ABCB6_HUMAN
ID ABCB6_HUMAN Reviewed; 842 AA.
AC Q9NP58; O75542; Q49A66; Q59GQ5; Q6ZME6; Q96ME8; Q9HAQ6; Q9HAQ7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000305};
DE AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000305};
DE EC=7.6.2.5 {ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442};
DE AltName: Full=Mitochondrial ABC transporter 3 {ECO:0000303|PubMed:10837493};
DE Short=Mt-ABC transporter 3 {ECO:0000303|PubMed:10837493};
DE AltName: Full=P-glycoprotein-related protein;
DE AltName: Full=Ubiquitously-expressed mammalian ABC half transporter;
GN Name=ABCB6 {ECO:0000312|HGNC:HGNC:47};
GN Synonyms=MTABC3 {ECO:0000303|PubMed:10837493}, PRP, UMAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10837493; DOI=10.1074/jbc.275.23.17536;
RA Mitsuhashi N., Miki T., Senbongi H., Yokoi N., Yano H., Miyazaki M.,
RA Nakajima N., Iwanaga T., Yokoyama Y., Shibata T., Seino S.;
RT "MTABC3, a novel mitochondrial ATP-binding cassette protein involved in
RT iron homeostasis.";
RL J. Biol. Chem. 275:17536-17540(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-229.
RC TISSUE=Colon, and Liver;
RX PubMed=11955620; DOI=10.1016/s0167-4781(01)00340-2;
RA Emadi-Konjin H.-P., Zhang H., Anandan V., Sun D., Schuetz J.D.,
RA Furuya K.N.;
RT "Isolation of a genomic clone containing the promoter region of the human
RT ATP binding cassette (ABC) transporter, ABCB6.";
RL Biochim. Biophys. Acta 1574:117-130(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hirsch-Ernst K.I., Schaefer A., Ernst B.-P., Schmitz-Salue C., Awuah D.,
RA Kahl G.F.;
RT "Subcellular localization of the ABC transporter umat.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 112-842 (ISOFORM 1).
RC TISSUE=Hepatoma, and Neuroepithelium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-842 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY CELLULAR PORPHYRINS, SUBUNIT,
RP SUBCELLULAR LOCATION, INTERACTION WITH HEMIN, AND CATALYTIC ACTIVITY.
RX PubMed=17006453; DOI=10.1038/nature05125;
RA Krishnamurthy P.C., Du G., Fukuda Y., Sun D., Sampath J., Mercer K.E.,
RA Wang J., Sosa-Pineda B., Murti K.G., Schuetz J.D.;
RT "Identification of a mammalian mitochondrial porphyrin transporter.";
RL Nature 443:586-589(2006).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17661442; DOI=10.1021/bi700015m;
RA Paterson J.K., Shukla S., Black C.M., Tachiwada T., Garfield S.,
RA Wincovitch S., Ernst D.N., Agadir A., Li X., Ambudkar S.V., Szakacs G.,
RA Akiyama S., Gottesman M.M.;
RT "Human ABCB6 localizes to both the outer mitochondrial membrane and the
RT plasma membrane.";
RL Biochemistry 46:9443-9452(2007).
RN [10]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=18279659; DOI=10.1016/j.bbrc.2008.02.027;
RA Tsuchida M., Emi Y., Kida Y., Sakaguchi M.;
RT "Human ABC transporter isoform B6 (ABCB6) localizes primarily in the Golgi
RT apparatus.";
RL Biochem. Biophys. Res. Commun. 369:369-375(2008).
RN [11]
RP INDUCTION, GLYCOSYLATION AT ASN-6, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP ASN-6; CYS-8; CYS-26; CYS-50; CYS-120; ASN-447; ASN-498; ASN-677 AND
RP ASN-775, AND DISULFIDE BOND.
RX PubMed=21199866; DOI=10.1074/jbc.m110.174516;
RA Fukuda Y., Aguilar-Bryan L., Vaxillaire M., Dechaume A., Wang Y., Dean M.,
RA Moitra K., Bryan J., Schuetz J.D.;
RT "Conserved intramolecular disulfide bond is critical to trafficking and
RT fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea
RT receptor 1 (SUR1)/ABCC8.";
RL J. Biol. Chem. 286:8481-8492(2011).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=21266531; DOI=10.1093/toxsci/kfr008;
RA Chavan H., Oruganti M., Krishnamurthy P.;
RT "The ATP-binding cassette transporter ABCB6 is induced by arsenic and
RT protects against arsenic cytotoxicity.";
RL Toxicol. Sci. 120:519-528(2011).
RN [13]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND INDUCTION.
RX PubMed=22655043; DOI=10.1371/journal.pone.0037378;
RA Kiss K., Brozik A., Kucsma N., Toth A., Gera M., Berry L., Vallentin A.,
RA Vial H., Vidal M., Szakacs G.;
RT "Shifting the paradigm: the putative mitochondrial protein ABCB6 resides in
RT the lysosomes of cells and in the plasma membrane of erythrocytes.";
RL PLoS ONE 7:e37378-e37378(2012).
RN [14]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS MCOPCB7 THR-57 AND
RP VAL-811, AND CHARACTERIZATION OF VARIANTS MCOPCB7 THR-57 AND VAL-811.
RX PubMed=22226084; DOI=10.1016/j.ajhg.2011.11.026;
RA Wang L., He F., Bu J., Liu X., Du W., Dong J., Cooney J.D., Dubey S.K.,
RA Shi Y., Gong B., Li J., McBride P.F., Jia Y., Lu F., Soltis K.A., Lin Y.,
RA Namburi P., Liang C., Sundaresan P., Paw B.H., Li D.Y., Phillips J.D.,
RA Yang Z.;
RT "ABCB6 mutations cause ocular coloboma.";
RL Am. J. Hum. Genet. 90:40-48(2012).
