ID ABCB6_RAT Reviewed; 836 AA.
AC O70595;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000305};
DE AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000250|UniProtKB:Q9NP58};
DE EC=7.6.2.5 {ECO:0000250|UniProtKB:Q9NP58};
DE AltName: Full=Ubiquitously-expressed mammalian ABC half transporter;
GN Name=Abcb6 {ECO:0000312|RGD:71077}; Synonyms=Umat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Hepatocyte;
RX PubMed=9705847; DOI=10.1006/bbrc.1998.9110;
RA Hirsch-Ernst K.I., Gaini-Rahimi S., Ernst B.-P., Schmitz-Salue C.,
RA Blume S., Kahl G.F.;
RT "Molecular cDNA cloning and tissue distribution of mRNA encoding a novel
RT ATP-binding cassette (ABC) half-transporter.";
RL Biochem. Biophys. Res. Commun. 249:151-155(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=16390497; DOI=10.1111/j.1365-2605.2005.00616.x;
RA Melaine N., Satie A.-P., Lassurguere J., Desmots S., Jegou B., Samson M.;
RT "Molecular cloning of several rat ABC transporters including a new ABC
RT transporter, Abcb8, and their expression in rat testis.";
RL Int. J. Androl. 29:392-399(2006).
RN [4]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18160489; DOI=10.1152/ajpcell.00612.2006;
RA Jalil Y.A., Ritz V., Jakimenko A., Schmitz-Salue C., Siebert H., Awuah D.,
RA Kotthaus A., Kietzmann T., Ziemann C., Hirsch-Ernst K.I.;
RT "Vesicular localization of the rat ATP-binding cassette half-transporter
RT rAbcb6.";
RL Am. J. Physiol. 294:C579-C590(2008).
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 (By
CC similarity). May also function as an ATP-dependent importer of
CC porphyrins from the cytoplasm into the mitochondria, in turn may
CC participate in the de novo heme biosynthesis regulation and in the
CC coordination of heme and iron homeostasis during phenylhydrazine stress
CC (By similarity). May play a key role in the early steps of
CC melanogenesis producing PMEL amyloid fibrils (By similarity). In vitro,
CC it confers to cells a resistance to toxic metal such as arsenic and
CC cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-
CC 38 and vincristin (By similarity). In addition may play a role in the
CC transition metal homeostasis (PubMed:18160489).
CC {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NP58}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18160489}. Late
CC endosome membrane {ECO:0000269|PubMed:18160489}. Early endosome
CC membrane {ECO:0000269|PubMed:18160489}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:Q9NP58}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature
CC erythrocytes and in exosomes released from reticulocytes during the
CC final steps of erythroid maturation. Traffics from endoplasmic
CC reticulum to Golgi during its glycans's maturation, therefrom is first
CC targeted to the plasma membrane, and is rapidly internalized through
CC endocytosis to be distributed to the limiting membrane of
CC multivesicular bodies and lysosomes. Localized on the limiting membrane
CC of early melanosomes of pigment cells (By similarity). Targeted to the
CC endolysosomal compartment (PubMed:18160489).
CC {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis
CC by meiotic pachytene spermatocytes and post-meiotic early spermatids.
CC {ECO:0000269|PubMed:16390497, ECO:0000269|PubMed:9705847}.
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:0000250|UniProtKB:Q9NP58}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18160489}.
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 or
CC endolysosomal localization, therefore questioning the requirement of
CC ABCB6 in the mitochondrial import of porphyrins.
CC {ECO:0000250|UniProtKB:Q9NP58}.
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DR EMBL; AJ003004; CAA05793.1; -; mRNA.
DR EMBL; BC085712; AAH85712.1; -; mRNA.
DR PIR; JE0248; JE0248.
DR RefSeq; NP_542149.1; NM_080582.1.
DR AlphaFoldDB; O70595; -.
DR SMR; O70595; -.
DR STRING; 10116.ENSRNOP00000025627; -.
DR PhosphoSitePlus; O70595; -.
DR SwissPalm; O70595; -.
DR jPOST; O70595; -.
DR PaxDb; 10116-ENSRNOP00000025627; -.
DR Ensembl; ENSRNOT00000025627.7; ENSRNOP00000025627.3; ENSRNOG00000018697.8.
