AB30G_ARATH
ID AB30G_ARATH Reviewed; 1400 AA.
AC Q8GZ52; O23376; O23377; Q7PC89;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ABC transporter G family member 30 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.30 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG30 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 2 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
DE Short=AtPDR2 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
GN Name=ABCG30 {ECO:0000303|PubMed:18299247};
GN Synonyms=PDR2 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
GN OrderedLocusNames=At4g15230/At4g15220 {ECO:0000312|Araport:AT4G15230};
GN ORFNames=dl3660w/dl3655w {ECO:0000312|EMBL:CAB10301.1,
GN ECO:0000312|EMBL:CAB45997.1}, FCAALL.241 {ECO:0000312|EMBL:CAB78564.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19854857; DOI=10.1104/pp.109.147462;
RA Badri D.V., Quintana N., El Kassis E.G., Kim H.K., Choi Y.H., Sugiyama A.,
RA Verpoorte R., Martinoia E., Manter D.K., Vivanco J.M.;
RT "An ABC transporter mutation alters root exudation of phytochemicals that
RT provoke an overhaul of natural soil microbiota.";
RL Plant Physiol. 151:2006-2017(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26334616; DOI=10.1038/ncomms9113;
RA Kang J., Yim S., Choi H., Kim A., Lee K.P., Lopez-Molina L., Martinoia E.,
RA Lee Y.;
RT "Abscisic acid transporters cooperate to control seed germination.";
RL Nat. Commun. 6:8113-8113(2015).
CC -!- FUNCTION: Together with ABCG40, import into the embryo the abscisic
CC acid (ABA) delivered from the endosperm via ABCG25 and ABCG31-mediated
CC export to suppress radicle extension and subsequent embryonic growth
CC (PubMed:26334616). Involved in root secretion of phytochemicals
CC (phenolics and sugars) which regulate soil microbiota, influencing both
CC fungal and bacterial communities (PubMed:19854857). May be a general
CC defense protein (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19854857, ECO:0000269|PubMed:26334616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=abscisate(out) + ATP + H2O = abscisate(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:63960, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62432, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:26334616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63961;
CC Evidence={ECO:0000269|PubMed:26334616};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26334616};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GZ52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GZ52-2; Sequence=VSP_018392;
CC -!- TISSUE SPECIFICITY: Confined to roots (PubMed:12430018). In seeds,
CC mainly expressed in the embryo and, to a lesser extent, in the
CC endosperm (PubMed:26334616). {ECO:0000269|PubMed:12430018,
CC ECO:0000269|PubMed:26334616}.
CC -!- INDUCTION: Repressed by cold/dark treatment.
CC {ECO:0000269|PubMed:12430018}.
CC -!- DISRUPTION PHENOTYPE: Early seeds germination on imbibition without
CC stratification, and reduced abscisic acid (ABA)-mediated inhibition of
CC stratified seeds germination (PubMed:26334616). Altered root exudation
CC of phytochemicals, with increased phenolics (e.g. benzoic acid,
CC salicylic acid, syringic acid, tartaric acid, lactic acid, alpha-
CC linolenic acid, cyanidin, sinapoyl malate, valine and indole 3-acetic
CC acid) and decreased sugars levels (e.g. raffinose, glucose, fructose
CC and mannitol), leading to an overhaul of natural soil microbiota,
CC including both fungal and bacterial communities; this phenotype is
CC associated with an up-regulation of some genes involved in biosynthesis
CC and transport of secondary metabolites, but the down-regulation of some
CC sugar transporters (PubMed:19854857). {ECO:0000269|PubMed:19854857,
CC ECO:0000269|PubMed:26334616}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10301.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15220 and At4g15230.; Evidence={ECO:0000305};
CC Sequence=CAB45997.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15220 and At4g15230.; Evidence={ECO:0000305};
CC Sequence=CAB78564.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15220 and At4g15230.; Evidence={ECO:0000305};
CC Sequence=CAB78565.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g15220 and At4g15230.; Evidence={ECO:0000305};
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DR EMBL; Z97338; CAB10301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z97338; CAB45997.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78565.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83571.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66937.1; -; Genomic_DNA.
DR EMBL; AK117203; BAC41879.1; -; mRNA.
DR EMBL; BK001000; DAA00869.1; -; Genomic_DNA.
DR PIR; C71416; C71416.
DR PIR; D71416; D71416.
DR PIR; G85167; G85167.
DR RefSeq; NP_001319944.1; NM_001341010.1. [Q8GZ52-1]
DR RefSeq; NP_193258.3; NM_117611.5. [Q8GZ52-1]
DR AlphaFoldDB; Q8GZ52; -.
DR SMR; Q8GZ52; -.
DR BioGRID; 12484; 1.
DR STRING; 3702.AT4G15230.1; -.
DR TCDB; 3.A.1.205.28; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8GZ52; -.
DR PRIDE; Q8GZ52; -.