RN [15]
RP POLYMORPHISM, INVOLVEMENT IN LANGEREIS BLOOD GROUP SYSTEM, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22246506; DOI=10.1038/ng.1069;
RA Helias V., Saison C., Ballif B.A., Peyrard T., Takahashi J., Takahashi H.,
RA Tanaka M., Deybach J.C., Puy H., Le Gall M., Sureau C., Pham B.N.,
RA Le Pennec P.Y., Tani Y., Cartron J.P., Arnaud L.;
RT "ABCB6 is dispensable for erythropoiesis and specifies the new blood group
RT system Langereis.";
RL Nat. Genet. 44:170-173(2012).
RN [16]
RP SUBCELLULAR LOCATION, INDUCTION, INVOLVEMENT IN PSHK2, AND VARIANTS PSHK2
RP GLN-375 AND TRP-375.
RX PubMed=23180570; DOI=10.1002/ajh.23357;
RA Andolfo I., Alper S.L., Delaunay J., Auriemma C., Russo R., Asci R.,
RA Esposito M.R., Sharma A.K., Shmukler B.E., Brugnara C., De Franceschi L.,
RA Iolascon A.;
RT "Missense mutations in the ABCB6 transporter cause dominant familial
RT pseudohyperkalemia.";
RL Am. J. Hematol. 88:66-72(2013).
RN [17]
RP SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF LYS-629.
RX PubMed=23792964; DOI=10.1074/jbc.m113.485284;
RA Chavan H., Khan M.M., Tegos G., Krishnamurthy P.;
RT "Efficient purification and reconstitution of ATP binding cassette
RT transporter B6 (ABCB6) for functional and structural studies.";
RL J. Biol. Chem. 288:22658-22669(2013).
RN [18]
RP FUNCTION.
RX PubMed=25202056;
RA Minami K., Kamijo Y., Nishizawa Y., Tabata S., Horikuchi F., Yamamoto M.,
RA Kawahara K., Shinsato Y., Tachiwada T., Chen Z.S., Tsujikawa K.,
RA Nakagawa M., Seki N., Akiyama S., Arima K., Takeda Y., Furukawa T.;
RT "Expression of ABCB6 is related to resistance to 5-FU, SN-38 and
RT vincristine.";
RL Anticancer Res. 34:4767-4773(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP MUTAGENESIS OF LYS-629, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP REGION, AND DOMAIN.
RX PubMed=25627919; DOI=10.1042/bj20141085;
RA Kiss K., Kucsma N., Brozik A., Tusnady G.E., Bergam P., van Niel G.,
RA Szakacs G.;
RT "Role of the N-terminal transmembrane domain in the endo-lysosomal
RT targeting and function of the human ABCB6 protein.";
RL Biochem. J. 467:127-139(2015).
RN [21]
RP SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-629, AND
RP CHARACTERIZATION OF VARIANT DUH3 GLU-579.
RX PubMed=29940187; DOI=10.1016/j.jmb.2018.06.033;
RA Bergam P., Reisecker J.M., Rakvacs Z., Kucsma N., Raposo G., Szakacs G.,
RA van Niel G.;
RT "ABCB6 Resides in Melanosomes and Regulates Early Steps of Melanogenesis
RT Required for PMEL Amyloid Matrix Formation.";
RL J. Mol. Biol. 430:3802-3818(2018).
RN [22]
RP MUTAGENESIS OF LYS-629, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=31053883; DOI=10.1007/s00018-019-03105-5;
RA Rakvacs Z., Kucsma N., Gera M., Igriczi B., Kiss K., Barna J., Kovacs D.,
RA Vellai T., Bencs L., Reisecker J.M., Szoboszlai N., Szakacs G.;
RT "The human ABCB6 protein is the functional homologue of HMT-1 proteins
RT mediating cadmium detoxification.";
RL Cell. Mol. Life Sci. 76:4131-4144(2019).
RN [23]
RP INVOLVEMENT IN PSHK2, AND VARIANT PSHK2 GLN-723.
RX PubMed=24947683; DOI=10.1111/trf.12757;
RA Bawazir W.M., Flatt J.F., Wallis J.P., Rendon A., Cardigan R.A., New H.V.,
RA Wiltshire M., Page L., Chapman C.E., Stewart G.W., Bruce L.J.;
RT "Familial pseudohyperkalemia in blood donors: a novel mutation with
RT implications for transfusion practice.";
RL Transfusion 54:3043-3050(2014).
RN [24]
RP STRUCTURE BY NMR OF 558-842 IN COMPLEX WITH ADP.
RX PubMed=16791740; DOI=10.1007/s10858-006-9000-6;
RA Kurashima-Ito K., Ikeya T., Senbongi H., Tochio H., Mikawa T., Shibata T.,
RA Ito Y.;
RT "Heteronuclear multidimensional NMR and homology modelling studies of the
RT C-terminal nucleotide-binding domain of the human mitochondrial ABC
RT transporter ABCB6.";
RL J. Biomol. NMR 35:53-71(2006).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 558-842 IN COMPLEXES WITH ADP;
RP ATP AND PHOSPHATE.
RX PubMed=20823549; DOI=10.1107/s0907444910028593;
RA Haffke M., Menzel A., Carius Y., Jahn D., Heinz D.W.;
RT "Structures of the nucleotide-binding domain of the human ABCB6 transporter
RT and its complexes with nucleotides.";
RL Acta Crystallogr. D 66:979-987(2010).