DR Ensembl; ENSRNOT00055017619; ENSRNOP00055014181; ENSRNOG00055010412.
DR Ensembl; ENSRNOT00060012860; ENSRNOP00060009740; ENSRNOG00060007794.
DR Ensembl; ENSRNOT00065014142; ENSRNOP00065010578; ENSRNOG00065008855.
DR GeneID; 140669; -.
DR KEGG; rno:140669; -.
DR UCSC; RGD:71077; rat.
DR AGR; RGD:71077; -.
DR CTD; 10058; -.
DR RGD; 71077; Abcb6.
DR eggNOG; KOG0056; Eukaryota.
DR GeneTree; ENSGT00940000156160; -.
DR HOGENOM; CLU_000604_32_0_1; -.
DR InParanoid; O70595; -.
DR OMA; YYGAEHY; -.
DR OrthoDB; 2876209at2759; -.
DR PhylomeDB; O70595; -.
DR TreeFam; TF105194; -.
DR Reactome; R-RNO-1369007; Mitochondrial ABC transporters.
DR PRO; PR:O70595; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018697; Expressed in pancreas and 19 other cell types or tissues.
DR ExpressionAtlas; O70595; baseline and differential.
DR Genevisible; O70595; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0005740; C:mitochondrial envelope; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0032585; C:multivesicular body membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015439; F:ABC-type heme transporter activity; ISO:RGD.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0046906; F:tetrapyrrole binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; ISS:UniProtKB.
DR GO; GO:0042168; P:heme metabolic process; ISS:UniProtKB.
DR GO; GO:0035351; P:heme transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015886; P:heme transport; ISO:RGD.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; IDA:UniProtKB.
DR GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISO:RGD.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0033013; P:tetrapyrrole metabolic process; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18581; ABC_6TM_ABCB6; 1.
DR CDD; cd03253; ABCC_ATM1_transporter; 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; IPR032410; MTABC_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF586; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 6; 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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Golgi apparatus; Lysosome; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Secreted; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..836
FT /note="ATP-binding cassette sub-family B member 6"
FT /id="PRO_0000268679"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
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:0000250|UniProtKB:Q9NP58"
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:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 286..305
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 327..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:0000250|UniProtKB:Q9NP58"
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:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 551..836
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:0000250|UniProtKB:Q9NP58"
FT REGION 1..205
FT /note="Required for the lysosomal targeting"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 623..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DISULFID 8..26
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
SQ SEQUENCE 836 AA; 93305 MW; 40EC2C32E865522B CRC64;
MVTVGNYCEA EGPAGPAWTQ NGLSPCFFYT LVPSTLMTLG VLALVLVLPC RRREVPAGTE
ELSWAAGPRV APYALQLSLA ILQMALPLAS LAGRVGTARG VRLPGYLLLA SVLESLASAC
GLWLLVVERS QARQSLAMGV WMKFRHSLGL LLLWTVTFAA ENLVLVSWNS PQWWWSRADL
GQQVQFGLWV LRYMTSGGLF ILGLWAPGLR PQSYTLHVNE EDQDGGRNQG RSTDPRSTWR
DLGRKLRLLS GYLWPRGSPS LQLTVLLCMG LMGLDRALNV LVPIFYRDIV NLLTSKAPWS
SLAWTVTTYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRGVELRLF SHLHELSLRW
HLGRRTGEVL RIVDRGTSSV TGLLSYLVFN IIPTLADIII GIIYFSMFFN AWFGLIVFLC
MSLYLILTIM VTEWRAKFRR DMNTQENATR ARAVDSLLNF ETVKYYNAEG YELERYREAI
LKFQGLEWKS TASLVLLNQT QNMVIGFGLL AGSLLCAYFV SERRLQVGDF VLFGTYITQL
YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDVPGA GPLRFHKGRV EFENVHFSYA
DGRETLQDVS FTVMPGQTVA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQI
SLRSHIGVVP QDTVLFNDTI ANNIRYGRVT AGDSEIQAAA QAAGIHDAIL SFPEGYETQV
GERGLKLSGG EKQRVAIART ILKAPDIILL DEATSALDTS NERAIQASLA KVCTNRTTIV
VAHRLSTVVN ADQILVIKDG CIIERGRHEA LLSRGGVYAE MWQLQQQGQE TVPEDS
//
