AB1D_ARATH
ID AB1D_ARATH Reviewed; 1337 AA.
AC Q94FB9; Q8VWH7; Q9SMR8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ABC transporter D family member 1 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCD.1 {ECO:0000303|PubMed:18299247};
DE Short=AtABCD1 {ECO:0000303|PubMed:18299247};
DE EC=7.6.2.4;
DE AltName: Full=Peroxisomal ABC transporter 1;
DE Short=AtPXA1;
DE AltName: Full=Protein ACETATE NON-UTILIZING 2;
DE AltName: Full=Protein COMATOSE;
DE AltName: Full=Protein PEROXISOME DEFECTIVE 3;
DE Short=Ped3p;
GN Name=ABCD1 {ECO:0000303|PubMed:18299247};
GN Synonyms=ACN2, CTS, PED3, PMP2, PXA1; OrderedLocusNames=At4g39850;
GN ORFNames=T5J17.20;
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11706205; DOI=10.1104/pp.010550;
RA Zolman B.K., Silva I.D., Bartel B.;
RT "The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette
RT transporter-like protein required for peroxisomal fatty acid beta-
RT oxidation.";
RL Plant Physiol. 127:1266-1278(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12065405; DOI=10.1093/emboj/cdf300;
RA Footitt S., Slocombe S.P., Larner V., Kurup S., Wu Y., Larson T.,
RA Graham I., Baker A., Holdsworth M.;
RT "Control of germination and lipid mobilization by COMATOSE, the Arabidopsis
RT homologue of human ALDP.";
RL EMBO J. 21:2912-2922(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS OF SER-810 AND
RP ARG-1035, FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=11828016; DOI=10.1093/pcp/pcf023;
RA Hayashi M., Nito K., Takei-Hoshi R., Yagi M., Kondo M., Suenaga A.,
RA Yamaya T., Nishimura M.;
RT "Ped3p is a peroxisomal ATP-binding cassette transporter that might supply
RT substrates for fatty acid beta-oxidation.";
RL Plant Cell Physiol. 43:1-11(2002).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9490742; DOI=10.2307/3870697;
RA Hayashi M., Toriyama K., Kondo M., Nishimura M.;
RT "2,4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have
RT defects in glyoxysomal fatty acid beta-oxidation.";
RL Plant Cell 10:183-195(1998).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10934020; DOI=10.1242/dev.127.17.3759;
RA Russell L., Larner V., Kurup S., Bougourd S., Holdsworth M.;
RT "The Arabidopsis COMATOSE locus regulates germination potential.";
RL Development 127:3759-3767(2000).
RN [10]
RP FUNCTION.
RX PubMed=11063705; DOI=10.1093/genetics/156.3.1323;
RA Zolman B.K., Yoder A., Bartel B.;
RT "Genetic analysis of indole-3-butyric acid responses in Arabidopsis
RT thaliana reveals four mutant classes.";
RL Genetics 156:1323-1337(2000).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14963767; DOI=10.1007/s00438-004-0985-9;
RA Hooks M.A., Turner J.E., Murphy E.C., Graham I.A.;
RT "Acetate non-utilizing mutants of Arabidopsis: evidence that organic acids
RT influence carbohydrate perception in germinating seedlings.";
RL Mol. Genet. Genomics 271:249-256(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16844736; DOI=10.1093/jxb/erl045;
RA Footitt S., Marquez J., Schmuths H., Baker A., Theodoulou F.L.,
RA Holdsworth M.;
RT "Analysis of the role of COMATOSE and peroxisomal beta-oxidation in the
RT determination of germination potential in Arabidopsis.";
RL J. Exp. Bot. 57:2805-2814(2006).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17468211; DOI=10.1104/pp.107.099903;
RA Footitt S., Dietrich D., Fait A., Fernie A.R., Holdsworth M.J., Baker A.,
RA Theodoulou F.L.;
RT "The COMATOSE ATP-binding cassette transporter is required for full
RT fertility in Arabidopsis.";
RL Plant Physiol. 144:1467-1480(2007).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17322332; DOI=10.1104/pp.107.096057;
RA Carrera E., Holman T., Medhurst A., Peer W., Schmuths H., Footitt S.,
RA Theodoulou F.L., Holdsworth M.J.;
RT "Gene expression profiling reveals defined functions of the ATP-binding
RT cassette transporter COMATOSE late in phase II of germination.";
RL Plant Physiol. 143:1669-1679(2007).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17581114; DOI=10.1042/bj20070258;
RA Hooks M.A., Turner J.E., Murphy E.C., Johnston K.A., Burr S.,
RA Jaroslawski S.;
RT "The Arabidopsis ALDP protein homologue COMATOSE is instrumental in
RT peroxisomal acetate metabolism.";
RL Biochem. J. 406:399-406(2007).
