AB37G_ARATH
ID AB37G_ARATH Reviewed; 1450 AA.
AC Q9LFH0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ABC transporter G family member 37 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.37 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG37 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 9 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311, ECO:0000303|PubMed:16877699};
DE AltName: Full=Protein ENHANCER OF TIR1-1 AUXIN RESISTANCE 4 {ECO:0000303|PubMed:16877699};
DE AltName: Full=Protein POLAR AUXIN TRANSPORT INHIBITOR SENSITIVE 1 {ECO:0000303|PubMed:20498067};
GN Name=ABCG37 {ECO:0000303|PubMed:18299247};
GN Synonyms=ETA4 {ECO:0000303|PubMed:16877699},
GN PDR12 {ECO:0000303|PubMed:18299247}, PDR9 {ECO:0000303|PubMed:12430018,
GN ECO:0000303|PubMed:16506311, ECO:0000303|PubMed:16877699},
GN PIS1 {ECO:0000303|PubMed:20498067};
GN OrderedLocusNames=At3g53480 {ECO:0000312|Araport:AT3G53480};
GN ORFNames=F4P12.180 {ECO:0000312|EMBL:CAB67655.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12430018; DOI=10.1007/s00425-002-0889-z;
RA van den Brule S., Smart C.C.;
RT "The plant PDR family of ABC transporters.";
RL Planta 216:95-106(2002).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
RA Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
RT "Organization and function of the plant pleiotropic drug resistance ABC
RT transporter family.";
RL FEBS Lett. 580:1123-1130(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-1034, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16877699; DOI=10.1104/pp.106.084533;
RA Ito H., Gray W.M.;
RT "A gain-of-function mutation in the Arabidopsis pleiotropic drug resistance
RT transporter PDR9 confers resistance to auxinic herbicides.";
RL Plant Physiol. 142:63-74(2006).
RN [6]
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=20451385; DOI=10.1016/j.cub.2010.03.059;
RA Langowski L., Ruzicka K., Naramoto S., Kleine-Vehn J., Friml J.;
RT "Trafficking to the outer polar domain defines the root-soil interface.";
RL Curr. Biol. 20:904-908(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=20498067; DOI=10.1073/pnas.1005878107;
RA Ruzicka K., Strader L.C., Bailly A., Yang H., Blakeslee J., Langowski L.,
RA Nejedla E., Fujita H., Itoh H., Syono K., Hejatko J., Gray W.M.,
RA Martinoia E., Geisler M., Bartel B., Murphy A.S., Friml J.;
RT "Arabidopsis PIS1 encodes the ABCG37 transporter of auxinic compounds
RT including the auxin precursor indole-3-butyric acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10749-10753(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY IRON DEFICIENCY.
RC STRAIN=cv. Columbia;
RX PubMed=24015802; DOI=10.1111/nph.12471;
RA Fourcroy P., Siso-Terraza P., Sudre D., Saviron M., Reyt G., Gaymard F.,
RA Abadia A., Abadia J., Alvarez-Fernandez A., Briat J.-F.;
RT "Involvement of the ABCG37 transporter in secretion of scopoletin and
RT derivatives by Arabidopsis roots in response to iron deficiency.";
RL New Phytol. 201:155-167(2014).
RN [10]
RP REVIEW ON PHYTOHORMONE TRANSPORT.
RX PubMed=26517905; DOI=10.1042/bst20150106;
RA Borghi L., Kang J., Ko D., Lee Y., Martinoia E.;
RT "The role of ABCG-type ABC transporters in phytohormone transport.";
RL Biochem. Soc. Trans. 43:924-930(2015).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28623273; DOI=10.1038/s41598-017-03250-6;
RA Ziegler J., Schmidt S., Strehmel N., Scheel D., Abel S.;
RT "Arabidopsis transporter ABCG37/PDR9 contributes primarily highly
RT oxygenated coumarins to root exudation.";
RL Sci. Rep. 7:3704-3704(2017).
CC -!- FUNCTION: Together with ABCG36, regulates auxin homeostasis and
CC responses by playing a dual role in coumarine (and derivatives) and in
CC the auxin precursor indole 3-butyric acid (IBA) efflux transport, thus
CC influencing roots and root hairs development (PubMed:24015802,
CC PubMed:20498067). Mediates coumarin exudation in the rhizosphere,
CC especially in iron (Fe) deficient conditions, with a strong specificity
CC for highly oxygenated compounds such as scopoletin and derivatives,
CC dihydroxyscopoletin, esculetin, fraxin, fraxetin and esculin; these
CC molecules improve plant Fe nutrition (PubMed:28623273, PubMed:26517905,
CC PubMed:24015802). Involved in the cellular detoxification of
CC xenobiotics by promoting the excretion of some auxinic herbicides
CC including 2,4-dichlorophenoxyacetic acid (2,4-D), 4-(2,4-
CC dichlorophenoxy)butyric acid (2,4-DB) and other members of the
CC phenoxyalkanoic acid family as well as the polar auxin transport
CC inhibitor, napthylphthalamic acid (NPA) (PubMed:24015802,
CC PubMed:16877699, PubMed:20498067). May be a general defense protein (By
CC similarity). {ECO:0000250|UniProtKB:Q9XIE2,
CC ECO:0000269|PubMed:16877699, ECO:0000269|PubMed:20498067,
CC ECO:0000269|PubMed:24015802, ECO:0000269|PubMed:28623273,
CC ECO:0000303|PubMed:26517905}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16877699,
CC ECO:0000269|PubMed:20451385, ECO:0000269|PubMed:20498067}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Polarized localization at the
CC outermost side of root epidermal and cap cells.
