ID MRP5_HUMAN Reviewed; 1437 AA. AC O15440; B9EIQ2; O14517; Q29ZA9; Q29ZB1; Q86UX3; Q86W30; Q9UN85; Q9UNP5; AC Q9UQC3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 204. DE RecName: Full=ATP-binding cassette sub-family C member 5; DE EC=7.6.2.- {ECO:0000269|PubMed:12637526, ECO:0000269|PubMed:12695538, ECO:0000269|PubMed:15899835, ECO:0000269|PubMed:17229149, ECO:0000269|PubMed:25964343, ECO:0000269|PubMed:26515061}; DE EC=7.6.2.2 {ECO:0000269|PubMed:10840050, ECO:0000269|PubMed:12435799, ECO:0000269|PubMed:12695538, ECO:0000269|PubMed:15899835}; DE AltName: Full=Multi-specific organic anion transporter C {ECO:0000303|PubMed:9827529}; DE Short=MOAT-C {ECO:0000303|PubMed:9827529}; DE AltName: Full=Multidrug resistance-associated protein 5; DE AltName: Full=SMRP; DE AltName: Full=pABC11 {ECO:0000303|PubMed:10438534}; GN Name=ABCC5; Synonyms=MRP5; 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), AND TISSUE SPECIFICITY. RX PubMed=9827529; DOI=10.1093/jnci/90.22.1735; RA Belinsky M.G., Bain L.J., Balsara B.B., Testa J.R., Kruh G.D.; RT "Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT RT subfamily of transporter proteins."; RL J. Natl. Cancer Inst. 90:1735-1741(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10438534; DOI=10.1074/jbc.274.33.23541; RA McAleer M.A., Breen M.A., White N.L., Matthews N.; RT "pABC11 (also known as MOAT-C and MRP5), a member of the ABC family of RT proteins, has anion transporter activity but does not confer multidrug RT resistance when overexpressed in human embryonic kidney 293 cells."; RL J. Biol. Chem. 274:23541-23548(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10721709; DOI=10.1016/s0378-1119(99)00529-6; RA Suzuki T., Sasaki H., Kuh H.J., Agui M., Tatsumi Y., Tanabe S., Terada M., RA Saijo N., Nishio K.; RT "Detailed structural analysis on both human MRP5 and mouse mrp5 RT transcripts."; RL Gene 242:167-173(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Brain, and Ovarian carcinoma; RX PubMed=10840050; DOI=10.1073/pnas.120159197; RA Wijnholds J., Mol C.A.A.M., van Deemter L., de Haas M., Scheffer G.L., RA Baas F., Beijnen J.H., Scheper R.J., Hatse S., De Clercq E., Balzarini J., RA Borst P.; RT "Multidrug-resistance protein 5 is a multispecific organic anion RT transporter able to transport nucleotide analogs."; RL Proc. Natl. Acad. Sci. U.S.A. 97:7476-7481(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, AND RP ALTERNATIVE SPLICING. RC TISSUE=Retina; RX PubMed=17521428; DOI=10.1186/1471-2199-8-42; RA Stojic J., Stohr H., Weber B.H.; RT "Three novel ABCC5 splice variants in human retina and their role as RT regulators of ABCC5 gene expression."; RL BMC Mol. Biol. 8:42-42(2007). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RC TISSUE=Skeletal muscle; RA Ito T., Kato R., Ishikawa T.; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 492-1437 (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=9325169; DOI=10.1006/bbrc.1997.7346; RA Suzuki T., Nishio K., Sasaki H., Kurokawa H., Saito-Ohara F., Ikeuch T., RA Tanabe S., Terada M., Saijo N.; RT "cDNA cloning of a short type of multidrug resistance protein homologue, RT SMRP, from a human lung cancer cell line."; RL Biochem. Biophys. Res. Commun. 238:790-794(1997). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1216-1437 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9270026; RA Kool M., de Haas M., Scheffer G.L., Scheper R.J., van Eijk M.J., RA Juijn J.A., Baas F., Borst P.; RT "Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues RT of the multidrug resistance-associated protein gene (MRP1), in human cancer RT cell lines."; RL Cancer Res. 57:3537-3547(1997). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=10893247; DOI=10.1074/jbc.m005463200; RA Jedlitschky G., Burchell B., Keppler D.; RT "The multidrug resistance protein 5 functions as an ATP-dependent export RT pump for cyclic nucleotides."; RL J. Biol. Chem. 275:30069-30074(2000). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12435799; DOI=10.1124/mol.62.6.1321; RA Wielinga P.R., Reid G., Challa E.E., van der Heijden I., van Deemter L., RA de Haas M., Mol C., Kuil A.J., Groeneveld E., Schuetz J.D., Brouwer C., RA De Abreu R.A., Wijnholds J., Beijnen J.H., Borst P.; RT "Thiopurine metabolism and identification of the thiopurine metabolites RT transported by MRP4 and MRP5 overexpressed in human embryonic kidney RT cells."; RL Mol. Pharmacol. 62:1321-1331(2002). RN [14] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=12695538; DOI=10.1124/mol.63.5.1094; RA Reid G., Wielinga P., Zelcer N., De Haas M., Van Deemter L., Wijnholds J., RA Balzarini J., Borst P.; RT "Characterization of the transport of nucleoside analog drugs by the human RT multidrug resistance proteins MRP4 and MRP5."; RL Mol. Pharmacol. 63:1094-1103(2003). RN [15] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12637526; DOI=10.1074/jbc.m212723200; RA Wielinga P.R., van der Heijden I., Reid G., Beijnen J.H., Wijnholds J., RA Borst P.; RT "Characterization of the MRP4- and MRP5-mediated transport of cyclic RT nucleotides from intact cells."; RL J. Biol. Chem. 278:17664-17671(2003). RN [16] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15501592; DOI=10.1016/j.neuroscience.2004.07.051; RA Nies A.T., Jedlitschky G., Koenig J., Herold-Mende C., Steiner H.H., RA Schmitt H.P., Keppler D.; RT "Expression and immunolocalization of the multidrug resistance proteins, RT MRP1-MRP6 (ABCC1-ABCC6), in human brain."; RL Neuroscience 129:349-360(2004). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15899835; DOI=10.1158/0008-5472.can-04-2810; RA Wielinga P., Hooijberg J.H., Gunnarsdottir S., Kathmann I., Reid G., RA Zelcer N., van der Born K., de Haas M., van der Heijden I., Kaspers G., RA Wijnholds J., Jansen G., Peters G., Borst P.; RT "The human multidrug resistance protein MRP5 transports folates and can RT mediate cellular resistance against antifolates."; RL Cancer Res. 65:4425-4430(2005). RN [18] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17229149; DOI=10.1111/j.1742-4658.2006.05591.x; RA de Wolf C.J., Yamaguchi H., van der Heijden I., Wielinga P.R., RA Hundscheid S.L., Ono N., Scheffer G.L., de Haas M., Schuetz J.D., RA Wijnholds J., Borst P.; RT "cGMP transport by vesicles from human and mouse erythrocytes."; RL FEBS J. 274:439-450(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND THR-513, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19; SER-60; SER-505 RP AND SER-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24836561; DOI=10.1016/j.cmet.2014.03.030; RA Korolnek T., Zhang J., Beardsley S., Scheffer G.L., Hamza I.; RT "Control of metazoan heme homeostasis by a conserved multidrug resistance RT protein."; RL Cell Metab. 19:1008-1019(2014). RN [23] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=26515061; DOI=10.1074/jbc.m115.692103; RA Jansen R.S., Mahakena S., de Haas M., Borst P., van de Wetering K.; RT "ATP-binding Cassette Subfamily C Member 5 (ABCC5) Functions as an Efflux RT Transporter of Glutamate Conjugates and Analogs."; RL J. Biol. Chem. 290:30429-30440(2015). RN [24] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=25964343; DOI=10.1073/pnas.1424638112; RA Jansen R.S., Addie R., Merkx R., Fish A., Mahakena S., Bleijerveld O.B., RA Altelaar M., Ijlst L., Wanders R.J., Borst P., van de Wetering K.; RT "N-lactoyl-amino acids are ubiquitous metabolites that originate from RT CNDP2-mediated reverse proteolysis of lactate and amino acids."; RL Proc. Natl. Acad. Sci. U.S.A. 112:6601-6606(2015). CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) CC family that actively extrudes physiological compounds, and xenobiotics CC from cells. Mediates ATP-dependent transport of endogenous metabolites CC such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro) CC (PubMed:10893247, PubMed:15899835, PubMed:25964343, PubMed:17229149, CC PubMed:12695538, PubMed:12637526). Acts also as a general glutamate CC conjugate and analog transporter that can limit the brain levels of CC endogenous metabolites, drugs, and toxins (PubMed:26515061). Confers CC resistance to the antiviral agent PMEA (PubMed:12695538). Able to CC transport several anticancer drugs including methotrexate, and CC nucleotide analogs in vitro, however it does with low affinity, thus CC the exact role of ABCC5 in mediating resistance still needs to be CC elucidated (PubMed:10840050, PubMed:15899835, PubMed:12435799, CC PubMed:12695538). Acts as a heme transporter required for the CC translocation of cytosolic heme to the secretory pathway CC (PubMed:24836561). May play a role in energy metabolism by regulating CC the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine CC cells (By similarity). {ECO:0000250|UniProtKB:Q9R1X5, CC ECO:0000269|PubMed:10840050, ECO:0000269|PubMed:10893247, CC ECO:0000269|PubMed:12435799, ECO:0000269|PubMed:12637526, CC ECO:0000269|PubMed:12695538, ECO:0000269|PubMed:15899835, CC ECO:0000269|PubMed:17229149, ECO:0000269|PubMed:24836561, CC ECO:0000269|PubMed:25964343, ECO:0000269|PubMed:26515061}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:10840050, CC ECO:0000269|PubMed:12435799, ECO:0000269|PubMed:12695538, CC ECO:0000269|PubMed:15899835}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP CC + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57746, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:10893247, ECO:0000269|PubMed:12637526, CC ECO:0000269|PubMed:12695538}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189; CC Evidence={ECO:0000305|PubMed:10893247}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP CC + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58165, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:10893247, ECO:0000269|PubMed:12637526, CC ECO:0000269|PubMed:12695538}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185; CC Evidence={ECO:0000305|PubMed:10893247}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-acetyl-L-aspartyl-L-glutamate(in) = ADP + H(+) + CC N-acetyl-L-aspartyl-L-glutamate(out) + phosphate; CC Xref=Rhea:RHEA:66728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66729; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate(in) = CC ADP + H(+) + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate(out) + CC phosphate; Xref=Rhea:RHEA:66732, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:76935, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66733; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-acetyl-L-glutamate(in) = ADP + H(+) + N-acetyl- CC L-glutamate(out) + phosphate; Xref=Rhea:RHEA:66740, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:44337, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66741; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-acetyl-L-aspartate(in) = ADP + H(+) + N-acetyl- CC L-aspartate(out) + phosphate; Xref=Rhea:RHEA:66744, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66745; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-2-[5-amino-1-(beta-D-ribosyl)imidazole-4- CC carboxamido]succinate(in) + ATP + H2O = (2S)-2-[5-amino-1-(beta-D- CC ribosyl)imidazole-4-carboxamido]succinate(out) + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:66752, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167466, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66753; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + domoate(in) + H2O = ADP + domoate(out) + H(+) + CC phosphate; Xref=Rhea:RHEA:66756, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167470, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66757; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-citrylglutamate(in) + H2O = ADP + beta- CC