RN [16]
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: Contributes to the transport of fatty acids and their
CC derivatives (acyl CoAs) across the peroxisomal membrane. Provides
CC acetate to the glyoxylate cycle in developing seedlings. Involved in
CC pollen tube elongation, ovule fertilization, and seeds germination
CC after imbibition (controls the switch between the opposing
CC developmental programs of dormancy and germination), probably by
CC promoting beta-oxidation of storage lipids during gluconeogenesis.
CC Required for biosynthesis of jasmonic acid and conversion of indole
CC butyric acid to indole acetic acid. Confers sensitivity to
CC monofluoroacetic acid (FAc), a toxic acetate analog, and to 2,4-
CC dichlorophenoxybutyric acid (2,4-DB) and indole-3-butyric acid (IBA),
CC two precursors of auxin after beta-oxidation.
CC {ECO:0000269|PubMed:10934020, ECO:0000269|PubMed:11063705,
CC ECO:0000269|PubMed:11706205, ECO:0000269|PubMed:11828016,
CC ECO:0000269|PubMed:12065405, ECO:0000269|PubMed:14963767,
CC ECO:0000269|PubMed:16844736, ECO:0000269|PubMed:17322332,
CC ECO:0000269|PubMed:17468211, ECO:0000269|PubMed:17581114,
CC ECO:0000269|PubMed:9490742}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA(out) + ATP + H2O = ADP + an acyl-CoA(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:15181, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:456216; EC=7.6.2.4;
CC -!- INTERACTION:
CC Q94FB9; Q9SRQ3: PEX19-1; NbExp=2; IntAct=EBI-7933055, EBI-1151789;
CC Q94FB9; Q94EI3: PEX19-2; NbExp=2; IntAct=EBI-7933055, EBI-7933092;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:12065405}; Multi-pass membrane protein
CC {ECO:0000255}. Glyoxysome membrane {ECO:0000269|PubMed:11828016};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94FB9-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Levels increase transiently after germination,
CC before and during radicle emergence, especially in darkness (at protein
CC level). {ECO:0000269|PubMed:11828016, ECO:0000269|PubMed:12065405}.
CC -!- DISRUPTION PHENOTYPE: Impaired germination after imbibition, rescued by
CC sucrose treatment. Resistance to FAc, IBA and 2,4-DB. Compromised
CC ability to convert acetate into soluble carbohydrate. Defective in
CC lipid mobilization and accumulate acyl CoAs. Poor initiation of lateral
CC root formation and smaller rosettes with fewer leaves than in wild-
CC type. Crinkled and waxy leaves. {ECO:0000269|PubMed:10934020,
CC ECO:0000269|PubMed:11706205, ECO:0000269|PubMed:11828016,
CC ECO:0000269|PubMed:12065405, ECO:0000269|PubMed:14963767,
CC ECO:0000269|PubMed:16844736, ECO:0000269|PubMed:17322332,
CC ECO:0000269|PubMed:17468211, ECO:0000269|PubMed:17581114,
CC ECO:0000269|PubMed:9490742}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38898.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80648.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF378120; AAK95343.1; -; mRNA.
DR EMBL; AJ311341; CAC85290.1; -; Genomic_DNA.
DR EMBL; AB070615; BAB84550.1; -; Genomic_DNA.
DR EMBL; AB070616; BAB84551.1; -; mRNA.
DR EMBL; AL035708; CAB38898.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161596; CAB80648.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87126.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66328.1; -; Genomic_DNA.
DR PIR; T06091; T06091.
DR RefSeq; NP_001328232.1; NM_001342558.1. [Q94FB9-1]
DR RefSeq; NP_568072.1; NM_120148.3. [Q94FB9-1]
DR AlphaFoldDB; Q94FB9; -.
DR SMR; Q94FB9; -.
DR BioGRID; 15424; 7.
DR IntAct; Q94FB9; 2.
DR MINT; Q94FB9; -.
DR STRING; 3702.AT4G39850.3; -.
DR TCDB; 3.A.1.203.5; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q94FB9; -.
DR PaxDb; Q94FB9; -.
DR PRIDE; Q94FB9; -.
DR ProteomicsDB; 245130; -. [Q94FB9-1]
DR EnsemblPlants; AT4G39850.1; AT4G39850.1; AT4G39850. [Q94FB9-1]
DR EnsemblPlants; AT4G39850.4; AT4G39850.4; AT4G39850. [Q94FB9-1]
DR GeneID; 830144; -.
DR Gramene; AT4G39850.1; AT4G39850.1; AT4G39850. [Q94FB9-1]
DR Gramene; AT4G39850.4; AT4G39850.4; AT4G39850. [Q94FB9-1]
DR KEGG; ath:AT4G39850; -.