RN [26] {ECO:0007744|PDB:7D7N, ECO:0007744|PDB:7D7R}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), SUBUNIT, REGION,
RP MUTAGENESIS OF TYR-286; VAL-531; MET-542 AND TRP-546, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33007128; DOI=10.1002/pro.3960;
RA Wang C., Cao C., Wang N., Wang X., Wang X., Zhang X.C.;
RT "Cryo-electron microscopy structure of human ABCB6 transporter.";
RL Protein Sci. 29:2363-2374(2020).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-69.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [28]
RP VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579, AND CHARACTERIZATION OF
RP VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579.
RX PubMed=23519333; DOI=10.1038/jid.2013.145;
RA Zhang C., Li D., Zhang J., Chen X., Huang M., Archacki S., Tian Y., Ren W.,
RA Mei A., Zhang Q., Fang M., Su Z., Yin Y., Liu D., Chen Y., Cui X., Li C.,
RA Yang H., Wang Q., Wang J., Liu M., Deng Y.;
RT "Mutations in ABCB6 cause dyschromatosis universalis hereditaria.";
RL J. Invest. Dermatol. 133:2221-2228(2013).
RN [29]
RP VARIANT DUH3 LYS-555.
RX PubMed=24224009; DOI=10.1371/journal.pone.0079808;
RA Cui Y.X., Xia X.Y., Zhou Y., Gao L., Shang X.J., Ni T., Wang W.P.,
RA Fan X.B., Yin H.L., Jiang S.J., Yao B., Hu Y.A., Wang G., Li X.J.;
RT "Novel mutations of ABCB6 associated with autosomal dominant dyschromatosis
RT universalis hereditaria.";
RL PLoS ONE 8:E79808-E79808(2013).
RN [30]
RP VARIANTS DUH3 ARG-322 AND HIS-424.
RX PubMed=25288164; DOI=10.1016/j.jdermsci.2014.08.015;
RA Lu C., Liu J., Liu F., Liu Y., Ma D., Zhang X.;
RT "Novel missense mutations of ABCB6 in two chinese families with
RT dyschromatosis universalis hereditaria.";
RL J. Dermatol. Sci. 76:255-258(2014).
RN [31]
RP VARIANT DUH3 VAL-453.
RX PubMed=24498303; DOI=10.1371/journal.pone.0087250;
RA Liu H., Li Y., Hung K.K., Wang N., Wang C., Chen X., Sheng D., Fu X.,
RA See K., Foo J.N., Low H., Liany H., Irwan I.D., Liu J., Yang B., Chen M.,
RA Yu Y., Yu G., Niu G., You J., Zhou Y., Ma S., Wang T., Yan X., Goh B.K.,
RA Common J.E., Lane B.E., Sun Y., Zhou G., Lu X., Wang Z., Tian H., Cao Y.,
RA Chen S., Liu Q., Liu J., Zhang F.;
RT "Genome-wide linkage, exome sequencing and functional analyses identify
RT ABCB6 as the pathogenic gene of dyschromatosis universalis hereditaria.";
RL PLoS ONE 9:E87250-E87250(2014).
RN [32]
RP VARIANTS GLN-192; TRP-276; THR-492; SER-521; SER-588 AND THR-681,
RP CHARACTERIZATION OF VARIANTS TRP-276; THR-492 AND SER-521, CATALYTIC
RP ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27507172; DOI=10.1038/ncomms12353;
RA Fukuda Y., Cheong P.L., Lynch J., Brighton C., Frase S., Kargas V.,
RA Rampersaud E., Wang Y., Sankaran V.G., Yu B., Ney P.A., Weiss M.J.,
RA Vogel P., Bond P.J., Ford R.C., Trent R.J., Schuetz J.D.;
RT "The severity of hereditary porphyria is modulated by the porphyrin
RT exporter and Lan antigen ABCB6.";
RL Nat. Commun. 7:12353-12353(2016).
CC -!- FUNCTION: ATP-dependent transporter that catalyzes the transport of a
CC broad-spectrum of porphyrins from the cytoplasm to the extracellular
CC space through the plasma membrane or into the vesicle lumen
CC (PubMed:33007128, PubMed:27507172, PubMed:17661442, PubMed:23792964).
