; DB12597; Asciminib. DR DrugBank; DB16098; Atogepant. DR DrugBank; DB12267; Brigatinib. DR DrugBank; DB04830; Buformin. DR DrugBank; DB00520; Caspofungin. DR DrugBank; DB01114; Chlorpheniramine. DR DrugBank; DB00122; Choline. DR DrugBank; DB14006; Choline salicylate. DR DrugBank; DB00501; Cimetidine. DR DrugBank; DB00758; Clopidogrel. DR DrugBank; DB00318; Codeine. DR DrugBank; DB00434; Cyproheptadine. DR DrugBank; DB11963; Dacomitinib. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB16650; Deucravacitinib. DR DrugBank; DB09555; Dexchlorpheniramine maleate. DR DrugBank; DB00280; Disopyramide. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB00590; Doxazosin. DR DrugBank; DB04855; Dronedarone. DR DrugBank; DB00625; Efavirenz. DR DrugBank; DB00668; Epinephrine. 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; DB00983; Formoterol. DR DrugBank; DB01004; Ganciclovir. DR DrugBank; DB00406; Gentian violet cation. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB01018; Guanfacine. DR DrugBank; DB00536; Guanidine. DR DrugBank; DB05381; Histamine. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB00224; Indinavir. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00448; Lansoprazole. DR DrugBank; DB11732; Lasmiditan. DR DrugBank; DB01137; Levofloxacin. DR DrugBank; DB08882; Linagliptin. DR DrugBank; DB12674; Lurbinectedin. DR DrugBank; DB00331; Metformin. DR DrugBank; DB08893; Mirabegron. DR DrugBank; DB12598; Nafamostat. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB00238; Nevirapine. DR DrugBank; DB00184; Nicotine. DR DrugBank; DB09079; Nintedanib. DR DrugBank; DB00368; Norepinephrine. DR DrugBank; DB11837; Osilodrostat. DR DrugBank; DB11697; Pacritinib. DR DrugBank; DB09073; Palbociclib. DR DrugBank; DB01337; Pancuronium. DR DrugBank; DB00914; Phenformin. DR DrugBank; DB00925; Phenoxybenzamine. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB11642; Pitolisant. DR DrugBank; DB00413; Pramipexole. DR DrugBank; DB00457; Prazosin. DR DrugBank; DB01032; Probenecid. DR DrugBank; DB01035; Procainamide. DR DrugBank; DB00396; Progesterone. DR DrugBank; DB00908; Quinidine. DR DrugBank; DB00468; Quinine. DR DrugBank; DB00863; Ranitidine. DR DrugBank; DB00206; Reserpine. DR DrugBank; DB00728; Rocuronium. DR DrugBank; DB12332; Rucaparib. DR DrugBank; DB00938; Salmeterol. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB03566; Spermidine. DR DrugBank; DB00127; Spermine. DR DrugBank; DB00391; Sulpiride. DR DrugBank; DB15133; Tepotinib. DR DrugBank; DB08837; Tetraethylammonium. DR DrugBank; DB00152; Thiamine. DR DrugBank; DB01623; Thiothixene. DR DrugBank; DB06137; Tirbanibulin. DR DrugBank; DB01199; Tubocurarine. DR DrugBank; DB00661; Verapamil. DR DrugCentral; O15245; -. DR GuidetoPHARMACOLOGY; 1019; -. DR TCDB; 2.A.1.19.29; the major facilitator superfamily (mfs). DR GlyCosmos; O15245; 1 site, No reported glycans. DR GlyGen; O15245; 1 site. DR iPTMnet; O15245; -. DR PhosphoSitePlus; O15245; -. DR BioMuta; SLC22A1; -. DR MassIVE; O15245; -. DR PaxDb; 9606-ENSP00000355930; -. DR PeptideAtlas; O15245; -. DR ProteomicsDB; 48536; -. [O15245-1] DR ProteomicsDB; 48537; -. [O15245-2] DR ProteomicsDB; 48538; -. [O15245-3] DR ProteomicsDB; 48539; -. [O15245-4] DR Antibodypedia; 33480; 338 antibodies from 33 providers. DR DNASU; 6580; -. DR Ensembl; ENST00000324965.8; ENSP00000318103.4; ENSG00000175003.15. [O15245-2] DR Ensembl; ENST00000366963.9; ENSP00000355930.4; ENSG00000175003.15. [O15245-1] DR Ensembl; ENST00000457470.6; ENSP00000409557.2; ENSG00000175003.15. [O15245-3] DR Ensembl; ENST00000460902.2; ENSP00000439274.1; ENSG00000175003.15. [O15245-4] DR GeneID; 6580; -. DR KEGG; hsa:6580; -. DR MANE-Select; ENST00000366963.9; ENSP00000355930.4; NM_003057.3; NP_003048.1. DR UCSC; uc003qtc.4; human. [O15245-1] DR AGR; HGNC:10963; -. DR CTD; 6580; -. DR DisGeNET; 6580; -. DR GeneCards; SLC22A1; -. DR HGNC; HGNC:10963; SLC22A1. DR HPA; ENSG00000175003; Tissue enriched (liver). DR MIM; 602607; gene. DR neXtProt; NX_O15245; -. DR OpenTargets; ENSG00000175003; -. DR PharmGKB; PA329; -. DR VEuPathDB; HostDB:ENSG00000175003; -. DR eggNOG; KOG0255; Eukaryota. DR