ID ABCB9_HUMAN Reviewed; 766 AA. AC Q9NP78; B4E2J0; Q5W9G7; Q769F3; Q769F4; Q96AB1; Q9P208; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 206. DE RecName: Full=ABC-type oligopeptide transporter ABCB9; DE EC=7.4.2.6 {ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18434309, ECO:0000269|PubMed:22641697}; DE AltName: Full=ATP-binding cassette sub-family B member 9; DE AltName: Full=ATP-binding cassette transporter 9; DE Short=ABC transporter 9 protein; DE Short=hABCB9; DE AltName: Full=TAP-like protein {ECO:0000303|PubMed:11011155}; DE Short=TAPL {ECO:0000303|PubMed:11011155}; GN Name=ABCB9 {ECO:0000312|HGNC:HGNC:50}; GN Synonyms=KIAA1520 {ECO:0000303|PubMed:10819331}; 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 INDUCTION. RC TISSUE=Embryonic kidney; RX PubMed=11011155; DOI=10.1093/oxfordjournals.jbchem.a022805; RA Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M., RA Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M., Yamaguchi Y., RA Maeda M.; RT "A half-type ABC transporter TAPL is highly conserved between rodent and RT man, and the human gene is not responsive to interferon-gamma in contrast RT to TAP1 and TAP2."; RL J. Biochem. 128:711-718(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Lymphoblast; RX PubMed=10748049; DOI=10.1074/jbc.m001819200; RA Zhang F., Zhang W., Liu L., Fisher C.L., Hui D., Childs S., RA Dorovini-Zis K., Ling V.; RT "Characterization of ABCB9, an ATP binding cassette protein associated with RT lysosomes."; RL J. Biol. Chem. 275:23287-23294(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5). RC TISSUE=Cervix carcinoma, and Embryonic kidney; RX PubMed=13679046; DOI=10.1016/j.bbrc.2003.08.081; RA Kobayashi A., Hori S., Suita N., Maeda M.; RT "Gene organization of human transporter associated with antigen processing- RT like (TAPL, ABCB9): analysis of alternative splicing variants and promoter RT activity."; RL Biochem. Biophys. Res. Commun. 309:815-822(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028; RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.; RT "Alternative splice variants encoding unstable protein domains exist in the RT human brain."; RL J. Mol. Biol. 343:1207-1220(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [6] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=15577206; DOI=10.1248/bpb.27.1916; RA Kobayashi A., Maeda T., Maeda M.; RT "Membrane localization of transporter associated with antigen processing RT (TAP)-like (ABCB9) visualized in vivo with a fluorescence protein-fusion RT technique."; RL Biol. Pharm. Bull. 27:1916-1922(2004). RN [11] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CATALYTIC ACTIVITY. RX PubMed=15863492; DOI=10.1074/jbc.m503231200; RA Wolters J.C., Abele R., Tampe R.; RT "Selective and ATP-dependent translocation of peptides by the homodimeric RT ATP binding cassette transporter TAP-like (ABCB9)."; RL J. Biol. Chem. 280:23631-23636(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY. RX PubMed=17977821; DOI=10.1074/jbc.m708139200; RA Demirel O., Waibler Z., Kalinke U., Grunebach F., Appel S., Brossart P., RA Hasilik A., Tampe R., Abele R.; RT "Identification of a lysosomal peptide transport system induced during RT dendritic cell development."; RL J. Biol. Chem. 282:37836-37843(2007). RN [13] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Placenta; RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x; RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., RA Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [14] RP SUBCELLULAR LOCATION, DOMAIN, AND SUBUNIT. RX PubMed=18952056; DOI=10.1016/j.bbrc.2008.10.078; RA Kamakura A., Fujimoto Y., Motohashi Y., Ohashi K., Ohashi-Kobayashi A., RA Maeda M.; RT "Functional dissection of transmembrane domains of human TAP-like RT (ABCB9)."; RL Biochem. Biophys. Res. Commun. 