AB1C_ARATH
ID AB1C_ARATH Reviewed; 1622 AA.
AC Q9C8G9; O24635; Q8RX76; Q9SAQ1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ABC transporter C family member 1;
DE Short=ABC transporter ABCC.1;
DE Short=AtABCC1;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump 1;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase 1;
DE AltName: Full=Multidrug resistance-associated protein 1;
GN Name=ABCC1; Synonyms=EST1, MRP1; OrderedLocusNames=At1g30400;
GN ORFNames=T4K22.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9223346; DOI=10.1073/pnas.94.15.8243;
RA Lu Y.-P., Li Z.-S., Rea P.A.;
RT "AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump:
RT isolation and functional definition of a plant ATP-binding cassette
RT transporter gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8243-8248(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1622.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1390-1486.
RX PubMed=9271206; DOI=10.1016/s0014-5793(97)00702-3;
RA Tommasini R., Vogt E., Schmid J., Fromentau M., Amrhein N., Martinoia E.;
RT "Differential expression of genes coding for ABC transporters after
RT treatment of Arabidopsis thaliana with xenobiotics.";
RL FEBS Lett. 411:206-210(1997).
RN [6]
RP INDUCTION.
RX PubMed=9671034; DOI=10.1007/s004380050779;
RA Sanchez-Fernandez R., Ardiles-Diaz W., Van Montagu M., Inze D., May M.J.;
RT "Cloning and expression analyses of the AtMRP4, a novel MRP-like gene from
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 258:655-662(1998).
RN [7]
RP TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9490749; DOI=10.2307/3870704;
RA Lu Y.-P., Li Z.-S., Drozdowicz Y.M., Hoertensteiner S., Martinoia E.,
RA Rea P.A.;
RT "AtMRP2, an Arabidopsis ATP-binding cassette transporter able to transport
RT glutathione S-conjugates and chlorophyll catabolites: functional
RT comparisons with AtMRP1.";
RL Plant Cell 10:267-282(1998).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [9]
RP GENE FAMILY.
RX PubMed=11855639; DOI=10.1007/s004250100661;
RA Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT "Multifunctionality of plant ABC transporters -- more than just
RT detoxifiers.";
RL Planta 214:345-355(2002).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA Martinoia E., Schulz B.;
RT "Family business: the multidrug-resistance related protein (MRP) ABC
RT transporter genes in Arabidopsis thaliana.";
RL Planta 216:107-119(2002).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PAS1;
RP CALMODULIN AND FKBP42/TWD1.
RX PubMed=15133126; DOI=10.1091/mbc.e03-11-0831;
RA Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
RA Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
RA Martinoia E.;
RT "Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar
RT ABC transporters.";
RL Mol. Biol. Cell 15:3393-3405(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [13]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
CC -!- FUNCTION: Pump for glutathione S-conjugates. Mediates the transport of
CC S-(2,4-dinitrophenyl)-glutathione (DNP-GS), GSSG, cyanidin 3-glucoside-
CC GS (C3G-GS) and metolachlor-GS (MOC-GS). {ECO:0000269|PubMed:9223346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for DNP-GS (at pH 8) {ECO:0000269|PubMed:9490749};
CC KM=220 uM for GSSG (at pH 8) {ECO:0000269|PubMed:9490749};
CC KM=60 uM for MOC-GS (at pH 8) {ECO:0000269|PubMed:9490749};
CC Vmax=0.82 nmol/min/mg enzyme with DNP-GS as substrate (at pH 8)
CC {ECO:0000269|PubMed:9490749};
CC Vmax=0.68 nmol/min/mg enzyme with GSSG as substrate (at pH 8)
CC {ECO:0000269|PubMed:9490749};
CC Vmax=1.75 nmol/min/mg enzyme with MOC-GS as substrate (at pH 8)
CC {ECO:0000269|PubMed:9490749};
CC Vmax=0.79 nmol/min/mg enzyme with C3G-GS as substrate (at pH 8)
CC {ECO:0000269|PubMed:9490749};
CC -!- SUBUNIT: Interacts with calmodulin (CaM), PAS1 and FKBP42/TWD1.