CC May also function as an ATP-dependent importer of porphyrins from the
CC cytoplasm into the mitochondria, in turn may participate in the de novo
CC heme biosynthesis regulation and in the coordination of heme and iron
CC homeostasis during phenylhydrazine stress (PubMed:17006453,
CC PubMed:10837493, PubMed:23792964, PubMed:33007128). May also play a key
CC role in the early steps of melanogenesis producing PMEL amyloid fibrils
CC (PubMed:29940187). In vitro, it confers to cells a resistance to toxic
CC metal such as arsenic and cadmium and against chemotherapeutics agent
CC such as 5-fluorouracil, SN-38 and vincristin (PubMed:25202056,
CC PubMed:21266531, PubMed:31053883). In addition may play a role in the
CC transition metal homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:O70595, ECO:0000269|PubMed:10837493,
CC ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442,
CC ECO:0000269|PubMed:21266531, ECO:0000269|PubMed:23792964,
CC ECO:0000269|PubMed:25202056, ECO:0000269|PubMed:27507172,
CC ECO:0000269|PubMed:29940187, ECO:0000269|PubMed:31053883,
CC ECO:0000269|PubMed:33007128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate;
CC Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344,
CC ChEBI:CHEBI:456216; EC=7.6.2.5;
CC Evidence={ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442,
CC ECO:0000269|PubMed:23792964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262;
CC Evidence={ECO:0000269|PubMed:17006453, ECO:0000305|PubMed:17661442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin
CC III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:131725, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:27507172,
CC ECO:0000269|PubMed:33007128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
CC Evidence={ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:27507172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide
CC a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58687, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17661442, ECO:0000269|PubMed:23792964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000305|PubMed:17661442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP +
CC coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate +
CC protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:33007128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC Evidence={ECO:0000269|PubMed:23792964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out)
CC + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167478, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate +
CC uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167480, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate +
CC uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167479, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by MgATP with an
CC IC(50) of 1.03 mM and up-regulated by coporphyrin III> hemin >
CC protoporphyrin IX (PubMed:23792964). ATPase activity for hemin is up-
CC regulated by glutathione (PubMed:33007128). The ATPase activity is
CC impaired by increasing copper concentrations (0-300 uM)
CC (PubMed:33007128). The ATPase activity is stimulated in presence of
CC glutathione for increasing copper concentrations (0-300 uM)
CC (PubMed:33007128). {ECO:0000269|PubMed:23792964,
CC ECO:0000269|PubMed:33007128}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.99 mM for ATP (from purified mitochondrial ABCB6)
CC {ECO:0000269|PubMed:23792964};
CC KM=0.97 mM for ATP (from liposome-reconstituted purified
CC mitochondrial ABCB6) {ECO:0000269|PubMed:23792964};
CC KM=11.97 uM for coproporphyrin III (from liposome-reconstituted
CC purified mitochondrial ABCB6) {ECO:0000269|PubMed:23792964};
CC KM=51 uM for glutathione (in the presence of 10 uM of hemin)
CC {ECO:0000269|PubMed:33007128};
CC KM=190 nM for hemin (in the presence of 1 mM of glutathione)
CC {ECO:0000269|PubMed:33007128};
CC KM=600 nM for hematin (in the presence of 1 mM of glutathione)
CC {ECO:0000269|PubMed:33007128};
CC KM=148 nM for Fe-coproporphyrin III (in the presence of 1 mM of
CC glutathione) {ECO:0000269|PubMed:33007128};
CC Vmax=492.3 nmol/min/mg enzyme toward ATP (from purified mitochondrial
CC ABCB6) {ECO:0000269|PubMed:23792964};
CC Vmax=614 nmol/min/mg enzyme toward ATP (from liposome-reconstituted
CC purified mitochondrial ABCB6) {ECO:0000269|PubMed:23792964};
CC Vmax=29.6 pmol/min/mg enzyme toward coproporphyrin III (from
CC liposome-reconstituted purified mitochondrial ABCB6)
CC {ECO:0000269|PubMed:23792964};
CC Vmax=5.13 pmol/min/mg enzyme toward verteporfin
CC {ECO:0000269|PubMed:23792964};
CC Vmax=2.7 pmol/min/mg enzyme toward tomatine
CC {ECO:0000269|PubMed:23792964};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16791740,
CC ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:23792964,
CC ECO:0000269|PubMed:25627919, ECO:0000269|PubMed:33007128}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17661442,
CC ECO:0000269|PubMed:22246506, ECO:0000269|PubMed:22655043,
CC ECO:0000269|PubMed:23180570, ECO:0000269|PubMed:27507172}; Multi-pass
CC membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18279659, ECO:0000269|PubMed:21199866,
CC ECO:0000269|PubMed:22226084}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18279659,
CC ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22226084}; Multi-pass
CC membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:25627919}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:22655043,
CC ECO:0000269|PubMed:25627919, ECO:0000269|PubMed:29940187,
CC ECO:0000269|PubMed:31053883}. Late endosome membrane
CC {ECO:0000250|UniProtKB:O70595}. Early endosome membrane
CC {ECO:0000250|UniProtKB:O70595}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:22655043}. Mitochondrion
CC {ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:23792964}. Endosome,
CC multivesicular body membrane {ECO:0000269|PubMed:25627919}. Melanosome
CC membrane {ECO:0000269|PubMed:29940187}. Note=Present in the membrane of
CC mature erythrocytes and in exosomes released from reticulocytes during
CC the final steps of erythroid maturation (PubMed:22655043). Traffics
CC from endoplasmic reticulum to Golgi during its glycans's maturation,
CC therefrom is first targeted to the plasma membrane, and is rapidly
CC internalized through endocytosis to be distributed to the limiting
CC membrane of multivesicular bodies and lysosomes (PubMed:25627919,
CC PubMed:21199866, PubMed:18279659). Localized on the limiting membrane
CC of early melanosomes of pigment cells (PubMed:29940187). Targeted to
CC the endolysosomal compartment (By similarity).
CC {ECO:0000250|UniProtKB:O70595, ECO:0000269|PubMed:18279659,
CC ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22655043,
CC ECO:0000269|PubMed:25627919, ECO:0000269|PubMed:29940187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP58-4; Sequence=VSP_021973;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression is detected in
CC the retinal epithelium (PubMed:10837493, PubMed:22226084). Expressed in
CC mature erythrocytes (PubMed:22655043). {ECO:0000269|PubMed:10837493,
CC ECO:0000269|PubMed:22226084, ECO:0000269|PubMed:22655043}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in fetal liver.
CC {ECO:0000269|PubMed:17006453}.
CC -!- INDUCTION: Up-regulated by cellular porphyrins (at protein level)
CC (PubMed:22655043, PubMed:17006453, PubMed:23180570). Up-regulated
CC during erythroid differentiation (at protein level) (PubMed:22655043).
CC Induced by sodium arsenite in a dose-dependent manner
CC (PubMed:21266531). {ECO:0000269|PubMed:17006453,
CC ECO:0000269|PubMed:21266531, ECO:0000269|PubMed:22655043,
CC ECO:0000269|PubMed:23180570}.
CC -!- DOMAIN: Contains two independently folding units, the N-terminal
CC transmembrane domain (residues 1-205) and the ABC-core domain (206-842)
CC are respectively responsible for the lysosomal targeting and the ATPase
CC activity. {ECO:0000269|PubMed:25627919}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18279659,
CC ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22655043,
CC ECO:0000269|PubMed:25627919}.
