ID   ATM1_YEAST              Reviewed;         690 AA.
AC   P40416; D6W0C8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000305};
DE            EC=7.-.-.- {ECO:0000269|PubMed:25006243};
DE   Flags: Precursor;
GN   Name=ATM1 {ECO:0000312|SGD:S000004916}; Synonyms=MDY {ECO:0000305};
GN   OrderedLocusNames=YMR301C; ORFNames=YM9952.03C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=JK9-3D alpha;
RX   PubMed=7828591; DOI=10.1002/j.1460-2075.1995.tb06989.x;
RA   Leighton J., Schatz G.;
RT   "An ABC transporter in the mitochondrial inner membrane is required for
RT   normal growth of yeast.";
RL   EMBO J. 14:188-195(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9428742; DOI=10.1016/s0014-5793(97)01414-2;
RA   Kispal G., Csere P., Guiard B., Lill R.;
RT   "The ABC transporter Atm1p is required for mitochondrial iron
RT   homeostasis.";
RL   FEBS Lett. 418:346-350(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   FUNCTION.
RX   PubMed=10406803; DOI=10.1093/emboj/18.14.3981;
RA   Kispal G., Csere P., Prohl C., Lill R.;
RT   "The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of
RT   cytosolic Fe/S proteins.";
RL   EMBO J. 18:3981-3989(1999).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   HOMODIMERIZATION, AND MUTAGENESIS OF LYS-475 AND GLU-598.
RX   PubMed=15225610; DOI=10.1016/j.febslet.2004.05.051;
RA   Chloupkova M., Reaves S.K., LeBard L.M., Koeller D.M.;
RT   "The mitochondrial ABC transporter Atm1p functions as a homodimer.";
RL   FEBS Lett. 569:65-69(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, TOPOLOGY, AND MUTAGENESIS OF ARG-216 AND LYS-475.
RX   PubMed=25006243; DOI=10.1074/jbc.m114.553438;
RA   Schaedler T.A., Thornton J.D., Kruse I., Schwarzlaender M., Meyer A.J.,
RA   van Veen H.W., Balk J.;
RT   "A conserved mitochondrial ATP-binding cassette transporter exports
RT   glutathione polysulfide for cytosolic metal cofactor assembly.";
RL   J. Biol. Chem. 289:23264-23274(2014).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31040179; DOI=10.1074/jbc.ra119.008600;
RA   Pandey A.K., Pain J., Dancis A., Pain D.;
RT   "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm
RT   for iron-sulfur cluster assembly and tRNA thiolation in yeast.";
RL   J. Biol. Chem. 294:9489-9502(2019).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 98-690 IN COMPLEX WITH
RP   GLUTATHIONE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND
RP   MUTAGENESIS OF 666-LEU--LEU-690.
RX   PubMed=24604199; DOI=10.1126/science.1246729;
RA   Srinivasan V., Pierik A.J., Lill R.;
RT   "Crystal structures of nucleotide-free and glutathione-bound mitochondrial
RT   ABC transporter Atm1.";
RL   Science 343:1137-1140(2014).
CC   -!- FUNCTION: Performs an essential function in the generation of
CC       cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export
CC       of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial
CC       proteins (PubMed:10406803, PubMed:31040179, PubMed:25006243).
CC       Hydrolyzes ATP (PubMed:25006243, PubMed:24604199). Binds glutathione
CC       and may function by transporting a glutathione-conjugated iron-sulfur
CC       compound (PubMed:24604199, PubMed:25006243, PubMed:31040179).
CC       {ECO:0000269|PubMed:10406803, ECO:0000269|PubMed:24604199,
CC       ECO:0000269|PubMed:25006243, ECO:0000269|PubMed:31040179}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=109 uM for glutathione disulfide {ECO:0000269|PubMed:25006243};
CC         Vmax=27.4 pmol/min/mg enzyme {ECO:0000269|PubMed:25006243};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24604199}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:7828591}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC       ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:25006243,
CC       ECO:0000269|PubMed:7828591}.