citrylglutamate(out) + H(+) + phosphate; Xref=Rhea:RHEA:66736, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76942, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66737; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + kainate(in) = ADP + H(+) + kainate(out) + CC phosphate; Xref=Rhea:RHEA:66760, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:156548, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:26515061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66761; CC Evidence={ECO:0000305|PubMed:26515061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-[(S)-lactoyl]-L-phenylalanine(in) = ADP + H(+) + CC N-[(S)-lactoyl]-L-phenylalanine(out) + phosphate; CC Xref=Rhea:RHEA:66720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167456, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25964343}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66721; CC Evidence={ECO:0000305|PubMed:25964343}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + folate(in) + H2O = ADP + folate(out) + H(+) + phosphate; CC Xref=Rhea:RHEA:66764, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:62501, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15899835}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66765; CC Evidence={ECO:0000305|PubMed:15899835}; CC -!- ACTIVITY REGULATION: cGMP transport is highly sensitive to inhibitors CC of cGMP phosphodiesterase, such as zaprinast, trequinsin and CC sildenafil. {ECO:0000269|PubMed:10893247}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=379 uM for cAMP {ECO:0000269|PubMed:10893247}; CC KM=2.1 uM for cGMP {ECO:0000269|PubMed:10893247}; CC KM=132 uM for cGMP {ECO:0000269|PubMed:17229149}; CC KM=1 mM for folate {ECO:0000269|PubMed:15899835}; CC KM=1 mM for N-[(S)-lactoyl]-L-phenylalanine CC {ECO:0000269|PubMed:25964343}; CC KM=1.9 mM for ZJ43 (glutamate analog) {ECO:0000269|PubMed:26515061}; CC KM=3.5 mM for N-acetylaspartylglutamate (NAAG) CC {ECO:0000269|PubMed:26515061}; CC KM=1.3 mM for methotrexate {ECO:0000269|PubMed:15899835}; CC Vmax=780 pmol/min/mg enzyme for methotrexate transport CC {ECO:0000269|PubMed:15899835}; CC Vmax=875 pmol/min/mg enzyme for folate transport CC {ECO:0000269|PubMed:15899835}; CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane CC {ECO:0000269|PubMed:24836561}; Multi-pass membrane protein CC {ECO:0000255}. Golgi apparatus lumen {ECO:0000269|PubMed:24836561}. CC Endosome membrane {ECO:0000269|PubMed:24836561}. Cytoplasmic granule CC {ECO:0000250|UniProtKB:Q9R1X5}. Apical cell membrane CC {ECO:0000269|PubMed:15501592}; Multi-pass membrane protein CC {ECO:0000255}. Note=In most cells, routes to the basolateral plasma CC membrane, but in the brain capillary endothelial cells that form the CC blood-brain barrier, resides in the apical membrane. CC {ECO:0000269|PubMed:15501592, ECO:0000269|PubMed:24836561}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=O15440-1; Sequence=Displayed; CC Name=2; Synonyms=SV1; CC IsoId=O15440-2; Sequence=VSP_043397, VSP_043402; CC Name=3; Synonyms=SV2; CC IsoId=O15440-3; Sequence=VSP_043398, VSP_043401, VSP_043402; CC Name=4; Synonyms=SV3; CC IsoId=O15440-4; Sequence=VSP_043399, VSP_043400, VSP_043402; CC Name=5; CC IsoId=O15440-5; Sequence=VSP_055354; CC -!- TISSUE SPECIFICITY: [Isoform 3]: Predominant isoform in retinal pigment CC epithelium, bladder, and stomach. {ECO:0000269|PubMed:17521428}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, but levels in brain and CC muscle are especially high (PubMed:9827529, PubMed:10438534, CC PubMed:15501592). All isoforms are equally expressed in retina CC (PubMed:17521428). {ECO:0000269|PubMed:10438534, CC ECO:0000269|PubMed:15501592, ECO:0000269|PubMed:17521428, CC ECO:0000269|PubMed:9827529}. CC -!- MISCELLANEOUS: [Isoform 2]: 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 -!