MRP2_MOUSE
ID MRP2_MOUSE Reviewed; 1543 AA.
AC Q8VI47; Q8VI46;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-binding cassette sub-family C member 2;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q92887};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q92887};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:Q92887};
DE AltName: Full=Canalicular multispecific organic anion transporter 1 {ECO:0000305};
DE AltName: Full=Multidrug resistance-associated protein 2 {ECO:0000250|UniProtKB:Q92887};
GN Name=Abcc2 {ECO:0000312|MGI:MGI:1352447};
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].
RC STRAIN=AKR/J, and C57L/J;
RA Bouchard G., Chao H., Lammert F., Carey M.C., Paigen B.;
RT "Murine cholesterol cholelithiasis is linked to a mutation in the Abcc2
RT gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16421286; DOI=10.1124/jpet.105.098665;
RA Chu X.Y., Strauss J.R., Mariano M.A., Li J., Newton D.J., Cai X.,
RA Wang R.W., Yabut J., Hartley D.P., Evans D.C., Evers R.;
RT "Characterization of mice lacking the multidrug resistance protein MRP2
RT (ABCC2).";
RL J. Pharmacol. Exp. Ther. 317:579-589(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-876, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and 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: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that binds and hydrolyzes ATP to enable active transport of
CC various substrates including many drugs, toxicants and endogenous
CC compound across cell membranes. Transports a wide variety of conjugated
CC organic anions such as sulfate-, glucuronide- and glutathione (GSH)-
CC conjugates of endo- and xenobiotics substrates. Mediates hepatobiliary
CC excretion of mono- and bis-glucuronidated bilirubin molecules and
CC therefore play an important role in bilirubin detoxification. Mediates
CC also hepatobiliary excretion of others glucuronide conjugates such as
CC 17beta-estradiol 17-glucosiduronic acid and leukotriene C4. Transports
CC sulfated bile salt such as taurolithocholate sulfate. Transport various
CC anticancer drugs, such as anthracycline, vinca alkaloid and
CC methotrexate and HIV-drugs such as protease inhibitors.
CC {ECO:0000250|UniProtKB:Q92887}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) +
CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
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:Q92887};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-glucuronoside(in) + H2O = ADP + bilirubin-
CC glucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57767, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-bisglucuronoside(in) + H2O = ADP + bilirubin-
CC bisglucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58471, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q92887};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q92887}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:16421286}.
CC -!- DISRUPTION PHENOTYPE: These mice are healthy and show no phenotypic
CC abnormalities. Mice display hyperbilirubinemia and reduced levels of
CC biliary GSH. {ECO:0000269|PubMed:16421286}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AF282772; AAL36985.1; -; mRNA.
DR EMBL; AF282773; AAL36986.1; -; mRNA.
DR CCDS; CCDS29838.1; -.
DR RefSeq; NP_038834.2; NM_013806.2.
DR AlphaFoldDB; Q8VI47; -.
DR SMR; Q8VI47; -.
DR STRING; 10090.ENSMUSP00000026208; -.
DR ChEMBL; CHEMBL2073681; -.
DR GlyGen; Q8VI47; 4 sites.
DR iPTMnet; Q8VI47; -.
DR PhosphoSitePlus; Q8VI47; -.
DR SwissPalm; Q8VI47; -.
DR jPOST; Q8VI47; -.
DR MaxQB; Q8VI47; -.
DR PaxDb; Q8VI47; -.
DR PeptideAtlas; Q8VI47; -.
DR PRIDE; Q8VI47; -.
DR ProteomicsDB; 290323; -.
DR Antibodypedia; 17520; 375 antibodies from 39 providers.
DR DNASU; 12780; -.
DR Ensembl; ENSMUST00000026208; ENSMUSP00000026208; ENSMUSG00000025194.
DR GeneID; 12780; -.
DR KEGG; mmu:12780; -.
DR UCSC; uc008how.1; mouse.
DR CTD; 1244; -.
DR MGI; MGI:1352447; Abcc2.
DR VEuPathDB; HostDB:ENSMUSG00000025194; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161741; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q8VI47; -.
DR OMA; ICMATPV; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q8VI47; -.
DR TreeFam; TF105199; -.
DR BRENDA; 7.6.2.3; 3474.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 12780; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Abcc2; mouse.
DR PRO; PR:Q8VI47; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VI47; protein.
DR Bgee; ENSMUSG00000025194; Expressed in left lobe of liver and 44 other tissues.
DR ExpressionAtlas; Q8VI47; baseline and differential.
DR Genevisible; Q8VI47; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR GO; GO:0046691; C:intracellular canaliculus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISO:MGI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
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:0015127; F:bilirubin transmembrane transporter activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0016999; P:antibiotic metabolic process; ISO:MGI.
DR GO; GO:1901086; P:benzylpenicillin metabolic process; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR GO; GO:0015723; P:bilirubin transport; ISO:MGI.
DR GO; GO:0015722; P:canalicular bile acid transport; ISO:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:MGI.
DR GO; GO:0050787; P:detoxification of mercury ion; ISO:MGI.