CC   -!- DISRUPTION PHENOTYPE: Impairs cytosolic iron-sulfur (Fe-S) cluster
CC       assembly and decreases cytosolic tRNA thiolation.
CC       {ECO:0000269|PubMed:31040179}.
CC   -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X82612; CAA57938.1; -; Genomic_DNA.
DR   EMBL; X81715; CAA57359.1; -; Genomic_DNA.
DR   EMBL; Z49212; CAA89134.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10202.1; -; Genomic_DNA.
DR   PIR; S54211; S54211.
DR   RefSeq; NP_014030.1; NM_001182810.1.
DR   PDB; 4MYC; X-ray; 3.06 A; A/B/C=98-690.
DR   PDB; 4MYH; X-ray; 3.38 A; A/B/C=98-690.
DR   PDB; 7PSL; EM; 3.30 A; A/B=92-690.
DR   PDB; 7PSM; EM; 3.40 A; A/B=92-690.
DR   PDB; 7PSN; EM; 2.90 A; A/B=92-690.
DR   PDBsum; 4MYC; -.
DR   PDBsum; 4MYH; -.
DR   PDBsum; 7PSL; -.
DR   PDBsum; 7PSM; -.
DR   PDBsum; 7PSN; -.
DR   AlphaFoldDB; P40416; -.
DR   EMDB; EMD-13613; -.
DR   EMDB; EMD-13614; -.
DR   EMDB; EMD-13615; -.
DR   SMR; P40416; -.
DR   BioGRID; 35481; 100.
DR   DIP; DIP-7617N; -.
DR   IntAct; P40416; 8.
DR   MINT; P40416; -.
DR   STRING; 4932.YMR301C; -.
DR   TCDB; 3.A.1.210.1; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; P40416; -.
DR   MaxQB; P40416; -.
DR   PaxDb; 4932-YMR301C; -.
DR   PeptideAtlas; P40416; -.
DR   EnsemblFungi; YMR301C_mRNA; YMR301C; YMR301C.
DR   GeneID; 855347; -.
DR   KEGG; sce:YMR301C; -.
DR   AGR; SGD:S000004916; -.
DR   SGD; S000004916; ATM1.
DR   VEuPathDB; FungiDB:YMR301C; -.
DR   eggNOG; KOG0057; Eukaryota.
DR   GeneTree; ENSGT00940000156281; -.
DR   HOGENOM; CLU_000604_84_1_1; -.
DR   InParanoid; P40416; -.
DR   OMA; VFHIIPI; -.
DR   OrthoDB; 2876209at2759; -.
DR   BioCyc; YEAST:G3O-32967-MONOMER; -.
DR   Reactome; R-SCE-1369007; Mitochondrial ABC transporters.
DR   BioGRID-ORCS; 855347; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P40416; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P40416; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IDA:UniProtKB.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR   GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IMP:UniProtKB.
DR   GO; GO:1902497; P:iron-sulfur cluster transmembrane transport; IMP:UniProtKB.
DR   GO; GO:1990542; P:mitochondrial transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..690
FT                   /note="Iron-sulfur clusters transporter ATM1,
FT                   mitochondrial"
FT                   /id="PRO_0000000258"
FT   TOPO_DOM        27..110
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        111..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..155
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        156..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..228
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        229..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..340
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        341..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..374
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   TRANSMEM        375..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..690
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0000269|PubMed:25006243"
FT   DOMAIN          111..401
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          436..672
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         280..284
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0007744|PDB:4MYH"
FT   BINDING         343..346
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:24604199,
FT                   ECO:0007744|PDB:4MYH"
FT   BINDING         393
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G506"
FT   BINDING         445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT   BINDING         469..480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MUTAGEN         216
FT                   /note="R->Q: Decreases ATP hydrolysis. Decreases
FT                   transporter activity."