377:847-851(2008). RN [15] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=18175933; DOI=10.1248/bpb.31.1; RA Ohara T., Ohashi-Kobayashi A., Maeda M.; RT "Biochemical characterization of transporter associated with antigen RT processing (TAP)-like (ABCB9) expressed in insect cells."; RL Biol. Pharm. Bull. 31:1-5(2008). RN [16] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18434309; DOI=10.1074/jbc.m801794200; RA Zhao C., Haase W., Tampe R., Abele R.; RT "Peptide specificity and lipid activation of the lysosomal transport RT complex ABCB9 (TAPL)."; RL J. Biol. Chem. 283:17083-17091(2008). RN [17] RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 136-LYS-LYS-137. RX PubMed=20377823; DOI=10.1111/j.1600-0854.2009.01021.x; RA Demirel O., Bangert I., Tampe R., Abele R.; RT "Tuning the cellular trafficking of the lysosomal peptide transporter TAPL RT by its N-terminal domain."; RL Traffic 11:383-393(2010). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21212514; DOI=10.1248/bpb.34.36; RA Fujimoto Y., Kamakura A., Motohashi Y., Ohashi-Kobayashi A., Maeda M.; RT "Transporter associated with antigen processing-like (ABCB9) stably RT expressed in Chinese hamster ovary-K1 cells is sorted to the microdomains RT of lysosomal membranes."; RL Biol. Pharm. Bull. 34:36-40(2011). RN [19] RP SUBCELLULAR LOCATION, INTERACTION WITH LAMP1 AND LAMP2 (ISOFORM LAMP-2B), RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN. RX PubMed=22641697; DOI=10.1242/jcs.087346; RA Demirel O., Jan I., Wolters D., Blanz J., Saftig P., Tampe R., Abele R.; RT "The lysosomal polypeptide transporter TAPL is stabilized by interaction RT with LAMP-1 and LAMP-2."; RL J. Cell Sci. 125:4230-4240(2012). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=25646430; DOI=10.1073/pnas.1418100112; RA Zollmann T., Moiset G., Tumulka F., Tampe R., Poolman B., Abele R.; RT "Single liposome analysis of peptide translocation by the ABC transporter RT TAPL."; RL Proc. Natl. Acad. Sci. U.S.A. 112:2046-2051(2015). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=30353140; DOI=10.1038/s41598-018-33841-w; RA Bock C., Loehr F., Tumulka F., Reichel K., Wuerz J., Hummer G., RA Schaefer L., Tampe R., Joseph B., Bernhard F., Doetsch V., Abele R.; RT "Structural and functional insights into the interaction and targeting hub RT TMD0 of the polypeptide transporter TAPL."; RL Sci. Rep. 8:15662-15662(2018). RN [22] RP SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-17; ASP-45; ASP-49; ARG-57 AND RP LYS-100, INTERACTION WITH YIF1B, DOMAIN, SITE, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=30877195; DOI=10.1074/jbc.ra118.007071; RA Graab P., Bock C., Weiss K., Hirth A., Koller N., Braner M., Jung J., RA Loehr F., Tampe R., Behrends C., Abele R.; RT "Lysosomal targeting of the ABC transporter TAPL is determined by membrane- RT localized charged residues."; RL J. Biol. Chem. 294:7308-7323(2019). RN [23] RP MUTAGENESIS OF LYS-545 AND HIS-699, CATALYTIC ACTIVITY, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=31417173; DOI=10.1038/s41598-019-48343-6; RA Bock C., Zollmann T., Lindt K.A., Tampe R., Abele R.; RT "Peptide translocation by the lysosomal ABC transporter TAPL is regulated RT by coupling efficiency and activation energy."; RL Sci. Rep. 9:11884-11884(2019). RN [24] RP VARIANT MET-121. RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6; RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., RA Nakamura Y.; RT "Three hundred twenty-six genetic variations in genes encoding nine members RT of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese RT population."; RL J. Hum. Genet. 