ATPA_PIG
ID ATPA_PIG Reviewed; 553 AA.
AC P80021; B2ZF46; Q29596;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit alpha {ECO:0000250|UniProtKB:P25705};
DE AltName: Full=ATP synthase subunit alpha heart isoform, mitochondrial;
DE AltName: Full=ATP synthase subunit alpha liver isoform, mitochondrial;
DE Flags: Precursor;
GN Name=ATP5F1A {ECO:0000250|UniProtKB:P25705}; Synonyms=ATP5A1, ATP5A2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu G.Y.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-148.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [3]
RP PROTEIN SEQUENCE OF 88-112 AND 127-133, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RX PubMed=1714390; DOI=10.1111/j.1432-1033.1991.tb16169.x;
RA Moradi-Ameli M., Clerc F.F., Cieur F., Seiberras G., Godinot C.;
RT "Localization on the mitochondrial F1 ATPase alpha subunit of an epitope
RT masked in the membrane-bound enzyme using a monoclonal antibody and
RT synthetic peptides.";
RL Eur. J. Biochem. 199:671-676(1991).
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). Binds the bacterial siderophore enterobactin and can
CC promote mitochondrial accumulation of enterobactin-derived iron ions
CC (By similarity). {ECO:0000250|UniProtKB:P19483,
CC ECO:0000250|UniProtKB:P25705}.
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) (PubMed:1714390).
CC CF(0) has three main subunits: a, b and c (By similarity). Interacts
CC with ATPAF2. Interacts with HRG; the interaction occurs on the surface
CC of T-cells and alters the cell morphology when associated with
CC concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the
CC interaction inhibits most of the angiogenic properties of angiostatin
CC (By similarity). Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). Interacts with BLOC1S1 (By similarity).
CC Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the
CC association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane
CC F(1)F(0) ATP synthase and enhances neurons metabolic efficiency (By
CC similarity). Interacts with CLN5 and PPT1 (By similarity). Interacts
CC with S100A1; this interaction increases F1-ATPase activity (By
CC similarity). Interacts with ABCB7; this interaction allows the
CC regulation of cellular iron homeostasis and cellular reactive oxygen
CC species (ROS) levels in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:P15999, ECO:0000250|UniProtKB:P19483,
CC ECO:0000250|UniProtKB:P25705, ECO:0000250|UniProtKB:Q03265,
CC ECO:0000269|PubMed:1714390}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1714390}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side
CC {ECO:0000250|UniProtKB:P19483}. Cell membrane
CC {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P25705}; Extracellular side
CC {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell
CC surface of T-cells. {ECO:0000250|UniProtKB:P25705}.
CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level).
CC {ECO:0000269|PubMed:1714390}.
CC -!- PTM: Acetylated on lysine residues. BLOC1S1 is required for
CC acetylation. {ECO:0000250|UniProtKB:P25705}.
CC -!- MISCELLANEOUS: The siderophore enterobactin (Ent) produced by enteric
CC bacteria binds Fe(3+) and helps bacteria scavenge iron ions from the
CC environment. As a consequence, the mammalian siderocalin LCN2 plays an
CC important role in defense against bacterial infections by sequestering
CC iron bound to microbial siderophores. LCN2 can also bind iron bound to
CC endogenous or nutrient-derived iron chelators and plays an important
CC role in cellular iron homeostasis. Enterobactin produced by non-
CC pathogenic E.coli strains can facilitate mitochondrial iron
CC assimilation, suggesting that iron bound to siderophores from non-
CC pathogenic bacteria may contribute to iron absorption by the host.
CC {ECO:0000250|UniProtKB:P25705}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; EU650784; ACD02421.1; -; mRNA.
DR EMBL; F14580; CAA23135.1; -; mRNA.
DR RefSeq; NP_001172071.1; NM_001185142.1.
DR PDB; 6J5I; EM; 3.34 A; A/B/C=45-553.
DR PDB; 6J5J; EM; 3.45 A; A/B/C=45-553.
DR PDB; 6J5K; EM; 6.20 A; A/AA/AB/AC/B/BA/BB/BC/C/CA/CB/CC=45-553.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR AlphaFoldDB; P80021; -.
DR BMRB; P80021; -.
DR SMR; P80021; -.
DR IntAct; P80021; 1.
DR STRING; 9823.ENSSSCP00000004854; -.
DR PaxDb; P80021; -.
DR PeptideAtlas; P80021; -.
DR PRIDE; P80021; -.
DR Ensembl; ENSSSCT00000056853; ENSSSCP00000037224; ENSSSCG00000004499.
DR Ensembl; ENSSSCT00005032810; ENSSSCP00005019999; ENSSSCG00005019791.
DR Ensembl; ENSSSCT00015002210; ENSSSCP00015000682; ENSSSCG00015001140.
DR Ensembl; ENSSSCT00025068568; ENSSSCP00025029507; ENSSSCG00025050081.
DR Ensembl; ENSSSCT00030005808; ENSSSCP00030002440; ENSSSCG00030004377.
DR Ensembl; ENSSSCT00040026509; ENSSSCP00040011211; ENSSSCG00040018805.
DR Ensembl; ENSSSCT00050022813; ENSSSCP00050009661; ENSSSCG00050016724.
DR Ensembl; ENSSSCT00055036600; ENSSSCP00055029082; ENSSSCG00055018686.
DR Ensembl; ENSSSCT00055037105; ENSSSCP00055029486; ENSSSCG00055018686.
DR Ensembl; ENSSSCT00060053537; ENSSSCP00060022810; ENSSSCG00060039559.
DR Ensembl; ENSSSCT00065032385; ENSSSCP00065013310; ENSSSCG00065024259.
DR GeneID; 100157880; -.
DR KEGG; ssc:100157880; -.
DR CTD; 498; -.
DR VGNC; VGNC:109475; ATP5F1A.
DR eggNOG; KOG1353; Eukaryota.
DR GeneTree; ENSGT00550000074846; -.
DR HOGENOM; CLU_010091_2_1_1; -.
DR OrthoDB; 470054at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000004499; Expressed in psoas major muscle and 43 other tissues.
DR ExpressionAtlas; P80021; baseline and differential.
DR Genevisible; P80021; SS.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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; Acetylation; ATP synthesis; ATP-binding; Cell membrane;
KW CF(1); Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT CHAIN 44..553
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144412"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT BINDING 473..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19483"
FT SITE 413
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 76
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15999"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 167
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 167
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 204
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 230
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 305
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 305
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 498
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 498
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 506
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 506
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 531
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25705"
FT MOD_RES 539
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT MOD_RES 541
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q03265"
FT CARBOHYD 76
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 100
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="EE -> KD (in Ref. 2; CAA23135)"
FT /evidence="ECO:0000305"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6J5J"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6J5J"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6J5J"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6J5J"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 297..304
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 399..403
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 408..417
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 426..442
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 457..470
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 481..491
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 492..498
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 518..522
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 541..548
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 553 AA; 59688 MW; A66233929D65FF19 CRC64;
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VAARNLHASN TRLQKTGTAE VSSILEERIL
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYAPMA
IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ ALLGKIRADG KISEETDAKL
KEIVTNFLAG FEA