CC -!- POLYMORPHISM: Genetic variations in ABCB6 define the Langereis blood
CC group system (LAN) [MIM:111600]. Individuals with Lan(-) blood group
CC lack the Lan antigen on their red blood cells. These individuals may
CC have anti-Lan antibodies in their serum, which can cause transfusion
CC reactions or hemolytic disease of the fetus or newborn. The Lan(-)
CC blood group is only clinically significant in transfusion settings or
CC during pregnancy; otherwise Lan(-) individuals have no clinical
CC features. {ECO:0000269|PubMed:22246506}.
CC -!- DISEASE: Microphthalmia, isolated, with coloboma, 7 (MCOPCB7)
CC [MIM:614497]: A disorder of eye formation, ranging from small size of a
CC single eye to complete bilateral absence of ocular tissues. Ocular
CC abnormalities like opacities of the cornea and lens, scaring of the
CC retina and choroid, and other abnormalities may also be present. Ocular
CC colobomas are a set of malformations resulting from abnormal
CC morphogenesis of the optic cup and stalk, and the fusion of the fetal
CC fissure (optic fissure). {ECO:0000269|PubMed:22226084}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Dyschromatosis universalis hereditaria 3 (DUH3) [MIM:615402]:
CC An autosomal dominant pigmentary genodermatosis characterized by a
CC mixture of hyperpigmented and hypopigmented macules distributed
CC randomly over the body, that appear in infancy or early childhood. The
CC trunk and extremities are the dominant sites of abnormal pigmentation.
CC Facial lesions can be seen in 50% of affected individuals, but
CC involvement of palms and soles is unusual. Abnormalities of hair and
CC nails have also been reported. Dyschromatosis universalis hereditaria
CC may be associated with abnormalities of dermal connective tissue, nerve
CC tissue, or other systemic complications. {ECO:0000269|PubMed:23519333,
CC ECO:0000269|PubMed:24224009, ECO:0000269|PubMed:24498303,
CC ECO:0000269|PubMed:25288164, ECO:0000269|PubMed:29940187}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Pseudohyperkalemia, familial, 2, due to red cell leak (PSHK2)
CC [MIM:609153]: A dominantly inherited condition characterized by
CC increased serum potassium levels, measured in whole-blood specimens
CC stored at or below room temperature. This condition is not accompanied
CC by clinical symptoms or biological signs except for borderline
CC abnormalities of red cell shape. {ECO:0000269|PubMed:23180570,
CC ECO:0000269|PubMed:24947683}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in ABCB6 may be the cause of a severe porphyria.
CC Affected individuals show higher urinary porphyrin concentrations.
CC {ECO:0000269|PubMed:27507172}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
CC -!- CAUTION: To date, the intracellular localization of ABCB6 is a matter
CC of debate, with conflicting reports suggesting mitochondrial
CC (PubMed:10837493, PubMed:17006453 and PubMed:17661442) or endolysosomal
CC localization (PubMed:22655043, PubMed:25627919, PubMed:29940187,
CC PubMed:31053883), therefore questioning the requirement of ABCB6 in the
CC mitochondrial import of porphyrins. {ECO:0000269|PubMed:10837493,
CC ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442,
CC ECO:0000269|PubMed:22655043, ECO:0000269|PubMed:25627919,
CC ECO:0000269|PubMed:29940187, ECO:0000269|PubMed:31053883}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG33617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG33618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH43423.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAD18782.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92291.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=BAB71347.1; Type=Miscellaneous discrepancy; Note=splicing through aberrant splice sites.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AB039371; BAA96733.1; -; Genomic_DNA.
DR EMBL; AF076775; AAF75107.1; -; mRNA.
DR EMBL; AF308472; AAG33617.1; ALT_INIT; mRNA.
DR EMBL; AF308473; AAG33618.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ289233; CAB95766.2; -; mRNA.
DR EMBL; AK057026; BAB71347.1; ALT_SEQ; mRNA.
DR EMBL; AK172812; BAD18782.1; ALT_SEQ; mRNA.
DR EMBL; AB209054; BAD92291.1; ALT_SEQ; mRNA.
DR EMBL; BC000559; AAH00559.1; -; mRNA.
DR EMBL; BC043423; AAH43423.1; ALT_SEQ; mRNA.
DR EMBL; AF070598; AAC28653.1; -; mRNA.
DR CCDS; CCDS2436.1; -. [Q9NP58-1]
DR CCDS; CCDS86920.1; -. [Q9NP58-4]
DR RefSeq; NP_005680.1; NM_005689.2. [Q9NP58-1]
DR PDB; 3NH6; X-ray; 2.00 A; A=558-842.
DR PDB; 3NH9; X-ray; 2.10 A; A=558-842.
DR PDB; 3NHA; X-ray; 2.10 A; A=558-842.
DR PDB; 3NHB; X-ray; 2.15 A; A=558-842.
DR PDB; 7D7N; EM; 5.20 A; A/B=1-842.
DR PDB; 7D7R; EM; 4.00 A; A/B=1-842.
DR PDB; 7EKL; EM; 3.50 A; A/B=1-842.
DR PDB; 7EKM; EM; 3.60 A; A/B=1-842.
DR PDBsum; 3NH6; -.
DR PDBsum; 3NH9; -.
DR PDBsum; 3NHA; -.
DR PDBsum; 3NHB; -.
DR PDBsum; 7D7N; -.
DR PDBsum; 7D7R; -.
DR PDBsum; 7EKL; -.
DR PDBsum; 7EKM; -.
DR AlphaFoldDB; Q9NP58; -.
DR BMRB; Q9NP58; -.