CC {ECO:0000269|PubMed:20451385, ECO:0000269|PubMed:20498067}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and, to a lower extent, in
CC seedlings. {ECO:0000269|PubMed:12430018, ECO:0000269|PubMed:16877699,
CC ECO:0000269|PubMed:20498067}.
CC -!- DEVELOPMENTAL STAGE: In roots, mostly expressed in the cells of the
CC lateral root cap and epidermal cells at the root tip (PubMed:16877699,
CC PubMed:20498067). In shoots, confined to the stipules
CC (PubMed:16877699). {ECO:0000269|PubMed:16877699,
CC ECO:0000269|PubMed:20498067}.
CC -!- INDUCTION: Induced by cycloheximide (CHX) and cold/dark treatment
CC (PubMed:12430018). Up-regulated in response to iron (Fe) deficiency
CC (PubMed:24015802). {ECO:0000269|PubMed:12430018,
CC ECO:0000269|PubMed:24015802}.
CC -!- DISRUPTION PHENOTYPE: Defects in efflux of the auxin precursor indole-
CC 3-butyric acid (IBA) associated with developmental defects such as
CC abnormally long root hairs and increased lateral root production
CC (PubMed:20498067). Strongly reduced coumarin (e.g. highly oxygenated
CC compounds scopoletin, dihydroxyscopoletin, esculetin, fraxin, fraxetin
CC and esculin) exudation in the rhizosphere, especially in iron (Fe)
CC deficient conditions (PubMed:28623273, PubMed:24015802).
CC Hypersensitivity to iron (Fe) deficiency (PubMed:24015802). Increased
CC sensitivity to the auxinic herbicides 2,4-dichlorophenoxyacetic acid
CC (2,4-D), 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and 2-
CC naphthoxyacetic acid (2-NOA), but normal responses to the endogenous
CC auxins indole-3-acetic acid (IAA), phenylacetic acid (PAA) and indole-
CC butyric acid (IBA) (PubMed:16877699, PubMed:20498067). Hypersensitivity
CC to polar auxin transport inhibitors including napthylphthalamic acid
CC (NPA), 1-naphthoxyacetic acid (1-NOA), 2-(1-pyrenoyl)benzoic acid (PBA)
CC and 2,3,5-triiodobenzoic acid (TIBA) (PubMed:16877699,
CC PubMed:20498067). {ECO:0000269|PubMed:16877699,
CC ECO:0000269|PubMed:20498067, ECO:0000269|PubMed:24015802,
CC ECO:0000269|PubMed:28623273}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AL132966; CAB67655.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79095.1; -; Genomic_DNA.
DR EMBL; BK001008; DAA00877.1; -; Genomic_DNA.
DR PIR; T45888; T45888.
DR RefSeq; NP_190916.1; NM_115208.4.
DR AlphaFoldDB; Q9LFH0; -.
DR SMR; Q9LFH0; -.
DR BioGRID; 9833; 2.
DR STRING; 3702.AT3G53480.1; -.
DR TCDB; 3.A.1.205.29; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9LFH0; -.
DR PaxDb; Q9LFH0; -.
DR PRIDE; Q9LFH0; -.
DR ProteomicsDB; 244337; -.
DR EnsemblPlants; AT3G53480.1; AT3G53480.1; AT3G53480.
DR GeneID; 824516; -.
DR Gramene; AT3G53480.1; AT3G53480.1; AT3G53480.
DR KEGG; ath:AT3G53480; -.
DR Araport; AT3G53480; -.
DR TAIR; locus:2084081; AT3G53480.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q9LFH0; -.
DR OMA; VYGWKVF; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q9LFH0; -.
DR PRO; PR:Q9LFH0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFH0; baseline and differential.
DR Genevisible; Q9LFH0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0018901; P:2,4-dichlorophenoxyacetic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1990748; P:cellular detoxification; IMP:UniProtKB.
DR GO; GO:0071366; P:cellular response to indolebutyric acid stimulus; IMP:TAIR.
DR GO; GO:0009804; P:coumarin metabolic process; IMP:UniProtKB.