47:38-50(2002). CC -!- FUNCTION: ATP-dependent low-affinity peptide transporter which CC translocates a broad spectrum of peptides from the cytosol to the CC lysosomal lumen for degradation (PubMed:15863492, PubMed:17977821, CC PubMed:18434309, PubMed:22641697, PubMed:25646430, PubMed:30877195, CC PubMed:31417173, PubMed:30353140). Displays a broad peptide length CC specificity from 6-mer up to at least 59-mer peptides with an optimum CC of 23-mers (PubMed:15863492, PubMed:25646430). Binds and transports CC smaller and larger peptides with the same affinity (PubMed:31417173). CC Favors positively charged, aromatic or hydrophobic residues in the CC N- and C-terminal positions whereas negatively charged residues as well CC as asparagine and methionine are not favored (PubMed:15863492, CC PubMed:17977821, PubMed:18434309). {ECO:0000269|PubMed:15863492, CC ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18434309, CC ECO:0000269|PubMed:22641697, ECO:0000269|PubMed:25646430, CC ECO:0000269|PubMed:30353140, ECO:0000269|PubMed:30877195, CC ECO:0000269|PubMed:31417173}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a [oligopeptide](in) + ATP + H2O = a [oligopeptide](out) + ADP CC + H(+) + phosphate; Xref=Rhea:RHEA:14429, Rhea:RHEA-COMP:10531, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.6; CC Evidence={ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:17977821, CC ECO:0000269|PubMed:18434309, ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:30353140, ECO:0000269|PubMed:30877195, CC ECO:0000269|PubMed:31417173}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14430; CC Evidence={ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:17977821, CC ECO:0000269|PubMed:18434309, ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:30353140, ECO:0000269|PubMed:30877195, CC ECO:0000269|PubMed:31417173}; CC -!- ACTIVITY REGULATION: Transport activity is limited by threshold levels CC of luminal peptide (PubMed:25646430). ATP hydrolysis is reduced in the CC presence of the spatial challenging 18-mer peptide by 50% and the CC branched 16-mer peptide by 75% (PubMed:31417173). Transport rate of the CC longer peptides is strongly reduced (PubMed:31417173). CC {ECO:0000269|PubMed:25646430, ECO:0000269|PubMed:31417173}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.8 uM for a 9-mer oligopeptide {ECO:0000269|PubMed:15863492}; CC KM=2.8 uM for a 9-mer oligopeptide (with a macroscopic filter assay) CC {ECO:0000269|PubMed:25646430}; CC KM=0.9 uM for a 9-mer oligopeptide (with a dual-color CC fluorescenceburst analysis (DCFBA)) {ECO:0000269|PubMed:25646430}; CC KM=15 uM for a 9-mer oligopeptide {ECO:0000269|PubMed:31417173}; CC KM=8 uM for a branched 16-mer oligopeptide CC {ECO:0000269|PubMed:31417173}; CC KM=7 uM for a spatial challenging 18-mer oligopeptide CC {ECO:0000269|PubMed:31417173}; CC KM=4.4 uM for a 9-mer oligopeptide (in presence of mM GTP) CC {ECO:0000269|PubMed:31417173}; CC KM=97 uM for ATP {ECO:0000269|PubMed:31417173}; CC KM=87 uM for GTP {ECO:0000269|PubMed:31417173}; CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:15863492}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. CC {ECO:0000269|PubMed:15863492}; CC -!