ID   ATP7B_MOUSE             Reviewed;        1462 AA.
AC   Q64446; B1AQ56;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Copper-transporting ATPase 2;
DE            EC=7.2.2.8 {ECO:0000250|UniProtKB:P35670};
DE   AltName: Full=Copper pump 2;
DE   AltName: Full=Wilson disease-associated protein homolog;
GN   Name=Atp7b; Synonyms=Wnd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN TX PHENOTYPE.
RC   STRAIN=DAT; TISSUE=Liver;
RX   PubMed=8894697; DOI=10.1093/hmg/5.10.1619;
RA   Theophilos M.B., Cox D.W., Mercer J.F.B.;
RT   "The toxic milk mouse is a murine model of Wilson disease.";
RL   Hum. Mol. Genet. 5:1619-1624(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Copper ion transmembrane transporter involved in the export
CC       of copper out of the cells, such as the efflux of hepatic copper into
CC       the bile. {ECO:0000250|UniProtKB:P35670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P35670};
CC   -!- SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (By similarity).
CC       Interacts with DCTN4, in a copper-dependent manner (By similarity).
CC       Interacts with ATOX1 (By similarity). Interacts (via C-terminus) with
CC       ZBTB16/PLZF (By similarity). {ECO:0000250|UniProtKB:P35670}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:P35670}; Multi-pass membrane protein
CC       {ECO:0000255}. Late endosome {ECO:0000250|UniProtKB:P35670}.
CC       Note=Predominantly found in the trans-Golgi network (TGN). Not
CC       redistributed to the plasma membrane in response to elevated copper
CC       levels. {ECO:0000250|UniProtKB:P35670}.
CC   -!- TISSUE SPECIFICITY: Detected in liver and kidney.
CC   -!- DOMAIN: Each HMA domain can bind a copper ion, they are tightly packed
CC       and closely interact with each other. Wild-type ATP7B can usually be
CC       loaded with an average 5.5 copper atoms per molecule (By similarity).
CC       {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in Atp7b are the cause of the toxic milk mouse
CC       mutant (tx) phenotype, characterized by accumulation of copper in the
CC       liver in a manner similar to that observed in patients with Wilson
CC       disease. {ECO:0000269|PubMed:8894697}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; U38477; AAC52852.1; -; mRNA.
DR   EMBL; AC163439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466580; EDL32910.1; -; Genomic_DNA.
DR   CCDS; CCDS22168.1; -.
DR   RefSeq; NP_031537.2; NM_007511.2.
DR   AlphaFoldDB; Q64446; -.
DR   SMR; Q64446; -.
DR   BioGRID; 198269; 4.
DR   STRING; 10090.ENSMUSP00000006742; -.
DR   iPTMnet; Q64446; -.
DR   PhosphoSitePlus; Q64446; -.
DR   MaxQB; Q64446; -.
DR   PaxDb; 10090-ENSMUSP00000006742; -.
DR   ProteomicsDB; 277215; -.
DR   Antibodypedia; 2396; 572 antibodies from 37 providers.
DR   DNASU; 11979; -.
DR   Ensembl; ENSMUST00000006742.11; ENSMUSP00000006742.5; ENSMUSG00000006567.12.
DR   GeneID; 11979; -.
DR   KEGG; mmu:11979; -.
DR   UCSC; uc009lck.1; mouse.
DR   AGR; MGI:103297; -.
DR   CTD; 540; -.
DR   MGI; MGI:103297; Atp7b.
DR   VEuPathDB; HostDB:ENSMUSG00000006567; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   GeneTree; ENSGT00940000155749; -.
DR   InParanoid; Q64446; -.
DR   OMA; MVCPRIH; -.
DR   OrthoDB; 5480493at2759; -.
DR   PhylomeDB; Q64446; -.
DR   TreeFam; TF300460; -.
DR   BRENDA; 7.2.2.8; 3474.
DR   BRENDA; 7.2.2.9; 3474.
DR   Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 11979; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q64446; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q64446; Protein.
DR   Bgee; ENSMUSG00000006567; Expressed in yolk sac and 96 other cell types or tissues.
DR   ExpressionAtlas; Q64446; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; ISS:HGNC.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0070160; C:tight junction; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:HGNC-UCL.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; ISS:HGNC-UCL.
DR   GO; GO:0005375; F:copper ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IDA:MGI.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0071280; P:cellular response to copper ion; ISO:MGI.
DR   GO; GO:0060003; P:copper ion export; ISO:MGI.
DR   GO; GO:0015677; P:copper ion import; ISO:MGI.
DR   GO; GO:0006825; P:copper ion transport; IDA:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0006878; P:intracellular copper ion homeostasis; IMP:MGI.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0015680; P:protein maturation by copper ion transfer; IMP:MGI.
DR   GO; GO:0046688; P:response to copper ion; ISO:MGI.
DR   GO; GO:0051208; P:sequestering of calcium ion; ISO:MGI.
DR   CDD; cd00371; HMA; 6.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 6.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   NCBIfam; TIGR00003; copper ion binding protein; 5.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 6.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00942; CUATPASEI.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 6.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 5.
