ID   AB25B_ARATH             Reviewed;         728 AA.
AC   Q9LVM1; Q9LF78;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-MAY-2024, entry version 163.
DE   RecName: Full=ABC transporter B family member 25, mitochondrial;
DE            Short=ABC transporter ABCB.25;
DE            Short=AtABCB25;
DE   AltName: Full=ABC transporter of the mitochondrion 3;
DE            Short=AtATM3;
DE            Short=Iron-sulfur clusters transporter ATM3;
DE   AltName: Full=Protein STARIK 1;
DE   Flags: Precursor;
GN   Name=ABCB25; Synonyms=ATM3, STA1; OrderedLocusNames=At5g58270;
GN   ORFNames=MCK7.14;
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11158531; DOI=10.1105/tpc.13.1.89;
RA   Kushnir S., Babiychuk E., Storozhenko S., Davey M.W., Papenbrock J.,
RA   De Rycke R., Engler G., Stephan U.W., Lange H., Kispal G., Lill R.,
RA   Van Montagu M.;
RT   "A mutation of the mitochondrial ABC transporter Sta1 leads to dwarfism and
RT   chlorosis in the Arabidopsis mutant starik.";
RL   Plant Cell 13:89-100(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=17517886; DOI=10.1074/jbc.m702383200;
RA   Chen S., Sanchez-Fernandez R., Lyver E.R., Dancis A., Rea P.A.;
RT   "Functional characterization of AtATM1, AtATM2, and AtATM3, a subfamily of
RT   Arabidopsis half-molecule ATP-binding cassette transporters implicated in
RT   iron homeostasis.";
RL   J. Biol. Chem. 282:21561-21571(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CADMIUM AND LEAD.
RX   PubMed=16461380; DOI=10.1104/pp.105.074146;
RA   Kim D.-Y., Bovet L., Kushnir S., Noh E.W., Martinoia E., Lee Y.;
RT   "AtATM3 is involved in heavy metal resistance in Arabidopsis.";
RL   Plant Physiol. 140:922-932(2006).
RN   [10]
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   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-612.
RX   PubMed=19710232; DOI=10.1104/pp.109.143651;
RA   Bernard D.G., Cheng Y., Zhao Y., Balk J.;
RT   "An allelic mutant series of ATM3 reveals its key role in the biogenesis of
RT   cytosolic iron-sulfur proteins in Arabidopsis.";
RL   Plant Physiol. 151:590-602(2009).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20164445; DOI=10.1105/tpc.109.068478;
RA   Teschner J., Lachmann N., Schulze J., Geisler M., Selbach K.,
RA   Santamaria-Araujo J., Balk J., Mendel R.R., Bittner F.;
RT   "A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in
RT   molybdenum cofactor biosynthesis.";
RL   Plant Cell 22:468-480(2010).
CC   -!- FUNCTION: Performs an essential function in the generation of
CC       cytoplasmic iron-sulfur proteins by mediating export of Fe/S cluster
CC       precursors synthesized by NFS1 and other mitochondrial proteins. Not
CC       required for mitochondrial and plastid Fe-S enzymes. Probably involved
CC       in the export of cyclic pyranopterin monophosphate (cPMP) from
CC       mitochondria into the cytosol. Mediates glutathione-dependent
CC       resistance to heavy metals such as cadmium and lead, as well as their
CC       transport from roots to leaves. Regulates nonprotein thiols (NPSH) and
CC       the cellular level of glutathione (GSH). {ECO:0000269|PubMed:11158531,
CC       ECO:0000269|PubMed:16461380, ECO:0000269|PubMed:17517886,
CC       ECO:0000269|PubMed:19710232, ECO:0000269|PubMed:20164445}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:11158531, ECO:0000269|PubMed:14671022,
CC       ECO:0000269|PubMed:17517886}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:11158531,
CC       ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17517886}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in roots, leaves, stems,
CC       flowers and siliques. {ECO:0000269|PubMed:17517886}.
CC   -!- INDUCTION: In roots by cadmium and lead. {ECO:0000269|PubMed:16461380}.
CC   -!- DISRUPTION PHENOTYPE: Plants exhibit an enhanced sensitivity to
CC       cadmium, dwarfism and chlorosis, with an altered morphology of leaf and
CC       cell nuclei. Mitochondria accumulate nonheme, nonprotein iron.
CC       Decreased levels of molybdenum cofactor (MOCO) and reduced activities
CC       of cytosolic Fe-S proteins. Reduced ability to produce abscisic acid
CC       under normal conditions and in response to drought stress. Male
CC       sterility when homozygous. {ECO:0000269|PubMed:11158531,
CC       ECO:0000269|PubMed:16461380, ECO:0000269|PubMed:19710232,
CC       ECO:0000269|PubMed:20164445}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR   EMBL; AJ272202; CAB97048.1; -; mRNA.
DR   EMBL; AF287699; AAG09829.1; -; mRNA.
DR   EMBL; AB019228; BAA96918.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97027.1; -; Genomic_DNA.
DR   EMBL; AF360334; AAK26044.1; -; mRNA.
DR   EMBL; AY142686; AAN13224.1; -; mRNA.
DR   RefSeq; NP_200635.1; NM_125212.3.
DR   PDB; 7N58; EM; 3.40 A; A/B=1-728.
DR   PDB; 7N59; EM; 3.60 A; A/B=1-728.
DR   PDB; 7N5A; EM; 3.95 A; A/B=1-728.
DR   PDB; 7N5B; EM; 3.80 A; A/B=1-728.
DR   PDBsum; 7N58; -.