- SUBUNIT: Homodimer (PubMed:15863492, PubMed:30353140). Interacts (via CC TMD0 region) with LAMP1; this interaction strongly stabilizes ABCB9 and CC protects ABCB9 against lysosomal degradation (PubMed:22641697). CC Interacts (via TMD0 region) with LAMP2 (isoform LAMP-2B) CC (PubMed:22641697). Interacts (via TMD0) with YIF1B; this interaction CC allows (but is not essential) the ER-to-Golgi trafficking and strongly CC depends on a salt bridge within TMD0 (PubMed:30877195). CC {ECO:0000269|PubMed:15863492, ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:30353140, ECO:0000269|PubMed:30877195}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:10748049, CC ECO:0000269|PubMed:15577206, ECO:0000269|PubMed:17897319, CC ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18175933, CC ECO:0000269|PubMed:18952056, ECO:0000269|PubMed:20377823, CC ECO:0000269|PubMed:21212514, ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:30877195}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:10748049, CC ECO:0000269|PubMed:15577206, ECO:0000269|PubMed:17897319, CC ECO:0000269|PubMed:17977821, ECO:0000269|PubMed:18175933, CC ECO:0000269|PubMed:18952056, ECO:0000269|PubMed:20377823, CC ECO:0000269|PubMed:21212514}. Note=May be located in membrane rafts. CC Takes an intracellular route from the endoplasmic reticulum (ER), via CC Golgi and early endosomes to late endosomal and lysosomal compartments CC (PubMed:30877195). {ECO:0000269|PubMed:30877195}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=12A, c1-l; CC IsoId=Q9NP78-1; Sequence=Displayed; CC Name=2; Synonyms=c1-s; CC IsoId=Q9NP78-2; Sequence=VSP_000027; CC Name=3; CC IsoId=Q9NP78-3; Sequence=VSP_000029, VSP_000030; CC Name=4; Synonyms=12B; CC IsoId=Q9NP78-5; Sequence=VSP_041884, VSP_041886; CC Name=5; Synonyms=12C; CC IsoId=Q9NP78-6; Sequence=VSP_041885; CC Name=6; CC IsoId=Q9NP78-7; Sequence=VSP_044884; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, and at moderate levels CC in brain, spinal cord, and thyroid. Not expressed in monocytes but CC strongly expressed during differentiation of monocytes to dendritic CC cells and macrophages. {ECO:0000269|PubMed:10748049, CC ECO:0000269|PubMed:17977821}. CC -!- INDUCTION: Not induced by interferon-gamma. CC {ECO:0000269|PubMed:11011155}. CC -!- DOMAIN: Divided into an N-terminal domain (TMD0) comprising four CC transmembrane helices and the following core domain (coreABCB9) CC (PubMed:18952056). TMD0 is required for lysosomal localization and CC LAMP1, LAMP2 and YIF1B interaction (PubMed:15577206, PubMed:18175933, CC PubMed:20377823, PubMed:22641697, PubMed:30877195). The core domain is CC required for homodimerization and peptide transport activity CC (PubMed:18952056, PubMed:20377823). {ECO:0000269|PubMed:15577206, CC ECO:0000269|PubMed:18175933, ECO:0000269|PubMed:18952056, CC ECO:0000269|PubMed:20377823, ECO:0000269|PubMed:22641697, CC ECO:0000269|PubMed:30877195}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC MHC peptide exporter (TC 3.A.1.209) subfamily. {ECO:0000305}. CC -!- CAUTION: Has also been detected in the endoplasmic reticulum but CC appears to be a lysosomal protein in vivo. CC {ECO:0000305|PubMed:11011155}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA96044.