FT                   /evidence="ECO:0000269|PubMed:25006243"
FT   MUTAGEN         475
FT                   /note="K->M: Loss of function; significant decrease in
FT                   ATP-binding; no homodimerization."
FT                   /evidence="ECO:0000269|PubMed:15225610"
FT   MUTAGEN         475
FT                   /note="Missing: Decreases ATP hydrolysis. Decreases
FT                   transporter activity."
FT                   /evidence="ECO:0000269|PubMed:25006243"
FT   MUTAGEN         598
FT                   /note="E->A: Loss of function; slight decrease in
FT                   ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:15225610"
FT   MUTAGEN         666..690
FT                   /note="Missing: Impairs protein stability."
FT                   /evidence="ECO:0000269|PubMed:24604199"
FT   CONFLICT        23
FT                   /note="I -> IRNHS (in Ref. 1; CAA57938)"
FT                   /evidence="ECO:0000305"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           105..139
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:7PSM"
FT   HELIX           152..200
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           211..232
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   TURN            233..236
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           237..252
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           257..303
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           305..309
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           314..366
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          367..370
FT                   /evidence="ECO:0007829|PDB:4MYH"
FT   HELIX           372..395
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           400..413
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          430..432
FT                   /evidence="ECO:0007829|PDB:4MYC"
FT   STRAND          436..443
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          445..448
FT                   /evidence="ECO:0007829|PDB:7PSM"
FT   STRAND          451..459
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          461..468
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           476..482
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          489..495
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           500..502
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           505..508
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          511..515
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          523..525
FT                   /evidence="ECO:0007829|PDB:4MYC"
FT   HELIX           526..530
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           531..533
FT                   /evidence="ECO:0007829|PDB:4MYC"
FT   HELIX           539..548
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           552..557
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   TURN            559..563
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          565..567
FT                   /evidence="ECO:0007829|PDB:4MYC"
FT   HELIX           568..570
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           575..589
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          592..598
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          601..603
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           605..616
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   TURN            621..623
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          625..629
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           633..635
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          640..646
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   STRAND          649..654
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           656..660
FT                   /evidence="ECO:0007829|PDB:7PSN"
FT   HELIX           666..675
FT                   /evidence="ECO:0007829|PDB:7PSN"
SQ   SEQUENCE   690 AA;  77522 MW;  009757811D331343 CRC64;
     MLLLPRCPVI GRIVRSKFRS GLIRNHSPVI FTVSKLSTQR PLLFNSAVNL WNQAQKDITH
     KKSVEQFSSA PKVKTQVKKT SKAPTLSELK ILKDLFRYIW PKGNNKVRIR VLIALGLLIS
     AKILNVQVPF FFKQTIDSMN IAWDDPTVAL PAAIGLTILC YGVARFGSVL FGELRNAVFA
     KVAQNAIRTV SLQTFQHLMK LDLGWHLSRQ TGGLTRAMDR GTKGISQVLT AMVFHIIPIS
     FEISVVCGIL TYQFGASFAA ITFSTMLLYS IFTIKTTAWR THFRRDANKA DNKAASVALD
     SLINFEAVKY FNNEKYLADK YNGSLMNYRD SQIKVSQSLA FLNSGQNLIF TTALTAMMYM
     GCTGVIGGNL TVGDLVLINQ LVFQLSVPLN FLGSVYRDLK QSLIDMETLF KLRKNEVKIK
     NAERPLMLPE NVPYDITFEN VTFGYHPDRK ILKNASFTIP AGWKTAIVGS SGSGKSTILK
     LVFRFYDPES GRILINGRDI KEYDIDALRK VIGVVPQDTP LFNDTIWENV KFGRIDATDE
     EVITVVEKAQ LAPLIKKLPQ GFDTIVGERG LMISGGEKQR LAIARVLLKN ARIMFFDEAT
     SALDTHTEQA LLRTIRDNFT SGSRTSVYIA HRLRTIADAD KIIVLDNGRV REEGKHLELL
     AMPGSLYREL WTIQEDLDHL ENELKDQQEL
//