CC {ECO:0000269|PubMed:15133126}.
CC -!- INTERACTION:
CC Q9C8G9; Q9LDC0: FKBP42; NbExp=4; IntAct=EBI-637633, EBI-360006;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15133126,
CC ECO:0000269|PubMed:17151019}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15133126}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in leaves and stems
CC and lower levels in roots. Localized in the root apex, root hair tips
CC and root epidermis. {ECO:0000269|PubMed:12430019,
CC ECO:0000269|PubMed:15133126, ECO:0000269|PubMed:9223346,
CC ECO:0000269|PubMed:9490749}.
CC -!- INDUCTION: Slightly induced by benoxacor, cloquintocet, fenchlorazol
CC and fluorazol. {ECO:0000269|PubMed:9671034}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF008124; AAB67319.1; -; mRNA.
DR EMBL; AF008125; AAB71832.1; -; Genomic_DNA.
DR EMBL; AC025295; AAG51096.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31212.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31213.1; -; Genomic_DNA.
DR EMBL; AY090258; AAL90919.1; ALT_INIT; mRNA.
DR EMBL; U96398; AAC49796.1; -; mRNA.
DR PIR; D86428; D86428.
DR RefSeq; NP_001031116.1; NM_001036039.2.
DR RefSeq; NP_174329.1; NM_102777.3.
DR AlphaFoldDB; Q9C8G9; -.
DR SMR; Q9C8G9; -.
DR BioGRID; 25155; 1.
DR IntAct; Q9C8G9; 2.
DR STRING; 3702.AT1G30400.2; -.
DR TCDB; 3.A.1.208.20; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9C8G9; -.
DR PaxDb; Q9C8G9; -.
DR PRIDE; Q9C8G9; -.
DR ProteomicsDB; 245099; -.
DR EnsemblPlants; AT1G30400.1; AT1G30400.1; AT1G30400.
DR EnsemblPlants; AT1G30400.2; AT1G30400.2; AT1G30400.
DR GeneID; 839920; -.
DR Gramene; AT1G30400.1; AT1G30400.1; AT1G30400.
DR Gramene; AT1G30400.2; AT1G30400.2; AT1G30400.
DR KEGG; ath:AT1G30400; -.
DR Araport; AT1G30400; -.
DR TAIR; locus:2204202; AT1G30400.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_2_1; -.
DR InParanoid; Q9C8G9; -.
DR OMA; IRYDFTP; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q9C8G9; -.
DR BioCyc; ARA:AT1G30400-MON; -.
DR BioCyc; MetaCyc:AT1G30400-MON; -.
DR BRENDA; 7.6.2.3; 399.
DR PRO; PR:Q9C8G9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8G9; baseline and differential.
DR Genevisible; Q9C8G9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:1902417; F:(+)-abscisic acid D-glucopyranosyl ester transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0044604; F:ABC-type phytochelatin transporter activity; IDA:TAIR.
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:0015446; F:ATPase-coupled arsenite transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:1902418; P:(+)-abscisic acid D-glucopyranosyl ester transmembrane transport; IDA:TAIR.