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD66830.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB045381; BAA97989.2; -; mRNA. DR EMBL; AF216494; AAF89993.1; -; mRNA. DR EMBL; AB112582; BAC98409.1; -; mRNA. DR EMBL; AB112583; BAC98410.1; -; mRNA. DR EMBL; AB177852; BAD66830.1; ALT_INIT; mRNA. DR EMBL; AB040953; BAA96044.2; ALT_INIT; mRNA. DR EMBL; AK304295; BAG65152.1; -; mRNA. DR EMBL; AC026362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017348; AAH17348.1; -; mRNA. DR CCDS; CCDS58286.1; -. [Q9NP78-7] DR CCDS; CCDS58287.1; -. [Q9NP78-6] DR CCDS; CCDS58288.1; -. [Q9NP78-5] DR CCDS; CCDS9241.1; -. [Q9NP78-1] DR RefSeq; NP_001229942.1; NM_001243013.1. [Q9NP78-7] DR RefSeq; NP_001229943.1; NM_001243014.1. [Q9NP78-6] DR RefSeq; NP_062570.1; NM_019624.3. [Q9NP78-2] DR RefSeq; NP_062571.1; NM_019625.3. [Q9NP78-1] DR RefSeq; NP_982269.2; NM_203444.3. [Q9NP78-5] DR RefSeq; XP_011536397.1; XM_011538095.2. [Q9NP78-1] DR RefSeq; XP_011536398.1; XM_011538096.2. [Q9NP78-1] DR RefSeq; XP_016874592.1; XM_017019103.1. [Q9NP78-1] DR AlphaFoldDB; Q9NP78; -. DR SMR; Q9NP78; -. DR BioGRID; 117021; 39. DR IntAct; Q9NP78; 9. DR STRING; 9606.ENSP00000440288; -. DR ChEMBL; CHEMBL1293189; -. DR TCDB; 3.A.1.209.2; the atp-binding cassette (abc) superfamily. DR GlyGen; Q9NP78; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NP78; -. DR PhosphoSitePlus; Q9NP78; -. DR BioMuta; ABCB9; -. DR DMDM; 22095458; -. DR EPD; Q9NP78; -. DR MassIVE; Q9NP78; -. DR PaxDb; 9606-ENSP00000440288; -. DR PeptideAtlas; Q9NP78; -. DR ProteomicsDB; 5823; -. DR ProteomicsDB; 81917; -. [Q9NP78-1] DR ProteomicsDB; 81918; -. [Q9NP78-2] DR ProteomicsDB; 81919; -. [Q9NP78-3] DR ProteomicsDB; 81920; -. [Q9NP78-5] DR ProteomicsDB; 81921; -. [Q9NP78-6] DR Antibodypedia; 31719; 266 antibodies from 30 providers. DR DNASU; 23457; -. DR Ensembl; ENST00000280560.13; ENSP00000280560.8; ENSG00000150967.19. [Q9NP78-1] DR Ensembl; ENST00000344275.11; ENSP00000456813.1; ENSG00000150967.19. [Q9NP78-6] DR Ensembl; ENST00000346530.9; ENSP00000280559.7; ENSG00000150967.19. [Q9NP78-2] DR Ensembl; ENST00000392439.7; ENSP00000376234.3; ENSG00000150967.19. [Q9NP78-1] DR Ensembl; ENST00000442833.6; ENSP00000456375.1; ENSG00000150967.19. [Q9NP78-5] DR Ensembl; ENST00000540285.5; ENSP00000441734.1; ENSG00000150967.19. [Q9NP78-7] DR Ensembl; ENST00000542678.5; ENSP00000440288.1; ENSG00000150967.19. [Q9NP78-1] DR GeneID; 23457; -. DR KEGG; hsa:23457; -. DR MANE-Select; ENST00000280560.13; ENSP00000280560.8; NM_019625.4; NP_062571.1. DR UCSC; uc001udm.5; human. [Q9NP78-1] DR AGR; HGNC:50; -. DR CTD; 23457; -. DR DisGeNET; 23457; -. DR GeneCards; ABCB9; -. DR HGNC; HGNC:50; ABCB9. DR HPA; ENSG00000150967; Tissue enhanced (brain). DR MIM; 605453; gene. DR neXtProt; NX_Q9NP78; -. DR OpenTargets; ENSG00000150967; -. DR PharmGKB; PA24391; -. DR VEuPathDB; HostDB:ENSG00000150967; -. DR eggNOG; KOG0058; Eukaryota. DR GeneTree; ENSGT00940000155431; -. DR InParanoid; Q9NP78; -. DR OrthoDB; 5487044at2759; -. DR PhylomeDB; Q9NP78; -. DR TreeFam; TF105197; -. DR BRENDA; 7.4.2.5; 2681. DR PathwayCommons; Q9NP78; -. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR SABIO-RK; Q9NP78; -. DR SignaLink; Q9NP78; -. DR BioGRID-ORCS; 23457; 15 hits in 1160 CRISPR screens. DR ChiTaRS; ABCB9; human. DR GeneWiki; ABCB9; -. DR GenomeRNAi; 23457; -. DR Pharos; Q9NP78; Tbio. DR PRO; PR:Q9NP78; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9NP78; Protein. DR Bgee; ENSG00000150967; Expressed in buccal mucosa cell and 171 other cell types or tissues. DR ExpressionAtlas; Q9NP78; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IDA:UniProtKB. DR GO; GO:0015440; F:ABC-type peptide transporter activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0006518; P:peptide metabolic process; IDA:UniProtKB. DR GO; GO:0015833; P:peptide transport; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd18784; ABC_6TM_ABCB9_like; 1. DR CDD; cd03248; ABCC_TAP; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; IPR030254; ABCB9_6-TMD. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039421; Type_1_exporter. DR PANTHER; PTHR43394:SF13; ATP BINDING CASSETTE SUBFAMILY B MEMBER 9; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR Genevisible; Q9NP78; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Lysosome; Membrane; Nucleotide-binding; KW Peptide transport; Protein transport; Reference proteome; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..766 FT /note="ABC-type oligopeptide transporter ABCB9" FT /id="PRO_0000000252" FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 185..205 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 319..339 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 416..436 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 188..471 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 504..740 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 539..546 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT SITE 17 FT /note="Intramolecular salt bridge with Arg-57. Essential FT for the release from the ER" FT /evidence="ECO:0000269|PubMed:30877195" FT SITE 45 FT /note="Important for the second trafficking step from the FT Golgi to the endosomal and lysosomal compartments" FT /evidence="ECO:0000269|PubMed:30877195" FT SITE 49 FT /note="Important for the second trafficking step from the FT Golgi to the endosomal and lysosomal compartments" FT /evidence="ECO:0000269|PubMed:30877195" FT SITE 57 FT /note="Intramolecular salt bridge with Asp-17. Essential FT for the release from the ER" FT /evidence="ECO:0000269|PubMed:30877195" FT VAR_SEQ 418..460 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10748049" FT /id="VSP_000027" FT VAR_SEQ 461..523 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_044884" FT VAR_SEQ 582..596 FT /note="ISLVSQEPVLFARSI -> VCARAWATLLRPFCI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_000029" FT VAR_SEQ 597..766 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_000030" FT VAR_SEQ 681..683 FT /note="IQQ -> CAG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:13679046" FT /id="VSP_041884" FT VAR_SEQ 682..766 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:13679046" FT /id="VSP_041885" FT VAR_SEQ 684..766 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:13679046" FT /id="VSP_041886" FT VARIANT 121 FT /note="V -> M (in dbSNP:rs3803002)" FT /evidence="ECO:0000269|PubMed:11829140" FT /id="VAR_013701" FT MUTAGEN 17 FT /note="D->N: Loss of lysosomal localization. Does not FT affect interaction between coreABCB9 and TMD0 domains. Does FT not affect dimerization. Does not affect peptide transport FT activity. Decreases interaction with YIF1B." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 17 FT /note="D->R: Loss of lysosomal localization. Does not FT affect lysosomal localization; when associated with D-57. FT Does not affect interaction between coreABCB9 and TMD0 FT domains. Does not affect interaction between coreABCB9 and FT TMD0 domains; when associated with D-57. Does not affect FT interaction between coreABCB9 and TMD0 domains; when FT associated with D-100." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 45 FT /note="D->K: Loss of lysosomal localization; when FT assosiated with K-49. Loss of lysosomal localization; when FT assosiated with K-49 and D-100. Does not affect peptide FT transport activity; when assosiated with K-49 and D-100." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 45 FT /note="D->N: Decreases lysosomal localization; when FT associated with N-49." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 49 FT /note="D->K: Loss of lysosomal localization; when FT assosiated with K-45. Loss of lysosomal localization; when FT assosiated with K-45 and D-100. Does not affect peptide FT transport activity; when assosiated with K-45 and D-100." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 49 FT /note="D->N: Decreases lysosomal localization; when FT associated with N-45." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 57 FT /note="R->A: Decreases lysosomal localization. Loss of FT lysosomal localization; when associated with A-100." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 57 FT /note="R->D: Loss of lysosomal localization. Does not FT affect lysosomal localization; when associated with R-17. FT Does not affect interaction between coreABCB9 and TMD0 FT domains. Does not affect interaction between coreABCB9 and FT TMD0 domains; when associated with R-17." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 100 FT /note="K->A: Decreases lysosomal localization. Loss of FT lysosomal localization; when associated with A-57." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 100 FT /note="K->D: Decreases lysosomal localization. Loss of FT lysosomal localization; when assosiated with R-17. Loss of FT lysosomal localization; when assosiated with K-45 and K-49. FT Does not affect peptide transport activity; when assosiated FT with K-45 and K-49. Does not affect interaction between FT coreABCB9 and TMD0 domains. Does not affect interaction FT between coreABCB9 and TMD0 domains; when associated with FT R-17." FT /evidence="ECO:0000269|PubMed:30877195" FT MUTAGEN 136..137 FT /note="LL->AA: No effect on lysosomal localization." FT /evidence="ECO:0000269|PubMed:20377823" FT MUTAGEN 545 FT /note="K->A: Loss of peptide transport activity; whena FT ssociated with A-699." FT /evidence="ECO:0000269|PubMed:31417173" FT MUTAGEN 699 FT /note="H->A: Loss of peptide transport activity; whena FT ssociated with A-545." FT /evidence="ECO:0000269|PubMed:31417173" SQ SEQUENCE 766 AA; 84475 MW; C83FA62C929EC792 CRC64; MRLWKAVVVT LAFMSVDICV TTAIYVFSHL DRSLLEDIRH FNIFDSVLDL WAACLYRSCL LLGATIGVAK NSALGPRRLR ASWLVITLVC LFVGIYAMVK LLLFSEVRRP IRDPWFWALF VWTYISLGAS FLLWWLLSTV RPGTQALEPG AATEAEGFPG SGRPPPEQAS GATLQKLLSY TKPDVAFLVA ASFFLIVAAL GETFLPYYTG RAIDGIVIQK SMDQFSTAVV IVCLLAIGSS FAAGIRGGIF TLIFARLNIR LRNCLFRSLV SQETSFFDEN RTGDLISRLT SDTTMVSDLV SQNINVFLRN TVKVTGVVVF MFSLSWQLSL VTFMGFPIIM MVSNIYGKYY KRLSKEVQNA LARASNTAEE TISAMKTVRS FANEEEEAEV YLRKLQQVYK LNRKEAAAYM YYVWGSGLTL LVVQVSILYY GGHLVISGQM TSGNLIAFII YEFVLGDCME SVGSVYSGLM QGVGAAEKVF EFIDRQPTMV HDGSLAPDHL EGRVDFENVT FTYRTRPHTQ VLQNVSFSLS PGKVTALVGP SGSGKSSCVN ILENFYPLEG GRVLLDGKPI SAYDHKYLHR VISLVSQEPV LFARSITDNI SYGLPTVPFE MVVEAAQKAN AHGFIMELQD GYSTETGEKG AQLSGGQKQR VAMARALVRN PPVLILDEAT SALDAESEYL IQQAIHGNLQ KHTVLIIAHR LSTVEHAHLI VVLDKGRVVQ QGTHQQLLAQ GGLYAKLVQR QMLGLQPAAD FTAGHNEPVA NGSHKA //