DR   PDBsum; 7N59; -.
DR   PDBsum; 7N5A; -.
DR   PDBsum; 7N5B; -.
DR   AlphaFoldDB; Q9LVM1; -.
DR   EMDB; EMD-24182; -.
DR   EMDB; EMD-24183; -.
DR   EMDB; EMD-24184; -.
DR   EMDB; EMD-24185; -.
DR   SMR; Q9LVM1; -.
DR   BioGRID; 21183; 7.
DR   IntAct; Q9LVM1; 5.
DR   STRING; 3702.Q9LVM1; -.
DR   TCDB; 3.A.1.210.8; the atp-binding cassette (abc) superfamily.
DR   MetOSite; Q9LVM1; -.
DR   PaxDb; 3702-AT5G58270-1; -.
DR   ProteomicsDB; 244536; -.
DR   EnsemblPlants; AT5G58270.1; AT5G58270.1; AT5G58270.
DR   GeneID; 835939; -.
DR   Gramene; AT5G58270.1; AT5G58270.1; AT5G58270.
DR   KEGG; ath:AT5G58270; -.
DR   Araport; AT5G58270; -.
DR   TAIR; AT5G58270; ABCB25.
DR   eggNOG; KOG0057; Eukaryota.
DR   HOGENOM; CLU_000604_84_1_1; -.
DR   InParanoid; Q9LVM1; -.
DR   OMA; VFHIIPI; -.
DR   OrthoDB; 2876209at2759; -.
DR   PhylomeDB; Q9LVM1; -.
DR   BioCyc; ARA:AT5G58270-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   PRO; PR:Q9LVM1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVM1; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0009536; C:plastid; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR   GO; GO:0051276; P:chromosome organization; IMP:TAIR.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:0050790; P:regulation of catalytic activity; IMP:TAIR.
DR   GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:TAIR.
DR   GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR   GO; GO:0010288; P:response to lead ion; IMP:TAIR.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
DR   CDD; cd18582; ABC_6TM_ATM1_ABCB7; 1.
DR   CDD; cd03253; ABCC_ATM1_transporter; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF402; IRON-SULFUR CLUSTERS TRANSPORTER ABCB7, MITOCHONDRIAL; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Ion transport; Iron; Iron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..97
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           98..728
FT                   /note="ABC transporter B family member 25, mitochondrial"
FT                   /id="PRO_0000379134"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          143..445
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          479..713
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          89..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         488
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         512..523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MUTAGEN         612
FT                   /note="R->K: Resistant to sirtinol and reduced chlorophyll
FT                   content."
FT                   /evidence="ECO:0000269|PubMed:19710232"
FT   CONFLICT        328
FT                   /note="R -> S (in Ref. 1; CAB97048)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="A -> D (in Ref. 1; CAB97048)"
FT                   /evidence="ECO:0000305"
FT   HELIX           118..131
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           137..168
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   TURN            169..175
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           198..244
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           247..252
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           255..278
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           280..291
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           292..295
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           300..347
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           349..354
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           361..410
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           419..430
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           433..437
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           439..456
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          479..486
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          488..491
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          494..498
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          507..512
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           520..525
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          535..540
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   TURN            543..545
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           548..554
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          566..568
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           569..574
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          577..579
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           582..592
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           595..598
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   TURN            602..605
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          608..610
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           618..632
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          635..639
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           648..661
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          663..665
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          667..673
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   TURN            674..676
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          680..687
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   STRAND          690..695
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           697..701
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   TURN            702..704
FT                   /evidence="ECO:0007829|PDB:7N58"
FT   HELIX           706..715
FT                   /evidence="ECO:0007829|PDB:7N58"
SQ   SEQUENCE   728 AA;  80420 MW;  A1FDD5C518E11B50 CRC64;
     MSRGSRFVRA PGLLLCRVNL QPQPKIPSFS YSLRSDYRLH NGFSNYIRRN SIRTSPVINA
     FLSDNSPSPS PSPSPIRFVQ RSSMLNGRLF STSTPNPDQT TTKTKEIKTT SSDSDSAMAD
     MKILRTLAGY LWMRDNPEFR FRVIAALGFL VGAKVLNVQV PFLFKLAVDW LASATGTGAS
     LTTFAATNPT LLTVFATPAA VLIGYGIART GSSAFNELRT AVFSKVALRT IRSVSRKVFS
     HLHDLDLRYH LSRETGGLNR IIDRGSRAIN FILSAMVFNV VPTILEISMV SGILAYKFGA
     AFAWITSLSV GSYIVFTLAV TQWRTKFRKA MNKADNDAST RAIDSLINYE TVKYFNNEGY
     EAEKYDQFLK KYEDAALQTQ RSLAFLNFGQ SIIFSTALST AMVLCSQGIM NGQMTVGDLV
     MVNGLLFQLS LPLNFLGSVY RETIQSLVDM KSMFQLLEEK SDITNTSDAK PLVLKGGNIE
     FENVHFSYLP ERKILDGISF VVPAGKSVAI VGTSGSGKST ILRMLFRFFD TDSGNIRIDG
     QDIKEVRLDS LRSSIGVVPQ DTVLFNDTIF HNIHYGRLSA TEEEVYEAAR RAAIHETISN
     FPDKYSTIVG ERGLKLSGGE KQRVALARTF LKSPAILLCD EATSALDSTT EAEILNALKA
     LASNRTSIFI AHRLTTAMQC DEIVVLENGK VVEQGPHDEL LGKSGRYAQL WTQQNSSVDM
     LDAAIKLE
//