DR ProteomicsDB; 245153; -. [Q8GZ52-1]
DR EnsemblPlants; AT4G15230.1; AT4G15230.1; AT4G15230. [Q8GZ52-1]
DR EnsemblPlants; AT4G15230.3; AT4G15230.3; AT4G15230. [Q8GZ52-1]
DR GeneID; 827187; -.
DR Gramene; AT4G15230.1; AT4G15230.1; AT4G15230. [Q8GZ52-1]
DR Gramene; AT4G15230.3; AT4G15230.3; AT4G15230. [Q8GZ52-1]
DR KEGG; ath:AT4G15230; -.
DR Araport; AT4G15230; -.
DR TAIR; locus:2129830; AT4G15230.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q8GZ52; -.
DR OrthoDB; 37708at2759; -.
DR PRO; PR:Q8GZ52; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GZ52; baseline and differential.
DR Genevisible; Q8GZ52; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0080168; P:abscisic acid transport; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0033231; P:carbohydrate export; IMP:TAIR.
DR GO; GO:0098657; P:import into cell; IMP:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; IMP:UniProtKB.
DR GO; GO:0048581; P:negative regulation of post-embryonic development; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
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; 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 Abscisic acid signaling pathway; Alternative splicing; ATP-binding;
KW Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1400
FT /note="ABC transporter G family member 30"
FT /id="PRO_0000234629"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1228..1248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1289..1309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1317..1337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1372..1392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 141..414
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 492..704
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 808..1053
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1125..1339
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 845..852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..640
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_018392"
SQ SEQUENCE 1400 AA; 157768 MW; EED12151C91EB57B CRC64;
MIQTGEEDEE KATSLEVEFA SGNGVDDEEE LRLQWATVER LPTFKRVTTA LLARDEVSGK
GRVIDVTRLE GAERRLLIEM LVKQIEDDNL RLLRKIRKRI DKVGIELPTV EVRFNNLSVE
AECQVIHGKP IPTLWNTIKG LLSEFICSKK ETKIGILKGV SGIVRPGRMT LLLGPPGCGK
TTLLQALSGK FSDSVKVGGE VCYNGCSLSE FIPEKTSSYI SQNDLHIPEL SVRETLDFSA
CCQGIGSRME IMKEISRMEK LQEIIPDPAV DAYMKATSVE GLKNNLQTDY ILKILGLDIC
ADTRVGDATR PGISGGEKRR LTTGELVVGP ATTLFMDEIS NGLDSSTTFQ IVSCLQQLAH
IAEATILISL LQPAPETFEL FDDVILMGEG KIIYHAPRAD ICRFFEEFGF KCPERKGVAD
FLQEIMSKKD QEQYWCHRDK PYSYISVDSF INKFKESNLG LLLKEELSKP FNKSQTRKDG
LCYKKYSLGK WEMLKACSRR EFLLMKRNSF IYLFKSALLV FNALVTMTVF LQVGATTDSL
HGNYLMGSLF TALFRLLADG LPELTLTISR LGVFCKQKDL YFYPAWAYAI PSIILKIPLS
VLDSFIWTLL TYYVIGYSPE VKRFFLQFLI LSTFNLSCVS MFRAIAAIFR TIIASTITGA
ISILVLSLFG GFVIPKSSMP AWLGWGFWLS PLSYAEIGLT ANEFFSPRWS KVISSKTTAG
EQMLDIRGLN FGRHSYWTAF GALVGFVLFF NALYVLALTY QNNPQRSRAI ISHEKYSRPI
EEDFKPCPKI TSRAKTGKII LPFKPLTVTF QNVQYYIETP QGKTRQLLSD ITGALKPGVL
TSLMGVSGAG KTTLLDVLSG RKTRGIIKGE IKVGGYPKVQ ETFARVSGYC EQFDIHSPNI
TVEESLKYSA WLRLPYNIDS KTKNELVKEV LETVELDDIK DSVVGLPGIS GLSIEQRKRL
TIAVELVANP SIIFMDEPTT GLDARAAAIV MRAVKNVAET GRTVVCTIHQ PSIDIFETFD
ELILMKNGGQ LVYYGPPGQN SSKVIEYFES FSGLPKIQKN CNPATWILDI TSKSAEEKLG
IDFSQSYKDS TLYKQNKMVV EQLSSASLGS EALRFPSQFS QTAWVQLKAC LWKQHYSYWR
NPSHNITRIV FILLDSTLCG LLFWQKAEDI NNQQDLISIF GSMYTLVVFP GMNNCAAVIN
FIAAERNVFY RERFARMYSS WAYSFSQVLI EVPYSLLQSL LCTIIVYPTI GYHMSVYKMF
WSLYSIFCSL LIFNYSGMLM VALTPNIHMA VTLRSSFFSM LNLFAGFVIP KQKIPKWWIW
MYYLSPTSWV LEGLLSSQYG DVDKEILVFG EKKRVSAFLE DYFGYKHESL AVVAFVLIAY
PIIVATLFAF FMSKLSFQKK