DR SMR; Q9NP58; -.
DR BioGRID; 115369; 116.
DR IntAct; Q9NP58; 20.
DR MINT; Q9NP58; -.
DR STRING; 9606.ENSP00000265316; -.
DR BindingDB; Q9NP58; -.
DR ChEMBL; CHEMBL2007630; -.
DR TCDB; 3.A.1.210.6; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q9NP58; 1 site.
DR iPTMnet; Q9NP58; -.
DR PhosphoSitePlus; Q9NP58; -.
DR SwissPalm; Q9NP58; -.
DR BioMuta; ABCB6; -.
DR DMDM; 13123949; -.
DR EPD; Q9NP58; -.
DR jPOST; Q9NP58; -.
DR MassIVE; Q9NP58; -.
DR MaxQB; Q9NP58; -.
DR PaxDb; Q9NP58; -.
DR PeptideAtlas; Q9NP58; -.
DR PRIDE; Q9NP58; -.
DR ProteomicsDB; 81888; -. [Q9NP58-1]
DR ProteomicsDB; 81889; -. [Q9NP58-4]
DR Antibodypedia; 20133; 196 antibodies from 29 providers.
DR DNASU; 10058; -.
DR Ensembl; ENST00000265316.9; ENSP00000265316.3; ENSG00000115657.14. [Q9NP58-1]
DR Ensembl; ENST00000295750.5; ENSP00000295750.5; ENSG00000115657.14. [Q9NP58-4]
DR GeneID; 10058; -.
DR KEGG; hsa:10058; -.
DR MANE-Select; ENST00000265316.9; ENSP00000265316.3; NM_005689.4; NP_005680.1.
DR UCSC; uc002vkc.3; human. [Q9NP58-1]
DR CTD; 10058; -.
DR DisGeNET; 10058; -.
DR GeneCards; ABCB6; -.
DR HGNC; HGNC:47; ABCB6.
DR HPA; ENSG00000115657; Low tissue specificity.
DR MalaCards; ABCB6; -.
DR MIM; 111600; phenotype.
DR MIM; 605452; gene.
DR MIM; 609153; phenotype.
DR MIM; 614497; phenotype.
DR MIM; 615402; phenotype.
DR neXtProt; NX_Q9NP58; -.
DR OpenTargets; ENSG00000115657; -.
DR Orphanet; 98942; Coloboma of choroid and retina.
DR Orphanet; 98943; Coloboma of eye lens.
DR Orphanet; 98946; Coloboma of eyelid.
DR Orphanet; 98944; Coloboma of iris.
DR Orphanet; 98945; Coloboma of macula.
DR Orphanet; 98947; Coloboma of optic disc.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR Orphanet; 241; Dyschromatosis universalis hereditaria.
DR Orphanet; 90044; Familial pseudohyperkalemia.
DR PharmGKB; PA24388; -.
DR VEuPathDB; HostDB:ENSG00000115657; -.
DR eggNOG; KOG0056; Eukaryota.
DR GeneTree; ENSGT00940000156160; -.
DR InParanoid; Q9NP58; -.
DR OMA; TDPWVRP; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q9NP58; -.
DR TreeFam; TF105194; -.
DR PathwayCommons; Q9NP58; -.
DR Reactome; R-HSA-1369007; Mitochondrial ABC transporters.
DR Reactome; R-HSA-5683371; Defective ABCB6 causes MCOPCB7.
DR SignaLink; Q9NP58; -.
DR BioGRID-ORCS; 10058; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; ABCB6; human.
DR EvolutionaryTrace; Q9NP58; -.
DR GeneWiki; ABCB6; -.
DR GenomeRNAi; 10058; -.
DR Pharos; Q9NP58; Tbio.
DR PRO; PR:Q9NP58; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NP58; protein.
DR Bgee; ENSG00000115657; Expressed in right ovary and 94 other tissues.
DR ExpressionAtlas; Q9NP58; baseline and differential.
DR Genevisible; Q9NP58; HS.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015439; F:ABC-type heme transporter activity; IMP:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046906; F:tetrapyrrole binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB.
DR GO; GO:0042168; P:heme metabolic process; IDA:UniProtKB.
DR GO; GO:0035351; P:heme transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015886; P:heme transport; IDA:UniProtKB.