- MISCELLANEOUS: Although other labs have confirmed the ability of ABCC5 CC to transport cGMP in an ATP-dependent manner, they obtained a much CC lower affinity for this substrate (PubMed:12637526, PubMed:12695538). CC The authors conclude that ABCC5 is a low-affinity cyclic nucleotide CC transporter a major function in cGMP excretion is unlikely CC (PubMed:12637526, PubMed:12695538). {ECO:0000269|PubMed:12637526, CC ECO:0000269|PubMed:12695538}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family. CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; 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; AF104942; AAD04169.1; -; mRNA. DR EMBL; AF146074; AAD37716.1; -; mRNA. DR EMBL; AB019002; BAA76608.1; -; mRNA. DR EMBL; U83661; AAB71758.2; -; mRNA. DR EMBL; AY754874; AAW82948.1; -; mRNA. DR EMBL; AY754875; AAW82949.1; -; mRNA. DR EMBL; AY754876; AAW82950.1; -; mRNA. DR EMBL; AY196484; AAO49801.1; -; mRNA. DR EMBL; AC068644; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78307.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78308.1; -; Genomic_DNA. DR EMBL; BC050744; AAH50744.1; -; mRNA. DR EMBL; BC140771; AAI40772.1; -; mRNA. DR EMBL; BC142719; AAI42720.1; -; mRNA. DR EMBL; AB005659; BAA22887.1; -; mRNA. DR CCDS; CCDS33898.1; -. [O15440-4] DR CCDS; CCDS43176.1; -. [O15440-1] DR PIR; JC5667; JC5667. DR RefSeq; NP_001018881.1; NM_001023587.2. [O15440-4] DR RefSeq; NP_001306961.1; NM_001320032.1. DR RefSeq; NP_005679.2; NM_005688.3. [O15440-1] DR RefSeq; XP_005247115.1; XM_005247058.4. DR RefSeq; XP_005247116.1; XM_005247059.4. [O15440-1] DR RefSeq; XP_011510616.1; XM_011512314.1. [O15440-1] DR RefSeq; XP_016860982.1; XM_017005493.1. [O15440-4] DR RefSeq; XP_016860983.1; XM_017005494.1. DR AlphaFoldDB; O15440; -. DR SMR; O15440; -. DR BioGRID; 115368; 48. DR IntAct; O15440; 18. DR MINT; O15440; -. DR STRING; 9606.ENSP00000333926; -. DR BindingDB; O15440; -. DR ChEMBL; CHEMBL2046258; -. DR DrugBank; DB00718; Adefovir dipivoxil. DR DrugBank; DB00770; Alprostadil. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB11672; Curcumin. DR DrugBank; DB14635; Curcumin sulfate. DR DrugBank; DB02527; Cyclic adenosine monophosphate. DR DrugBank; DB00917; Dinoprostone. DR DrugBank; DB00975; Dipyridamole. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB00143; Glutathione. DR DrugBank; DB08818; Hyaluronic acid. DR DrugBank; DB01033; Mercaptopurine. DR DrugBank; DB00642; Pemetrexed. DR DrugBank; DB01032; Probenecid. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB00203; Sildenafil. DR DrugBank; DB01138; Sulfinpyrazone. DR DrugBank; DB00495; Zidovudine. DR DrugCentral; O15440; -. DR GuidetoPHARMACOLOGY; 783; -. DR TCDB; 3.A.1.208.15; the atp-binding cassette (abc) superfamily. DR GlyCosmos; O15440; 8 sites, No reported glycans. DR GlyGen; O15440; 8 sites. DR iPTMnet; O15440; -. DR PhosphoSitePlus; O15440; -. DR BioMuta; ABCC5; -. DR EPD; O15440; -. DR jPOST; O15440; -. DR MassIVE; O15440; -. DR MaxQB; O15440; -. DR PaxDb; 9606-ENSP00000333926; -. DR PeptideAtlas; O15440; -. DR ProteomicsDB; 48667; -. [O15440-1] DR ProteomicsDB; 48668; -. [O15440-2] DR ProteomicsDB; 48669; -. [O15440-3] DR ProteomicsDB; 48670; -. [O15440-4] DR ProteomicsDB; 69929; -. DR Pumba; O15440; -. DR Antibodypedia; 18937; 477 antibodies from 38 providers. DR DNASU; 10057; -. DR Ensembl; ENST00000265586.10; ENSP00000265586.6; ENSG00000114770.17. [O15440-5] DR Ensembl; ENST00000334444.11; ENSP00000333926.6; ENSG00000114770.17. [O15440-1] DR Ensembl; ENST00000382494.6; ENSP00000371934.2; ENSG00000114770.17. [O15440-4] DR Ensembl; ENST00000392579.6; ENSP00000376358.2; ENSG00000114770.17. [O15440-2] DR Ensembl; ENST00000443376.5; ENSP00000416840.1; ENSG00000114770.17. [O15440-3] DR GeneID; 10057; -. DR KEGG; hsa:10057; -. DR MANE-Select; ENST00000334444.11; ENSP00000333926.6; NM_005688.4; NP_005679.2. DR UCSC; uc003fmg.4; human. [O15440-1] DR AGR; HGNC:56; -. DR CTD; 10057; -. DR DisGeNET; 10057; -. DR GeneCards; ABCC5; -. DR HGNC; HGNC:56; ABCC5. DR HPA; ENSG00000114770; Low tissue specificity. DR MIM; 605251; gene. DR neXtProt; NX_O15440; -. DR OpenTargets; ENSG00000114770; -. DR PharmGKB; PA395; -. DR VEuPathDB; HostDB:ENSG00000114770; -. DR eggNOG; KOG0054; Eukaryota. DR GeneTree; ENSGT00940000155470; -. DR HOGENOM; CLU_000604_27_3_1; -. DR InParanoid; O15440; -. DR OMA; QVTDAWT; -. DR OrthoDB; 3384185at2759; -. DR PhylomeDB; O15440; -. DR TreeFam; TF105202; -. DR BRENDA; 7.6.2.3; 2681. DR PathwayCommons; O15440; -. DR Reactome; R-HSA-2142850; Hyaluronan biosynthesis and export. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-9748787; Azathioprine ADME. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR SignaLink; O15440; -. DR BioGRID-ORCS; 10057; 9 hits in 1159 CRISPR screens. DR ChiTaRS; ABCC5; human. DR GeneWiki; ABCC5; -. DR GenomeRNAi; 10057; -. DR Pharos; O15440; Tchem. DR PRO; PR:O15440; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O15440; Protein. DR Bgee; ENSG00000114770; Expressed in right hemisphere of cerebellum and 201 other cell types or tissues. DR ExpressionAtlas; O15440; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IMP:UniProtKB. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central. DR GO; GO:1901505; F:carbohydrate derivative transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0015232; F:heme transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0022884; F:macromolecule transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:Reactome. DR GO; GO:0015216; F:purine nucleotide transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0070730; P:cAMP transport; IMP:UniProtKB. DR GO; GO:0070731; P:cGMP transport; IMP:UniProtKB. DR GO; GO:0140115; P:export across plasma membrane; IDA:ARUK-UCL. DR GO; GO:0098838; P:folate transmembrane transport; IMP:UniProtKB. DR GO; GO:0034775; P:glutathione transmembrane transport; IDA:ARUK-UCL. DR GO; GO:0035351; P:heme transmembrane transport; IMP:UniProtKB. DR GO; GO:0030213; P:hyaluronan biosynthetic process; TAS:Reactome. DR GO; GO:0015865; P:purine nucleotide transport; IDA:ARUK-UCL. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. 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:0006855; P:xenobiotic transmembrane transport; TAS:Reactome. DR GO; GO:0042908; P:xenobiotic transport; IDA:ARUK-UCL. DR CDD; cd18592; ABC_6TM_MRP5_8_9_D1; 1. DR CDD; cd18599; ABC_6TM_MRP5_8_9_D2; 1. DR CDD; cd03250; ABCC_MRP_domain1; 1. DR CDD; cd03244; ABCC_MRP_domain2; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1. DR PANTHER; PTHR24223:SF196; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 5; 1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS50929; ABC_TM1F; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; O15440; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Endosome; Glycoprotein; KW Golgi apparatus; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1437 FT /note="ATP-binding cassette sub-family C member 5" FT /id="PRO_0000093363" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 296..316 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 317..337 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 400..420 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 434..454 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 608..628 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 848..868 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 917..937 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 997..1017 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 1018..1038 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 1104..1124 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 1127..1147 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 179..459 FT /note="ABC transmembrane type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 562..783 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 859..1155 FT /note="ABC transmembrane type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 1193..1427 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 15..