DR GO; GO:0071716; P:leukotriene transport; ISO:MGI.
DR GO; GO:0015694; P:mercury ion transport; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR GO; GO:0015732; P:prostaglandin transport; ISO:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0070327; P:thyroid hormone transport; ISO:MGI.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISO:MGI.
DR GO; GO:0046618; P:xenobiotic export from cell; ISO:MGI.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:MGI.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:MGI.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR030247; ABCC2.
DR InterPro; IPR005292; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF176; PTHR24223:SF176; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Lipid transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1543
FT /note="ATP-binding cassette sub-family C member 2"
FT /id="PRO_0000093357"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 48..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 89..92
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 114..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 126..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 147..164
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 165..185
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 186..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..332
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 333..358
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 359..379
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 380..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 436..456
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 457..459
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 460..480
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 481..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 543..563
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 564..585
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 586..606
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 607..969
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 970..990
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 991..1031
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1032..1052
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1053..1095
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1096..1116
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1117
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1118..1138
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1139..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1210..1230
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1231..1232
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1233..1253
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1254..1543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 320..603
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 635..859
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 977..1262
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1298..1532
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 260..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 669..676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1332..1339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63120"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 613
FT /note="Q -> R (in Ref. 1; AAL36985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1543 AA; 173671 MW; 2D73F2881511FEC0 CRC64;
MDEFCNSTFW NLSLLKSPEA DLPLCFEQTV LVWIPLGFLW LLAPWQLYRI YRSRTKRFAI
TKFYLAKQVF VVCLLILAAI DLSLALTEDT GQATIPPVKY TNPILYLCTW LLVLVIQHCR
QCCIQKNSWF LSMFWILSLL CGIFQFQTLI RALLQDSKSN MTYSCLFFVS YGFQIVILIL
SAFSESSDST HAPSATASFL SSVTFSWYDS TVLKGYKHPL TIEDVWDIEE NLKAKSLTSK
FKTIMTKDLQ KARQALQRRL KKSQQSPEGT SHGLTKKQSQ SQDVLVLEDS KKKKKKSEAT
KDFPKSWLVK ALFKTFYVVI LKSFILKLAH DILLFLNPQL LKFLIGFVKD PDSYPWVGYI
YAILMFSVTL IQSFFLQCYF QFCFVLGMTV RTTIIASVYK KALTLSNLAR RQYTIGETVN
LMSVDSQKLM DVTNYIHLLW SSVLQIALSI FFLWRELGPS ILAGVGLMVL LVPVNGVLAT
KIRKIQVQNM KNKDKRLKIM NEILSGIKIL KYFAWEPSFK EQVNSIRKKE LRNLLRFSQL
QTILIFILHL TPTLVSVITF SVYVLVDSQN VLNAEKAFTS ITLFNILRFP LAMLPMVISS
VIQASVSVDR LEQYLGSDDL DLSAIRHVCH FDKAVQFSEA SFTWDRDLEA TIQDVNLDIK
PGQLVAVVGT VGSGKSSLIS AMLGEMENVH GHITIKGSIA YVPQQAWIQN GTIKDNILFG
SEYDEKKYQR VIEACALLPD LEMLPGGDMA EIGEKGINLS GGQKHRVSLA RATYQDADIY
ILDDPLSAVD THVGKHIFNK VVGPNGLLSG KTRILVTHGI HFLPQVDEIV VLGKGTILEK
GSYSDLMDKK GVFAKNWKTF MKHSGPEGEA TVDNDSEEED GDCGLIPTVE EIPDDAASLT
MRRENSLRRT LSRSSRSGSR RGKSLKSSLK IKSVNALNKK EEVVKGQKLI KKEFVETGKV
KFSIYLKYLQ AVGWWSLLFI VIFYVLNYVA FIGTNLWLSA WTSDSEKQNG TDNSPSQRDM
RIGVFGALGI AQGIFLLSSS LWSIYACRNA SKTLHRQLLT NILRAPMSFF DTTPTGRIVN
RFAGDISTVD DTLPQTLRSW LLCFFGIVST LVMICMATPI FIIIIIPLSI LYVSVQVFYV
ATSRQLRRLD SVTKSPIYSH FSETVSGLPV IRAFEHQQRF LANSEKQIDT NQKCVFSWIT
SNRWLAIRLE LVGNLIVFCS ALLLVIYKNS LTGDTVGFVL SNALNITQTL NWLVRMTSEV
ETNIVAVERI NEYINVDNEA PWVTDKKPPA DWPKKGEIQF NNYQVRYRPE LDLVLKGITC
NIKSTEKVGV VGRTGAGKSS LTNCLFRILE SAGGQIIIDG IDIASIGLHD LRGRLTIIPQ
DPILFSGNLR MNLDPFNKYS DEEIWRALEL AHLKSFVAGL QLGLLHEVTE GGDNLSIGQR
QLLCLGRAVL RKSKILVLDE ATAAVDLETD SLIQTTIRNE FSQCTVITIA HRLHTIMDSD
KIMVLDSGKI VEYGSPEELL SNMGPFYLMA KEAGIESVNH TEL