DR GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR GO; GO:0033013; P:tetrapyrrole metabolic process; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR032410; MTABC_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF16185; MTABC_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Disease variant; Disulfide bond; Dyskeratosis congenita;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Lysosome;
KW Membrane; Microphthalmia; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Secreted; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..842
FT /note="ATP-binding cassette sub-family B member 6"
FT /id="PRO_0000000248"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..106
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..185
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 285..291
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 313..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 397
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 419..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 521..529
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:18279659,
FT ECO:0000305|PubMed:21199866"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 551..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 265..556
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 590..824
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..236
FT /note="Required for ATPase activity"
FT /evidence="ECO:0000269|PubMed:33007128"
FT REGION 1..205
FT /note="Required for the lysosomal targeting"
FT /evidence="ECO:0000269|PubMed:25627919"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20823549,
FT ECO:0007744|PDB:3NH9"
FT BINDING 623..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20823549,
FT ECO:0007744|PDB:3NH9"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21199866"
FT DISULFID 8..26
FT /evidence="ECO:0000269|PubMed:21199866"
FT VAR_SEQ 183..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021973"
FT VARIANT 57
FT /note="A -> T (in MCOPCB7; unknown pathological
FT significance; hypomorphic mutation; dbSNP:rs387906911)"
FT /evidence="ECO:0000269|PubMed:22226084"
FT /id="VAR_067394"
FT VARIANT 69
FT /note="R -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035732"
FT VARIANT 170
FT /note="S -> G (in DUH3; the protein is retained in the
FT Golgi apparatus; dbSNP:rs397514757)"
FT /evidence="ECO:0000269|PubMed:23519333"
FT /id="VAR_070602"
FT VARIANT 192
FT /note="R -> Q (decrease expression; does not affect
FT susbtrate binding; does not affect ATP-binding; loss of
FT plasma membrane expression; dbSNP:rs150221689)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084494"
FT VARIANT 276
FT /note="R -> W (may be a modifier of disease severity in
FT porphyria patients; loss of expression; dbSNP:rs57467915)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084495"
FT VARIANT 293
FT /note="L -> V (in dbSNP:rs13018440)"
FT /id="VAR_047552"
FT VARIANT 322
FT /note="S -> R (in DUH3; dbSNP:rs1574815954)"
FT /evidence="ECO:0000269|PubMed:25288164"
FT /id="VAR_073973"
FT VARIANT 343
FT /note="R -> Q (in dbSNP:rs60322991)"
FT /id="VAR_060986"
FT VARIANT 356
FT /note="L -> P (in DUH3; the protein is retained in the
FT Golgi apparatus; dbSNP:rs397514756)"
FT /evidence="ECO:0000269|PubMed:23519333"
FT /id="VAR_070603"
FT VARIANT 375
FT /note="R -> Q (in PSHK2; dbSNP:rs754667801)"
FT /evidence="ECO:0000269|PubMed:23180570"
FT /id="VAR_071133"
FT VARIANT 375
FT /note="R -> W (in PSHK2; dbSNP:rs764893806)"
FT /evidence="ECO:0000269|PubMed:23180570"
FT /id="VAR_071134"
FT VARIANT 424
FT /note="Y -> H (in DUH3)"
FT /evidence="ECO:0000269|PubMed:25288164"
FT /id="VAR_073974"
FT VARIANT 453
FT /note="A -> V (in DUH3)"
FT /evidence="ECO:0000269|PubMed:24498303"
FT /id="VAR_071135"
FT VARIANT 492
FT /note="A -> T (may be a modifier of disease severity in
FT porphyria patients; increases expression; does not affect
FT susbtrate binding; impairs ATP-binding; Loss of ATP-
FT dependent coproporphyrin III transport; Highly decrease
FT plasma membrane expression; dbSNP:rs147445258)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084496"
FT VARIANT 521
FT /note="T -> S (may be a modifier of disease severity in
FT porphyria patients; loss of expression; dbSNP:rs149363094)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084497"
FT VARIANT 555
FT /note="Q -> K (in DUH3; dbSNP:rs796065353)"
FT /evidence="ECO:0000269|PubMed:24224009"
FT /id="VAR_071136"
FT VARIANT 579
FT /note="G -> E (in DUH3; the protein is retained in the
FT Golgi apparatus. Does not affect subcellular location in
FT early melanosome and lysosome. Does not rescue the normal
FT amyloid fibril formation and normal maturation of pigmented
FT melanosomes. Does not influence trafficking of melanosomal
FT proteins.; dbSNP:rs397514758)"
FT /evidence="ECO:0000269|PubMed:23519333,
FT ECO:0000269|PubMed:29940187"
FT /id="VAR_070604"
FT VARIANT 588
FT /note="G -> S (may be a modifier of disease severity in
FT porphyria patients; loss of expression; dbSNP:rs145526996)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084498"
FT VARIANT 648
FT /note="R -> Q (in dbSNP:rs13402964)"
FT /id="VAR_029749"
FT VARIANT 681
FT /note="A -> T (may be a modifier of disease severity in
FT porphyria patients; loss of expression; dbSNP:rs142421126)"
FT /evidence="ECO:0000269|PubMed:27507172"
FT /id="VAR_084499"
FT VARIANT 723
FT /note="R -> Q (in PSHK2; dbSNP:rs148211042)"
FT /evidence="ECO:0000269|PubMed:24947683"
FT /id="VAR_076206"
FT VARIANT 811
FT /note="L -> V (in MCOPCB7; hypomorphic mutation;
FT dbSNP:rs387906910)"
FT /evidence="ECO:0000269|PubMed:22226084"
FT /id="VAR_067395"
FT MUTAGEN 6
FT /note="N->Q: Loss of N-glycosylation. Loss of N-
FT glycosylation; when associated with Q-447; Q-498; Q-677 and
FT Q-775. Does not affect subtrate binding."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 8
FT /note="C->G: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 8
FT /note="C->S: Does not affect subtrate binding. Does not
FT affect N-glycosylation. Impairs endoplasmic reticulum exit.
FT Impairs endoplasmic reticulum exit; when associated with C-
FT 8. Increases ABCB6 proteasomal degradation. Affects protein
FT stability. Does not affect migration in the presence of
FT DTT; when associated with A-50 and A-120."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 26
FT /note="C->A: Decreases protein expression. Affects protein
FT stability. Loss of ability to stimulate porphyrin
FT synthesis."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 26
FT /note="C->S: Decreases protein expression. Impairs
FT endoplasmic reticulum exit; when associated with C-8.
FT Affects protein stability."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 50
FT /note="C->A: Increases migration in the absence of DTT;
FT when associated with A-120. Reduces migration in with the
FT presence of DTT; when associated with A-120."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 120
FT /note="C->A: Increases migration in the absence of DTT;
FT when associated with A-50. Reduces migration in with the
FT presence of DTT; when associated with A-50."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 286
FT /note="Y->A: Loss of substrate-stimulate ATPase activity.