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..538 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..827 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..41 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 799..827 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 595..602 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 1227..1234 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 513 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CARBOHYD 494 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 636 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 684 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 890 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 897 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1044 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1417 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 198..225 FT /note="AFMVKHLLEYTQATESNLQYSLLLVLGL -> PSFGDCSISAEVCGNRLHCT FT AILLSCFT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17521428" FT /id="VSP_043397" FT VAR_SEQ 198..212 FT /note="AFMVKHLLEYTQATE -> LAWCCQDLDLGGVSL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17521428" FT /id="VSP_043398" FT VAR_SEQ 198..208 FT /note="AFMVKHLLEYT -> NFQDGCILRSE (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17521428" FT /id="VSP_043399" FT VAR_SEQ 209..225 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17521428" FT /id="VSP_043400" FT VAR_SEQ 213..225 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17521428" FT /id="VSP_043401" FT VAR_SEQ 226..1437 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17521428" FT /id="VSP_043402" FT VAR_SEQ 1033..1075 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_055354" FT CONFLICT 176 FT /note="R -> P (in Ref. 3; BAA76608)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="S -> G (in Ref. 1; AAD04169)" FT /evidence="ECO:0000305" FT CONFLICT 581 FT /note="I -> V (in Ref. 2; AAD37716)" FT /evidence="ECO:0000305" FT CONFLICT 1383 FT /note="T -> N (in Ref. 3; BAA76608 and 8; BAA22887)" FT /evidence="ECO:0000305" SQ SEQUENCE 1437 AA; 160660 MW; 00558076B3BB4C00 CRC64; MKDIDIGKEY IIPSPGYRSV RERTSTSGTH RDREDSKFRR TRPLECQDAL ETAARAEGLS LDASMHSQLR ILDEEHPKGK YHHGLSALKP IRTTSKHQHP VDNAGLFSCM TFSWLSSLAR VAHKKGELSM EDVWSLSKHE SSDVNCRRLE RLWQEELNEV GPDAASLRRV VWIFCRTRLI LSIVCLMITQ LAGFSGPAFM VKHLLEYTQA TESNLQYSLL LVLGLLLTEI VRSWSLALTW ALNYRTGVRL RGAILTMAFK KILKLKNIKE KSLGELINIC SNDGQRMFEA AAVGSLLAGG PVVAILGMIY NVIILGPTGF LGSAVFILFY PAMMFASRLT AYFRRKCVAA TDERVQKMNE VLTYIKFIKM YAWVKAFSQS VQKIREEERR ILEKAGYFQS ITVGVAPIVV VIASVVTFSV HMTLGFDLTA AQAFTVVTVF NSMTFALKVT PFSVKSLSEA SVAVDRFKSL FLMEEVHMIK NKPASPHIKI EMKNATLAWD SSHSSIQNSP KLTPKMKKDK RASRGKKEKV RQLQRTEHQA VLAEQKGHLL LDSDERPSPE EEEGKHIHLG HLRLQRTLHS IDLEIQEGKL VGICGSVGSG KTSLISAILG QMTLLEGSIA ISGTFAYVAQ QAWILNATLR DNILFGKEYD EERYNSVLNS CCLRPDLAIL PSSDLTEIGE RGANLSGGQR QRISLARALY SDRSIYILDD PLSALDAHVG NHIFNSAIRK HLKSKTVLFV THQLQYLVDC DEVIFMKEGC ITERGTHEEL MNLNGDYATI FNNLLLGETP PVEINSKKET SGSQKKSQDK GPKTGSVKKE KAVKPEEGQL VQLEEKGQGS VPWSVYGVYI QAAGGPLAFL VIMALFMLNV GSTAFSTWWL SYWIKQGSGN TTVTRGNETS VSDSMKDNPH MQYYASIYAL SMAVMLILKA IRGVVFVKGT LRASSRLHDE LFRRILRSPM KFFDTTPTGR ILNRFSKDMD EVDVRLPFQA EMFIQNVILV FFCVGMIAGV FPWFLVAVGP LVILFSVLHI VSRVLIRELK RLDNITQSPF LSHITSSIQG LATIHAYNKG QEFLHRYQEL LDDNQAPFFL FTCAMRWLAV RLDLISIALI TTTGLMIVLM HGQIPPAYAG LAISYAVQLT GLFQFTVRLA SETEARFTSV ERINHYIKTL SLEAPARIKN KAPSPDWPQE GEVTFENAEM RYRENLPLVL KKVSFTIKPK EKIGIVGRTG SGKSSLGMAL FRLVELSGGC IKIDGVRISD IGLADLRSKL SIIPQEPVLF SGTVRSNLDP FNQYTEDQIW DALERTHMKE CIAQLPLKLE SEVMENGDNF SVGERQLLCI ARALLRHCKI LILDEATAAM DTETDLLIQE TIREAFADCT MLTIAHRLHT VLGSDRIMVL AQGQVVEFDT PSVLLSNDSS RFYAMFAAAE NKVAVKG //