DR GO; GO:0015700; P:arsenite transport; IDA:TAIR.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
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 PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1622
FT /note="ABC transporter C family member 1"
FT /id="PRO_0000226072"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1027..1049
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1053..1072
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 302..582
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 614..838
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 916..1200
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1237..1471
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 852..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1246
FT /note="Interaction with calmodulin and FKP42/TWD1"
FT COMPBIAS 859..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1271..1278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 765
FT /note="D -> E (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="Q -> P (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="D -> H (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="S -> I (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="L -> W (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
FT CONFLICT 1314
FT /note="L -> V (in Ref. 1; AAB67319/AAB71832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1622 AA; 181927 MW; B71E085798F1BBD6 CRC64;
MGFEPLDWYC KPVPNGVWTK TVDYAFGAYT PCAIDSFVLG ISHLVLLILC LYRLWLITKD
HKVDKFCLRS KWFSYFLALL AAYATAEPLF RLVMRISVLD LDGAGFPPYE AFMLVLEAFA
WGSALVMTVV ETKTYIHELR WYVRFAVIYA LVGDMVLLNL VLSVKEYYGS FKLYLYISEV
AVQVAFGTLL FVYFPNLDPY PGYTPVGTEN SEDYEYEELP GGENICPERH ANLFDSIFFS
WLNPLMTLGS KRPLTEKDVW HLDTWDKTET LMRSFQKSWD KELEKPKPWL LRALNNSLGG
RFWWGGFWKI GNDCSQFVGP LLLNELLKSM QLNEPAWIGY IYAISIFVGV VLGVLCEAQY
FQNVMRVGYR LRSALIAAVF RKSLRLTNEG RKKFQTGKIT NLMTTDAESL QQICQSLHTM
WSAPFRIIVA LVLLYQQLGV ASIIGALFLV LMFPIQTVII SKTQKLTKEG LQRTDKRIGL
MNEVLAAMDT VKCYAWENSF QSKVQTVRDD ELSWFRKAQL LSAFNMFILN SIPVLVTVVS
FGVFSLLGGD LTPARAFTSL SLFSVLRFPL FMLPNIITQM VNANVSLNRL EEVLSTEERV
LLPNPPIEPG QPAISIRNGY FSWDSKADRP TLSNINLDIP LGSLVAVVGS TGEGKTSLIS
AMLGELPARS DATVTLRGSV AYVPQVSWIF NATVRDNILF GAPFDQEKYE RVIDVTALQH
DLELLPGGDL TEIGERGVNI SGGQKQRVSM ARAVYSNSDV CILDDPLSAL DAHVGQQVFE
KCIKRELGQT TRVLVTNQLH FLSQVDKILL VHEGTVKEEG TYEELCHSGP LFQRLMENAG
KVEDYSEENG EAEVDQTSVK PVENGNANNL QKDGIETKNS KEGNSVLVKR EERETGVVSW
KVLERYQNAL GGAWVVMMLV ICYVLTQVFR VSSSTWLSEW TDSGTPKTHG PLFYNIVYAL
LSFGQVSVTL INSYWLIMSS LYAAKKMHDA MLGSILRAPM VFFQTNPLGR IINRFAKDMG
DIDRTVAVFV NMFMGSIAQL LSTVILIGIV STLSLWAIMP LLVVFYGAYL YYQNTSREIK
RMDSTTRSPV YAQFGEALNG LSSIRAYKAY DRMAEINGRS MDNNIRFTLV NMAANRWLGI
RLEVLGGLMV WLTASLAVMQ NGKAANQQAY ASTMGLLLSY ALSITSSLTA VLRLASLAEN
SLNSVERVGN YIEIPSEAPL VIENNRPPPG WPSSGSIKFE DVVLRYRPEL PPVLHGVSFL
ISPMDKVGIV GRTGAGKSSL LNALFRIVEL EKGRILIDEC DIGRFGLMDL RKVLGIIPQA
PVLFSGTVRF NLDPFSEHND ADLWESLERA HLKDTIRRNP LGLDAEVTEA GENFSVGQRQ
LLSLARALLR RSKILVLDEA TAAVDVRTDV LIQKTIREEF KSCTMLIIAH RLNTIIDCDK
VLVLDSGKVQ EFSSPENLLS NGESSFSKMV QSTGTANAEY LRSITLENKR TREANGDDSQ
PLEGQRKWQA SSRWAAAAQF ALAVSLTSSH NDLQSLEIED DNSILKKTKD AVVTLRSVLE
GKHDKEIEDS LNQSDISRER WWPSLYKMVE GLAVMSRLAR NRMQHPDYNL EGKSFDWDNV
EM