GeneTree; ENSGT00940000162065; -. DR HOGENOM; CLU_001265_33_5_1; -. DR InParanoid; O15245; -. DR OMA; IMIFIPH; -. DR OrthoDB; 1474205at2759; -. DR PhylomeDB; O15245; -. DR TreeFam; TF315847; -. DR PathwayCommons; O15245; -. DR Reactome; R-HSA-112311; Neurotransmitter clearance. DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-HSA-2161517; Abacavir transmembrane transport. DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters. DR Reactome; R-HSA-549127; Organic cation transport. DR Reactome; R-HSA-9793528; Ciprofloxacin ADME. DR SABIO-RK; O15245; -. DR SignaLink; O15245; -. DR BioGRID-ORCS; 6580; 10 hits in 1148 CRISPR screens. DR GeneWiki; SLC22A1; -. DR GenomeRNAi; 6580; -. DR Pharos; O15245; Tchem. DR PRO; PR:O15245; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O15245; Protein. DR Bgee; ENSG00000175003; Expressed in right lobe of liver and 100 other cell types or tissues. DR ExpressionAtlas; O15245; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005330; F:dopamine:sodium symporter activity; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0008504; F:monoamine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005334; F:norepinephrine:sodium symporter activity; IEA:Ensembl. DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015489; F:putrescine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015214; F:pyrimidine nucleoside transmembrane transporter activity; IMP:ARUK-UCL. DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0008513; F:secondary active organic cation transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015606; F:spermidine transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015870; P:acetylcholine transport; IDA:UniProtKB. DR GO; GO:1902616; P:acyl carnitine transmembrane transport; IEA:Ensembl. DR GO; GO:0015872; P:dopamine transport; IDA:UniProtKB. DR GO; GO:0090494; P:dopamine uptake; IDA:ARUK-UCL. DR GO; GO:0048241; P:epinephrine transport; IDA:UniProtKB. DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IEA:Ensembl. DR GO; GO:0072237; P:metanephric proximal tubule development; IEA:Ensembl. DR GO; GO:0015844; P:monoamine transport; IDA:UniProtKB. DR GO; GO:0006836; P:neurotransmitter transport; IDA:ARUK-UCL. DR GO; GO:0015874; P:norepinephrine transport; IDA:ARUK-UCL. DR GO; GO:0015695; P:organic cation transport; IDA:ARUK-UCL. DR GO; GO:0015732; P:prostaglandin transport; IDA:UniProtKB. DR GO; GO:0072530; P:purine-containing compound transmembrane transport; TAS:Reactome. DR GO; GO:0015847; P:putrescine transport; IDA:UniProtKB. DR GO; GO:0015697; P:quaternary ammonium group transport; IDA:ARUK-UCL. DR GO; GO:0006837; P:serotonin transport; IDA:UniProtKB. DR GO; GO:0051610; P:serotonin uptake; IDA:ARUK-UCL. DR GO; GO:0015848; P:spermidine transport; ISS:UniProtKB. DR GO; GO:0071934; P:thiamine transmembrane transport; IDA:UniProtKB. DR GO; GO:0015888; P:thiamine transport; IDA:UniProtKB. DR GO; GO:1901998; P:toxin 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 GO; GO:0042908; P:xenobiotic transport; IDA:UniProtKB. DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; NAS:ARUK-UCL. DR CDD; cd17379; MFS_SLC22A1_2_3; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport-like. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR004749; Orgcat_transp/SVOP. DR InterPro; IPR005829; Sugar_transporter_CS. DR NCBIfam; TIGR00898; 2A0119; 1. DR PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1. DR PANTHER; PTHR24064:SF291; SOLUTE CARRIER FAMILY 22 MEMBER 1; 1. DR Pfam; PF00083; Sugar_tr; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. DR Genevisible; O15245; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein; KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..554 FT /note="Solute carrier family 22 member 1" FT /id="PRO_0000333875" FT TOPO_DOM 1..21 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 22..42 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 43..149 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 171..176 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 177..197 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 198..206 