DR   PROSITE; PS50846; HMA_2; 6.
DR   Genevisible; Q64446; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Copper; Copper transport; Disease variant; Endosome;
KW   Golgi apparatus; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1462
FT                   /note="Copper-transporting ATPase 2"
FT                   /id="PRO_0000046315"
FT   TOPO_DOM        1..655
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        656..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        678..699
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        700..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        720..726
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        748..766
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        767..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        788..921
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        922..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        945..974
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        975..996
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        997..1319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1320..1337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1338..1348
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1349..1368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1369..1462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          68..134
FT                   /note="HMA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          153..219
FT                   /note="HMA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          267..333
FT                   /note="HMA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          361..427
FT                   /note="HMA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          490..556
FT                   /note="HMA 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          566..632
FT                   /note="HMA 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1029
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         82
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         164
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         167
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         278
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         281
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         372
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000305"
FT   BINDING         501
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         504
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         577
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         580
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         1264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         1268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64535"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64535"
FT   MOD_RES         1395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64535"
FT   MOD_RES         1454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64535"
FT   VARIANT         1356
FT                   /note="M -> V (in tx mice)"
FT   CONFLICT        107..108
FT                   /note="SA -> KH (in Ref. 1; AAC52852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1462 AA;  157190 MW;  BEC219F80EB74214 CRC64;
     MDPRKNLASV GTMPEQERQV TAKEASRKIL SKLALPGRPW EQSMKQSFAF DNVGYEGGLD
     STSSSPAATD VVNILGMTCH SCVKSIEDRI SSLKGIVNIK VSLEQGSATV RYVPSVMNLQ
     QICLQIEDMG FEASAAEGKA ASWPSRSSPA QEAVVKLRVE GMTCQSCVSS IEGKIRKLQG
     VVRIKVSLSN QEAVITYQPY LIQPEDLRDH ICDMGFEAAI KNRTAPLRLG PIDVNKLEST
     NLKKETVSPV QISNHFETLG HQGSYLATLP LRIDGMHCKS CVLNIEGNIG QLPGVQNIHV
     SLENKTAQIQ YDPSCVTPMF LQTAIEALPP GHFKVSLPDG VEENEPQSGS SQRHQEQGPG
     RTAVLTISGI TCASSVQPIE DMLSQRKGVQ QTSISLAEGT GAVLYDPSIV SLDELRTAVE
     DMGFEVSVNS ETFTINPVRN FKSGNSVPQT MGDIAGSVQK MAPDTRGLPT HQGPGHSSET
     PSSPGATASQ KCFVQIKGMT CASCVSNIER SLQRHAGILS VLVALMSGKA EVKYDPEIIQ
     SPRIAQLIQD LGFEASVMED NTVSEGDIEL IITGMTCASC VHNIESKLTR TNGITYASVA
     LATSKAHVKF DPEIVGPRDI IKIIEEIGFH ASLAQRNPNA HHLDHKTEIK QWKKSFLCSL
     VFGIPVMGLM VYMLIPSSTP QETMVLDHNI IPGLSVLNLI FFILCTFVQF LGGWYFYVQA
     YKSLRHRSAN MDVLIVLATT IAYAYSLVIL VVAVAEKAEK SPVTFFDTPP MLFVFIALGR
     WLEHVAKSKT SEALAKLMSL QATEATVVTL GEDNLILREE QVPMELVQRG DVIKVVPGGK
     FPVDGKVLEG NTMADESLIT GEAMPVTKKP GSIVIAGSIN AHGSVLLKAT HVGNDTTLAQ
     IVKLVEEAQM SKAPIQQLAD RFSGYFVPFI IIISTLTLVV WIVIGFVDFG VVQKYFPSPS
     KHISQTEVII RFAFQTSITV LCIACPCSLG LATPTAVMVG TGVAAQNGVL IKGGKPLEMA
     HKIKTVMFDK TGTITHGVPR VMRFLLLADV ATLPLRKVLA VVGTAEASSE HPLGVAVTKY
     CKEELGTETL GYSTDFQAVP GCGISCKVSN VEGILARSDL TAHPVGVGNP PTGEGAGPQT
     FSVLIGNREW MRRNGLTISS DISDAMTDHE MKGQTAILVA IDGVLCGMIA IADAVKPEAA
     LAIYTLKSMG VDVALITGDN RKTARAIATQ VGINKVFAEV LPSHKVAKVQ ELQNEGKKVA
     MVGDGVNDSP ALAQADVGIA IGTGTDVAIE AADVVLIRND LLDVVASIHL SKRTVRRIRV
     NLVLALIYNM VGIPIAAGVF MPIGIVLQPW MGSAAMAASS VSVVLSSLQL KCYRKPDLER
     YEAQAHGRMK PLSASQVSVH IGMDDRRRDS PRATAWDQVS YVSQVSLSSL TSDRLSRHGG
     AAEDGGDKWS LLLSDRDEEQ CI
//