FT Impairs protein expression."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 447
FT /note="N->Q: Does not affect N-glycosylation. Does not
FT affect N-glycosylation; when associated with Q-498; Q-677
FT and Q-775. Does not affect trafficking from endoplasmic
FT reticulum; when associated with Q-498; Q-677 and Q-775."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 498
FT /note="N->Q: Does not affect N-glycosylation. Does not
FT affect N-glycosylation; when associated with Q-447; Q-677
FT and Q-775. Does not affect trafficking from endoplasmic
FT reticulum; when associated with Q-447; Q-677 and Q-775."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 531
FT /note="V->A: Loss of substrate-stimulate ATPase activity.
FT Impairs protein expression."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 542
FT /note="M->A: Loss of substrate-stimulate ATPase activity."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 546
FT /note="W->A: Loss of substrate-stimulate ATPase activity.
FT Impairs protein expression."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 546
FT /note="W->F: Does not affect substrate-stimulate ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 546
FT /note="W->V: Loss of substrate-stimulate ATPase activity.
FT Impairs protein expression."
FT /evidence="ECO:0000269|PubMed:33007128"
FT MUTAGEN 629
FT /note="K->A: Abolishes ATP hydrolysis. Abolishes
FT coproporphyrin III transport."
FT /evidence="ECO:0000269|PubMed:23792964,
FT ECO:0000269|PubMed:25627919"
FT MUTAGEN 629
FT /note="K->M: Does not affect subcellular location in early
FT melanosome and lysosome. Does not rescue the normal amyloid
FT fibril formation and normal maturation of pigmented
FT melanosomes. Does not influence trafficking of melanosomal
FT proteins. Fails to rescue vacuolar sequestration of cadmium
FT in Schizosaccharomyces pombe and Caenorhabditis elegans
FT strains defective for HMT-1. Fails to rescue the cadmium
FT tolerance in Schizosaccharomyces pombe and Caenorhabditis
FT elegans strains defective for HMT-1. Does not rescue
FT vacuolar cadmium levels in hmt-1 mutant S. pombe."
FT /evidence="ECO:0000269|PubMed:29940187,
FT ECO:0000269|PubMed:31053883"
FT MUTAGEN 677
FT /note="N->Q: Does not affect N-glycosylation. Does not
FT affect N-glycosylation; when associated with Q-447; Q-498;
FT and Q-775. Does not affect trafficking from endoplasmic
FT reticulum; when associated with Q-447; Q-498; and Q-775."
FT /evidence="ECO:0000269|PubMed:21199866"
FT MUTAGEN 775
FT /note="N->Q: Does not affect N-glycosylation. Does not
FT affect N-glycosylation; when associated with Q-447; Q-498
FT and Q-677. Does not affect trafficking from endoplasmic
FT reticulum; when associated with Q-447; Q-498 and Q-677."
FT /evidence="ECO:0000269|PubMed:21199866"
FT CONFLICT 170
FT /note="S -> N (in Ref. 2; AAG33618)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="T -> S (in Ref. 4; BAD18782)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="F -> S (in Ref. 4; BAD18782)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="G -> E (in Ref. 4; BAD18782)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="R -> L (in Ref. 4; BAD18782)"
FT /evidence="ECO:0000305"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 265..294
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 299..316
FT /evidence="ECO:0007829|PDB:7EKL"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:7EKL"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 392..403
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 404..409
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 427..431
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 432..446
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 502..521
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 527..534
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 543..546
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 561..572
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 604..613
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 643..649
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 654..656
FT /evidence="ECO:0007829|PDB:3NH9"
FT HELIX 659..664
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 680..685
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 693..702
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 706..711
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:7EKL"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 729..743
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 746..751
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 753..757
FT /evidence="ECO:0007829|PDB:7EKL"
FT HELIX 759..773
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 785..789
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 792..798
FT /evidence="ECO:0007829|PDB:3NH6"
FT STRAND 801..806
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 808..814
FT /evidence="ECO:0007829|PDB:3NH6"
FT HELIX 817..826
FT /evidence="ECO:0007829|PDB:3NH6"
SQ SEQUENCE 842 AA; 93886 MW; E63A7D59DCE5B9ED CRC64;
MVTVGNYCEA EGPVGPAWMQ DGLSPCFFFT LVPSTRMALG TLALVLALPC RRRERPAGAD
SLSWGAGPRI SPYVLQLLLA TLQAALPLAG LAGRVGTARG APLPSYLLLA SVLESLAGAC
GLWLLVVERS QARQRLAMGI WIKFRHSPGL LLLWTVAFAA ENLALVSWNS PQWWWARADL
GQQVQFSLWV LRYVVSGGLF VLGLWAPGLR PQSYTLQVHE EDQDVERSQV RSAAQQSTWR
DFGRKLRLLS GYLWPRGSPA LQLVVLICLG LMGLERALNV LVPIFYRNIV NLLTEKAPWN
SLAWTVTSYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRRVELLIF SHLHELSLRW
HLGRRTGEVL RIADRGTSSV TGLLSYLVFN VIPTLADIII GIIYFSMFFN AWFGLIVFLC
MSLYLTLTIV VTEWRTKFRR AMNTQENATR ARAVDSLLNF ETVKYYNAES YEVERYREAI
IKYQGLEWKS SASLVLLNQT QNLVIGLGLL AGSLLCAYFV TEQKLQVGDY VLFGTYIIQL
YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDLPGA GPLRFQKGRI EFENVHFSYA
DGRETLQDVS FTVMPGQTLA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQA
SLRSHIGVVP QDTVLFNDTI ADNIRYGRVT AGNDEVEAAA QAAGIHDAIM AFPEGYRTQV
GERGLKLSGG EKQRVAIART ILKAPGIILL DEATSALDTS NERAIQASLA KVCANRTTIV
VAHRLSTVVN ADQILVIKDG CIVERGRHEA LLSRGGVYAD MWQLQQGQEE TSEDTKPQTM
ER