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 207..229 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 230..235 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 257..262 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 263..283 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 284..347 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 348..368 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 369..376 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 398..402 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 403..423 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 424..431 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 432..452 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 453..464 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 465..485 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 486..492 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 493..513 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 514..554 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOTIF 283..287 FT /note="Proline-rich sequence" FT /evidence="ECO:0000305|PubMed:26979622" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08966" FT MOD_RES 541 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 354..554 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_033587" FT VAR_SEQ 462..532 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_033588" FT VAR_SEQ 462..506 FT /note="RNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVLGLLA -> SGV FT GPACRGSDATSSRDQGGRFARDHEGRREPWEKSKAQRKHDLP (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_033589" FT VAR_SEQ 507..554 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_033590" FT VARIANT 14 FT /note="S -> F (exclusively found in the African American FT population; increased MPP(+) uptake when associated with FT V-408; dbSNP:rs34447885)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043319" FT VARIANT 41 FT /note="F -> L (in dbSNP:rs2297373)" FT /evidence="ECO:0000269|PubMed:15499200" FT /id="VAR_043320" FT VARIANT 61 FT /note="R -> C (affects transporter activity; reduction of FT MPP(+) uptake; reduction of serum FT O-isobutanoyl-(R)-carnitine levels; reduction of MPP(+) FT uptake when associated with V-408; dbSNP:rs12208357)" FT /evidence="ECO:0000269|PubMed:12439218, FT ECO:0000269|PubMed:12719534, ECO:0000269|PubMed:28942964" FT /id="VAR_043321" FT VARIANT 85 FT /note="L -> F (no changes in MPP(+) uptake; when associated FT with V-408; dbSNP:rs35546288)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043322" FT VARIANT 88 FT /note="C -> R (affects transporter activity; reduction of FT MPP(+), serotonin and TEA uptake; dbSNP:rs55918055)" FT /evidence="ECO:0000269|PubMed:12439218" FT /id="VAR_043323" FT VARIANT 160 FT /note="L -> F (no changes in both MPP(+) and TEA uptake; FT abolishes MPP(+) uptake when associated with S-401; largely FT localized to the plasma membrane; dbSNP:rs683369)" FT /evidence="ECO:0000269|PubMed:12439218, FT ECO:0000269|PubMed:12719534, ECO:0000269|PubMed:14697261, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15499200, ECO:0000269|PubMed:9260930" FT /id="VAR_043324" FT VARIANT 189 FT /note="S -> L (no changes in MPP(+) uptake; FT dbSNP:rs34104736)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043325" FT VARIANT 220 FT /note="G -> V (affects transporter activity; reduction of FT MPP(+) uptake when associated with V-408; FT dbSNP:rs36103319)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043326" FT VARIANT 283 FT /note="P -> L (in dbSNP:rs4646277)" FT /evidence="ECO:0000269|PubMed:14697261" FT /id="VAR_043327" FT VARIANT 287 FT /note="R -> G (in dbSNP:rs4646278)" FT /evidence="ECO:0000269|PubMed:14697261" FT /id="VAR_043328" FT VARIANT 341 FT /note="P -> L (affects transporter activity; reduction of FT TEA uptake; reduction o MPP(+) uptake when associated with FT V-408; largely localized to the plasma membrane; FT dbSNP:rs2282143)" FT /evidence="ECO:0000269|PubMed:12719534, FT ECO:0000269|PubMed:14697261, ECO:0000269|PubMed:15499200" FT /id="VAR_043329" FT VARIANT 342 FT /note="R -> H (no changes in MPP(+) uptake