ATPA_YEAST
ID ATPA_YEAST Reviewed; 545 AA.
AC P07251; D6VPQ6; Q92449;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE Flags: Precursor;
GN Name=ATP1; OrderedLocusNames=YBL099W; ORFNames=YBL0827;
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].
RX PubMed=2876995; DOI=10.1016/s0021-9258(18)66841-3;
RA Takeda M., Chen W.-J., Saltzgaber J., Douglas M.G.;
RT "Nuclear genes encoding the yeast mitochondrial ATPase complex. Analysis of
RT ATP1 coding the F1-ATPase alpha-subunit and its assembly.";
RL J. Biol. Chem. 261:15126-15133(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-291 AND THR-383.
RC STRAIN=ATCC 64665 / S288c / DC5;
RX PubMed=10744740; DOI=10.1074/jbc.275.14.10492;
RA Mabuchi T., Ichimura Y., Takeda M., Douglas M.G.;
RT "ASC1/RAS2 suppresses the growth-defect on glycerol caused by the atp1-2
RT mutation in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:10492-10497(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 340.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [10]
RP 3D-STRUCTURE MODELING.
RX PubMed=10576729; DOI=10.1126/science.286.5445.1700;
RA Stock D., Leslie A.G., Walker J.E.;
RT "Molecular architecture of the rotary motor in ATP synthase.";
RL Science 286:1700-1705(1999).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits. Subunit
CC alpha does not bear the catalytic high-affinity ATP-binding sites (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169}. Note=Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 41500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; J02603; AAA66888.1; -; Genomic_DNA.
DR EMBL; D88458; BAA13613.1; -; Genomic_DNA.
DR EMBL; D37948; BAA22508.1; -; Genomic_DNA.
DR EMBL; X79489; CAA56001.1; -; Genomic_DNA.
DR EMBL; Z35861; CAA84924.1; -; Genomic_DNA.
DR EMBL; AY692969; AAT92988.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07026.2; -; Genomic_DNA.
DR PIR; S45401; PWBYA.
DR RefSeq; NP_009453.2; NM_001178339.2.
DR PDB; 2HLD; X-ray; 2.80 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 2WPD; X-ray; 3.43 A; A/B/C=36-545.
DR PDB; 2XOK; X-ray; 3.01 A; A/B/C=1-545.
DR PDB; 3FKS; X-ray; 3.59 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 3OE7; X-ray; 3.19 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 3OEE; X-ray; 2.74 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 3OEH; X-ray; 3.00 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 3OFN; X-ray; 3.20 A; A/B/C/J/K/L/S/T/U=36-545.
DR PDB; 3ZIA; X-ray; 2.50 A; A/B/C/K/L/M=36-545.
DR PDB; 3ZRY; X-ray; 6.50 A; A/B/C=36-545.
DR PDB; 4B2Q; EM; 37.00 A; A/C/a/c=61-545, B/b=60-545.
DR PDB; 6B8H; EM; 3.60 A; B/C/K/W/X/n=36-545.
DR PDB; 6CP3; EM; 3.80 A; A/B/C=36-545.
DR PDB; 6CP6; EM; 3.60 A; A/B/C=36-545.
DR PDBsum; 2HLD; -.
DR PDBsum; 2WPD; -.
DR PDBsum; 2XOK; -.
DR PDBsum; 3FKS; -.
DR PDBsum; 3OE7; -.
DR PDBsum; 3OEE; -.
DR PDBsum; 3OEH; -.
DR PDBsum; 3OFN; -.
DR PDBsum; 3ZIA; -.
DR PDBsum; 3ZRY; -.
DR PDBsum; 4B2Q; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP6; -.
DR AlphaFoldDB; P07251; -.
DR SMR; P07251; -.
DR BioGRID; 32606; 188.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3025N; -.
DR IntAct; P07251; 115.
DR MINT; P07251; -.
DR STRING; 4932.YBL099W; -.
DR TCDB; 3.A.2.1.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P07251; -.
DR MaxQB; P07251; -.
DR PaxDb; P07251; -.
DR PRIDE; P07251; -.
DR EnsemblFungi; YBL099W_mRNA; YBL099W; YBL099W.
DR GeneID; 852177; -.
DR KEGG; sce:YBL099W; -.
DR SGD; S000000195; ATP1.
DR VEuPathDB; FungiDB:YBL099W; -.
DR eggNOG; KOG1353; Eukaryota.
DR GeneTree; ENSGT00550000074846; -.
DR HOGENOM; CLU_010091_2_1_1; -.
DR InParanoid; P07251; -.
DR OMA; LQAPGVM; -.
DR BioCyc; YEAST:G3O-28984-MON; -.
DR BRENDA; 7.1.2.2; 984.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR EvolutionaryTrace; P07251; -.
DR PRO; PR:P07251; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P07251; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT CHAIN 36..545
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000002433"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MUTAGEN 291
FT /note="G->D: In ATP1-2; growth-defect."
FT /evidence="ECO:0000269|PubMed:10744740"
FT MUTAGEN 383
FT /note="T->I: In ATP1-1; growth-defect."
FT /evidence="ECO:0000269|PubMed:10744740"
FT CONFLICT 311..313
FT /note="QAV -> ASL (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="L -> M (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> P (in Ref. 3; CAA56001 and 4; CAA84924)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="G -> A (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="E -> Q (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..483
FT /note="VPLIY -> SMII (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT CONFLICT 490..493
FT /note="LDGI -> SGWY (in Ref. 1; AAA66888)"
FT /evidence="ECO:0000305"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 124..137
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3OEE"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3OEE"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2WPD"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 418..437
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 449..465
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 488..492
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 498..512
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 514..523
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 528..542
FT /evidence="ECO:0007829|PDB:3ZIA"
SQ SEQUENCE 545 AA; 58608 MW; E8041D289B924696 CRC64;
MLARTAAIRS LSRTLINSTK AARPAAAALA STRRLASTKA QPTEVSSILE ERIKGVSDEA
NLNETGRVLA VGDGIARVFG LNNIQAEELV EFSSGVKGMA LNLEPGQVGI VLFGSDRLVK
EGELVKRTGN IVDVPVGPGL LGRVVDALGN PIDGKGPIDA AGRSRAQVKA PGILPRRSVH
EPVQTGLKAV DALVPIGRGQ RELIIGDRQT GKTAVALDTI LNQKRWNNGS DESKKLYCVY
VAVGQKRSTV AQLVQTLEQH DAMKYSIIVA ATASEAAPLQ YLAPFTAASI GEWFRDNGKH
ALIVYDDLSK QAVAYRQLSL LLRRPPGREA YPGDVFYLHS RLLERAAKLS EKEGSGSLTA
LPVIETQGGD VSAYIPTNVI SITDGQIFLE AELFYKGIRP AINVGLSVSR VGSAAQVKAL
KQVAGSLKLF LAQYREVAAF AQFGSDLDAS TKQTLVRGER LTQLLKQNQY SPLATEEQVP
LIYAGVNGHL DGIELSRIGE FESSFLSYLK SNHNELLTEI REKGELSKEL LASLKSATES
FVATF
