ABCG2_PIG
ID ABCG2_PIG Reviewed; 656 AA.
AC Q8MIB3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Broad substrate specificity ATP-binding cassette transporter ABCG2 {ECO:0000305};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q9UNQ0};
DE AltName: Full=ATP-binding cassette sub-family G member 2;
DE AltName: Full=Brain multidrug resistance protein;
DE AltName: Full=Urate exporter;
DE AltName: CD_antigen=CD338;
GN Name=ABCG2; Synonyms=BMDP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12054514; DOI=10.1016/s0006-291x(02)00376-5;
RA Eisenblaetter T., Galla H.-J.;
RT "A new multidrug resistance protein at the blood-brain barrier.";
RL Biochem. Biophys. Res. Commun. 293:1273-1278(2002).
CC -!- FUNCTION: Broad substrate specificity ATP-dependent transporter of the
CC ATP-binding cassette (ABC) family that actively extrudes a wide variety
CC of physiological compounds, dietary toxins and xenobiotics from cells.
CC Involved in porphyrin homeostasis, mediating the export of
CC protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol
CC to extracellular space, it also functions in the cellular export of
CC heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a
CC urate exporter functioning in both renal and extrarenal urate excretion
CC (By similarity). In kidney, it also functions as a physiological
CC exporter of the uremic toxin indoxyl sulfate (By similarity). Also
CC involved in the excretion of steroids like estrone 3-sulfate/E1S,
CC 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates
CC (By similarity). Mediates the secretion of the riboflavin and biotin
CC vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin
CC catabolite of chlorophyll, reducing its bioavailability (By
CC similarity). Plays an important role in the exclusion of xenobiotics
CC from the brain (PubMed:12054514). It confers to cells a resistance to
CC multiple drugs and other xenobiotics including mitoxantrone,
CC pheophorbide, camptothecin, methotrexate, azidothymidine, and the
CC anthracyclines daunorubicin and doxorubicin, through the control of
CC their efflux (By similarity). In placenta, it limits the penetration of
CC drugs from the maternal plasma into the fetus. May play a role in early
CC stem cell self-renewal by blocking differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q7TMS5, ECO:0000250|UniProtKB:Q9UNQ0,
CC ECO:0000269|PubMed:12054514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out);
CC Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl
CC sulfate(out) + phosphate; Xref=Rhea:RHEA:61332, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:144643, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) +
CC phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-
CC sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP +
CC dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4-
CC methylumbelliferone sulfate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:61368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144581,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-
CC benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-
CC 2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-
CC glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61384,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:144584, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-
CC methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:61372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144582,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-
CC benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-
CC methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:61376, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:144583, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out)
CC + phosphate; Xref=Rhea:RHEA:61356, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50681, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate +
CC riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57986, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
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:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
CC -!- SUBUNIT: Homodimer; disulfide-linked. The minimal functional unit is a
CC homodimer, but the major oligomeric form in plasma membrane is a
CC homotetramer with possibility of higher order oligomerization up to
CC homododecamers. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UNQ0};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9UNQ0}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UNQ0};
CC Multi-pass membrane protein {ECO:0000255}. Note=Enriched in membrane
CC lipid rafts. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- TISSUE SPECIFICITY: High expression in brain, kidney and lung. Also
CC expressed in livere, colon, small intestine, heart, skeletal muscle,
CC spleen, stomach and pancreas. {ECO:0000269|PubMed:12054514}.
CC -!- DOMAIN: The extracellular loop 3 (ECL3) is involved in binding
CC porphyrins and transfer them to other carriers, probably albumin.
CC {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- PTM: N-glycosylated. Glycosylation-deficient ABCG2 is normally
CC expressed and functional. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- PTM: Phosphorylated. Phosphorylation may regulate the localization to
CC the plasma membrane, the homooligomerization and therefore, the
CC activity of the transporter. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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; AJ420927; CAD12785.1; -; mRNA.
DR PIR; JC7860; JC7860.
DR RefSeq; NP_999175.1; NM_214010.1.
DR AlphaFoldDB; Q8MIB3; -.
DR SMR; Q8MIB3; -.
DR STRING; 9823.ENSSSCP00000028560; -.
DR PaxDb; Q8MIB3; -.
DR PeptideAtlas; Q8MIB3; -.
DR PRIDE; Q8MIB3; -.
DR Ensembl; ENSSSCT00000010088; ENSSSCP00000009822; ENSSSCG00000009215.
DR Ensembl; ENSSSCT00000033654; ENSSSCP00000029272; ENSSSCG00000009215.
DR Ensembl; ENSSSCT00000034970; ENSSSCP00000029787; ENSSSCG00000009215.
DR Ensembl; ENSSSCT00000045622; ENSSSCP00000051895; ENSSSCG00000009215.
DR Ensembl; ENSSSCT00000049571; ENSSSCP00000055593; ENSSSCG00000009215.
DR Ensembl; ENSSSCT00070029011; ENSSSCP00070024187; ENSSSCG00070014755.
DR GeneID; 397073; -.
DR KEGG; ssc:397073; -.
DR CTD; 9429; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000162658; -.
DR InParanoid; Q8MIB3; -.
DR OrthoDB; 1022017at2759; -.
DR ChiTaRS; ABCG2; pig.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Chromosome 8.
DR Bgee; ENSSSCG00000009215; Expressed in ileum and 41 other tissues.
DR ExpressionAtlas; Q8MIB3; baseline.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015878; P:biotin transport; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0097744; P:renal urate salt excretion; ISS:UniProtKB.
DR GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR030256; ABCG2.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48041:SF92; PTHR48041:SF92; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Lipid transport;
KW Membrane; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..656
FT /note="Broad substrate specificity ATP-binding cassette
FT transporter ABCG2"
FT /id="PRO_0000093389"
FT TOPO_DOM 1..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..631
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..286
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 390..652
FT /note="ABC transmembrane type-2"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 184..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 593..609
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT DISULFID 604
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
SQ SEQUENCE 656 AA; 72392 MW; 118ADD5B53D9D67F CRC64;
MSSNSYQVSI PMSKRNTNGL PGSSSNELKT SAGGAVLSFH DICYRVKVKS GFLFCRKTVE
KEILTNINGI MKPGLNAILG PTGGGKSSLL DVLAARKDPH GLSGDVLING APRPANFKCN
SGYVVQDDVV MGTLTVRENL QFSAALRLPT TMTNHEKNER INMVIQELGL DKVADSKVGT
QFIRGVSGGE RKRTSIAMEL ITDPSILFLD EPTTGLDSST ANAVLLLLKR MSKQGRTIIF
SIHQPRYSIF KLFDSLTLLA SGRLMFHGPA REALGYFASI GYNCEPYNNP ADFFLDVING
DSSAVVLSRA DRDEGAQEPE EPPEKDTPLI DKLAAFYTNS SFFKDTKVEL DQFSGGRKKK
KSSVYKEVTY TTSFCHQLRW ISRRSFKNLL GNPQASVAQI IVTIILGLVI GAIFYDLKND
PSGIQNRAGV LFFLTTNQCF SSVSAVELLV VEKKLFIHEY ISGYYRVSSY FFGKLLSDLL
PMRMLPSIIF TCITYFLLGL KPAVGSFFIM MFTLMMVAYS ASSMALAIAA GQSVVSVATL
LMTISFVFMM IFSGLLVNLK TVVPWLSWLQ YFSIPRYGFS ALQYNEFLGQ NFCPGLNVTT
NNTCSFAICT GAEYLENQGI SLSAWGLWQN HVALACMMVI FLTIAYLKLL LLKKYS