when associated FT with V-408; dbSNP:rs34205214)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043330" FT VARIANT 401 FT /note="G -> S (affects transporter activity; reduction of FT MPP(+), serotonin and TEA uptake; no MPP(+) uptake when FT associated with L-160; dbSNP:rs34130495)" FT /evidence="ECO:0000269|PubMed:12439218, FT ECO:0000269|PubMed:12719534" FT /id="VAR_043331" FT VARIANT 408 FT /note="M -> V (does not affect transporter activity; no FT changes in MPP(+) uptake when associated with F-14; no FT changes in MPP(+) uptake when associated with F-85; no FT changes in MPP(+) uptake when associated with L-189; no FT changes in MPP(+) uptake when associated with H-342; no FT changes in MPP(+) uptake when associated with M-420 del; no FT changes in MPP(+) uptake when associated with I-440; no FT changes in MPP(+) uptake when associated with I-461; no FT changes in MPP(+) uptake when associated with M-488; FT reduction of MPP uptake when associated with C-61; no FT MPP(+) uptake when associated with V-220; reduction of FT MPP(+) uptake when associated with L-341; no MPP(+) uptake FT when associated with S-401; no MPP(+) uptake when FT associated with R-465; dbSNP:rs628031)" FT /evidence="ECO:0000269|PubMed:12719534, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15499200" FT /id="VAR_043332" FT VARIANT 420 FT /note="Missing (reduction of serum FT O-isobutanoyl-(R)-carnitine levels; no change in MPP(+) FT uptake; no changes in MPP(+) uptake when associated with FT V-408; dbSNP:rs72552763)" FT /evidence="ECO:0000269|PubMed:12439218, FT ECO:0000269|PubMed:12719534, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:28942964" FT /id="VAR_043333" FT VARIANT 440 FT /note="M -> I (in dbSNP:rs35956182)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043334" FT VARIANT 461 FT /note="V -> I (no changes in MPP(+) uptake when associated FT with V-408; dbSNP:rs34295611)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043335" FT VARIANT 465 FT /note="G -> R (reduction of the localization to the FT basolateral membrane; no MPP(+) uptake when associated with FT V-408; dbSNP:rs34059508)" FT /evidence="ECO:0000269|PubMed:12719534, FT ECO:0000269|PubMed:14702039" FT /id="VAR_043336" FT VARIANT 488 FT /note="R -> M (no changes in MPP(+) uptake when associated FT with V-408; dbSNP:rs35270274)" FT /evidence="ECO:0000269|PubMed:12719534" FT /id="VAR_043337" FT MUTAGEN 24 FT /note="I->L: No change in fenoterol uptake. No change in FT trospium uptake. No change in terbutaline uptake." FT /evidence="ECO:0000269|PubMed:35469921" FT MUTAGEN 28 FT /note="L->I: No change in fenoterol uptake. No change in FT trospium uptake. No change in terbutaline uptake." FT /evidence="ECO:0000269|PubMed:35469921" FT MUTAGEN 31 FT /note="A->S: No change in fenoterol uptake. No change in FT trospium uptake. No change in terbutaline uptake." FT /evidence="ECO:0000269|PubMed:35469921" FT MUTAGEN 32 FT /note="F->L: No change in fenoterol uptake. Decreased FT trospium uptake. Decreased trospium affinity." FT /evidence="ECO:0000269|PubMed:35469921" FT MUTAGEN 36 FT /note="C->Y: Increased fenoterol uptake. Increased FT fenoterol affinity. No change in trospium uptake. No change FT in terbutaline uptake. No change in terbutaline affinity." FT /evidence="ECO:0000269|PubMed:35469921" FT MUTAGEN 240 FT /note="Y->F: Decreased TEA uptake." FT /evidence="ECO:0000269|PubMed:26979622" FT MUTAGEN 283 FT /note="P->A: Decreased TEA uptake." FT /evidence="ECO:0000269|PubMed:26979622" FT MUTAGEN 361 FT /note="Y->F: Decreased TEA uptake." FT /evidence="ECO:0000269|PubMed:26979622" FT MUTAGEN 376 FT /note="Y->F: Decreased TEA uptake." FT /evidence="ECO:0000269|PubMed:26979622" FT MUTAGEN 465 FT /note="G->A: No changes in MPP(+) uptake." FT /evidence="ECO:0000269|PubMed:12719534" SQ SEQUENCE 554 AA; 61154 MW; 55206B897DE32202 CRC64; MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYLWFTDSVL YQGLILHMGA TSGNLYLDFL YSALVEIPGA FIALITIDRV GRIYPMAMSN LLAGAACLVM IFISPDLHWL NIIIMCVGRM GITIAIQMIC LVNAELYPTF VRNLGVMVCS SLCDIGGIIT PFIVFRLREV WQALPLILFA VLGLLAAGVT LLLPETKGVA LPETMKDAEN LGRKAKPKEN TIYLKVQTSE PSGT //