DR Araport; AT4G39850; -.
DR eggNOG; KOG0060; Eukaryota.
DR eggNOG; KOG0064; Eukaryota.
DR OMA; WELCEIH; -.
DR PhylomeDB; Q94FB9; -.
DR BioCyc; ARA:AT4G39850-MON; -.
DR BRENDA; 7.6.2.4; 399.
DR PRO; PR:Q94FB9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94FB9; baseline and differential.
DR Genevisible; Q94FB9; AT.
DR GO; GO:0046861; C:glyoxysomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IMP:CACAO.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF06472; ABC_membrane_2; 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 Alternative splicing; ATP-binding; Glyoxysome; Membrane;
KW Nucleotide-binding; Peroxisome; Reference proteome; Repeat; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1337
FT /note="ABC transporter D family member 1"
FT /id="PRO_0000379135"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 117..395
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 448..695
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 751..1049
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1091..1337
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1130..1137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 810
FT /note="S->N: In ped3-4; Normal germination, but impaired
FT seedling, roots and leaves growth."
FT /evidence="ECO:0000269|PubMed:11828016"
FT MUTAGEN 1035
FT /note="R->W: In ped3-2; Normal germination, but impaired
FT seedling, roots and leaves growth."
FT /evidence="ECO:0000269|PubMed:11828016"
FT CONFLICT 64
FT /note="T -> A (in Ref. 3; BAB84551/BAB84550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1337 AA; 149576 MW; 9AA08CF944FC8BFE CRC64;
MPSLQLLQLT ERGRGLVASR RKSILLAAGI VAAGGTAVYL KSRVASRRPD SSRLCNGQSD
DDETLEKLTA TDQNAKITTK KKKGGGLKSL QVLTAILLSQ MGKMGARDLL ALVATVVFRT
ALSNRLAKVQ GFLFRAAFLR RAPLFLRLIS ENIMLCFMLS TLHSTSKYIT GALSLRFRKI
LTKIIHSHYF ENMVYYKISH VDGRITHPEQ RIASDVPRFS SELSDLILDD LTAVTDGILY
AWRLCSYASP KYIFWILAYV LGAGTAIRNF SPSFGKLMSK EQQLEGEYRQ LHSRLRTHSE
SIAFYGGETR EESHIQQKFK NLVSHMSHVL HDHWWFGMIQ DFLLKYLGAT VAVILIIEPF
FSGHLRPDDS TLGRAEMLSN IRYHTSVIIS LFQALGTLSI SSRRLNRLSG YADRIHELMA
VSRELSGDDK SSFQRNRSRN YLSEANYVEF SDVKVVTPTG NVLVEDLTLR VEQGSNLLIT
GPNGSGKSSL FRVLGGLWPL VSGHIVKPGV GSDLNKEIFY VPQRPYMAVG TLRDQLIYPL
TSGQESELLT EIGMVELLKN VDLEYLLDRY QPEKEVNWGD ELSLGEQQRL GMARLFYHKP
KFAILDECTS AVTTDMEERF AAKVRAMGTS CITISHRPAL VAFHDVVLSL DGEGGWSVHY
KRDDSALLTD AEIDSVKSSD TDRQNDAMVV QRAFAAARKE SATNSKAQSY QTQLIARSPV
VDKSVVLPRF PQPQTSQRAL PSRVAAMLNV LIPTIFDKQG AQLLAVACLV VSRTLISDRI
ASLNGTTVKY VLEQDKAAFV RLIGLSVLQS GASSIIAPSL RHLTQRLALG WRIRLTQHLL
RNYLRNNAFY KVFHMSGNSI DADQRLTRDL EKLTADLSGL LTGMVKPSVD ILWFTWRMKL
LTGQRGVAIL YTYMLLGLGF LRRVAPDFGD LAGEEQQLEG KFRFMHERLN THAESIAFFG
GGAREKAMVD KKFRALLDHS LMLLRKKWLY GILDDFVTKQ LPNNVTWGLS LLYALEHKGD
RALVSTQGEL AHALRYLASV VSQSFMAFGD ILELHKKFLE LSGGINRIFE LDEFLDASQS
GVTSENQTSR LDSQDLLSFS EVDIITPAQK LMASKLSCEI VSGKSLLVTG PNGSGKTSVF
RVLRDIWPTV CGRLTKPSLD IKELGSGNGM FFVPQRPYTC LGTLRDQIIY PLSKEEAEKR
AAKLYTSGES STEAGSILDS HLKTILENVR LVYLLERDVG GWDATTNWED ILSLGEQQRL
GMARLFFHRP KFGVLDECTN ATSVDVEEQL YRVARDMGVT FITSSQRPAL IPFHSLELRL
IDGEGNWELR SIEQTTE