DR GO; GO:0140352; P:export from cell; IMP:UniProtKB.
DR GO; GO:1990641; P:response to iron ion starvation; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Cell membrane; Detoxification;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1450
FT /note="ABC transporter G family member 37"
FT /id="PRO_0000234636"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1226..1246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1282..1302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1313..1333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1339..1359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1365..1385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1422..1442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 175..447
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 525..737
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 850..1103
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1175..1389
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255"
FT REGION 810..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 895..902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 1034
FT /note="A->T: In pdr9-1 and eta4; gain of function, probably
FT increasing protein stability, which leads to an enhanced
FT tolerance to the auxinic herbicides 2,4-
FT dichlorophenoxyacetic acid (2,4-D),4-chlorophenoxyacetic
FT acid (4-CPA), 4-chloro-2-methylphenoxy acetic acid (MCPA),
FT 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), 4,5-Cl(2)-IAA
FT and slighty to 4-Cl-IAA, but normal responses to the
FT endogenous auxins indole-3-acetic acid (IAA),
FT naphthylacetic acid (NAA) and indole-butyric acid (IBA)."
FT /evidence="ECO:0000269|PubMed:16877699"
SQ SEQUENCE 1450 AA; 164106 MW; F8F184B24ADC3A1A CRC64;
MAHMVGADDI ESLRVELAEI GRSIRSSFRR HTSSFRSSSS IYEVENDGDV NDHDAEYALQ
WAEIERLPTV KRMRSTLLDD GDESMTEKGR RVVDVTKLGA VERHLMIEKL IKHIENDNLK
LLKKIRRRID RVGMELPTIE VRYESLKVVA ECEVVEGKAL PTLWNTAKRV LSELVKLTGA
KTHEAKINII NDVNGIIKPG RLTLLLGPPS CGKTTLLKAL SGNLENNLKC SGEISYNGHR
LDEFVPQKTS AYISQYDLHI AEMTVRETVD FSARCQGVGS RTDIMMEVSK REKEKGIIPD
TEVDAYMKAI SVEGLQRSLQ TDYILKILGL DICAEILIGD VMRRGISGGQ KKRLTTAEMI
VGPTKALFMD EITNGLDSST AFQIVKSLQQ FAHISSATVL VSLLQPAPES YDLFDDIMLM
AKGRIVYHGP RGEVLNFFED CGFRCPERKG VADFLQEVIS KKDQAQYWWH EDLPYSFVSV
EMLSKKFKDL SIGKKIEDTL SKPYDRSKSH KDALSFSVYS LPNWELFIAC ISREYLLMKR
NYFVYIFKTA QLVMAAFITM TVFIRTRMGI DIIHGNSYMS ALFFALIILL VDGFPELSMT
AQRLAVFYKQ KQLCFYPAWA YAIPATVLKV PLSFFESLVW TCLSYYVIGY TPEASRFFKQ
FILLFAVHFT SISMFRCLAA IFQTVVASIT AGSFGILFTF VFAGFVIPPP SMPAWLKWGF
WANPLSYGEI GLSVNEFLAP RWNQMQPNNF TLGRTILQTR GMDYNGYMYW VSLCALLGFT
VLFNIIFTLA LTFLKSPTSS RAMISQDKLS ELQGTEKSTE DSSVRKKTTD SPVKTEEEDK
MVLPFKPLTV TFQDLNYFVD MPVEMRDQGY DQKKLQLLSD ITGAFRPGIL TALMGVSGAG
KTTLLDVLAG RKTSGYIEGD IRISGFPKVQ ETFARVSGYC EQTDIHSPNI TVEESVIYSA
WLRLAPEIDA TTKTKFVKQV LETIELDEIK DSLVGVTGVS GLSTEQRKRL TIAVELVANP
SIIFMDEPTT GLDARAAAIV MRAVKNVADT GRTIVCTIHQ PSIDIFEAFD ELVLLKRGGR
MIYTGPLGQH SRHIIEYFES VPEIPKIKDN HNPATWMLDV SSQSVEIELG VDFAKIYHDS
ALYKRNSELV KQLSQPDSGS SDIQFKRTFA QSWWGQFKSI LWKMNLSYWR SPSYNLMRMM
HTLVSSLIFG ALFWKQGQNL DTQQSMFTVF GAIYGLVLFL GINNCASALQ YFETERNVMY
RERFAGMYSA TAYALGQVVT EIPYIFIQAA EFVIVTYPMI GFYPSAYKVF WSLYSMFCSL
LTFNYLAMFL VSITPNFMVA AILQSLFYVG FNLFSGFLIP QTQVPGWWIW LYYLTPTSWT
LNGFISSQYG DIHEEINVFG QSTTVARFLK DYFGFHHDLL AVTAVVQIAF PIALASMFAF
FVGKLNFQRR
