ATPA_RAT
ID ATPA_RAT Reviewed; 553 AA.
AC P15999; Q6P753;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit alpha {ECO:0000250|UniProtKB:P25705};
DE Flags: Precursor;
GN Name=Atp5f1a {ECO:0000312|RGD:619993}; Synonyms=Atp5a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-553.
RC TISSUE=Liver;
RX PubMed=2137825; DOI=10.1016/s0021-9258(19)39614-0;
RA Lee J.H., Garboczi D.N., Thomas P.J., Pedersen P.L.;
RT "Mitochondrial ATP synthase. cDNA cloning, amino acid sequence,
RT overexpression, and properties of the rat liver alpha subunit.";
RL J. Biol. Chem. 265:4664-4669(1990).
RN [3]
RP PROTEIN SEQUENCE OF 46-58; 104-123; 134-161; 195-204; 335-347; 403-416;
RP 435-463; 467-493; 507-527 AND 540-553, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 319-553.
RC TISSUE=Muscle;
RA Frey B.A.J., Weber F.E., Fett R., Pette D.;
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [7]
RP INTERACTION WITH BCL2L1.
RX PubMed=21926988; DOI=10.1038/ncb2330;
RA Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S.,
RA Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M.,
RA Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J., Hardwick J.M.,
RA Jonas E.A.;
RT "Bcl-xL regulates metabolic efficiency of neurons through interaction with
RT the mitochondrial F1FO ATP synthase.";
RL Nat. Cell Biol. 13:1224-1233(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-134, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP GLYCOSYLATION AT SER-76.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
RN [10]
RP INTERACTION WITH ABCB7.
RX PubMed=31511561; DOI=10.1038/s41598-019-49666-0;
RA Kumar V., Kumar A., Sanawar R., Jaleel A., Santhosh Kumar T.R.,
RA Kartha C.C.;
RT "Chronic Pressure Overload Results in Deficiency of Mitochondrial Membrane
RT Transporter ABCB7 Which Contributes to Iron Overload, Mitochondrial
RT Dysfunction, Metabolic Shift and Worsens Cardiac Function.";
RL Sci. Rep. 9:13170-13170(2019).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-553, AND SUBUNIT.
RX PubMed=9736690; DOI=10.1073/pnas.95.19.11065;
RA Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.;
RT "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical
RT intermediate in ATP synthesis/hydrolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998).
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:17575325,
CC PubMed:9736690). CF(0) has three main subunits: a, b and c
CC (PubMed:17575325). Interacts with ATPAF2. Interacts with HRG; the
CC interaction occurs on the surface of T-cells and alters the cell
CC morphology when associated with concanavalin (in vitro). Interacts with
CC PLG (angiostatin peptide); the interaction inhibits most of the
CC angiogenic properties of angiostatin (By similarity). Component of an
CC ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts
CC with BLOC1S1 (By similarity). Interacts with BCL2L1 isoform BCL-X(L);
CC the interaction mediates the association of BCL2L1 isoform BCL-X(L)
CC with the mitochondrial membrane F(1)F(0) ATP synthase and enhances
CC neurons metabolic efficiency (PubMed:21926988). Interacts with CLN5 and
CC PPT1 (By similarity). Interacts with S100A1; this interaction increases
CC F1-ATPase activity (By similarity). Interacts with ABCB7; this
CC interaction allows the regulation of cellular iron homeostasis and
CC cellular reactive oxygen species (ROS) levels in cardiomyocytes
CC (PubMed:31511561). {ECO:0000250|UniProtKB:P19483,
CC ECO:0000250|UniProtKB:P25705, ECO:0000250|UniProtKB:Q03265,
CC ECO:0000269|PubMed:17575325, ECO:0000269|PubMed:21926988,
CC ECO:0000269|PubMed:31511561, ECO:0000269|PubMed:9736690}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17575325}.
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 flagella of epididymal sperm.
CC {ECO:0000269|PubMed:19423663}.
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; BC061830; AAH61830.1; -; mRNA.
DR EMBL; J05266; AAA40784.1; -; mRNA.
DR EMBL; X56133; CAA39599.1; -; mRNA.
DR PIR; A35730; A35730.
DR RefSeq; NP_075581.1; NM_023093.1.
DR PDB; 1MAB; X-ray; 2.80 A; A=44-553.
DR PDB; 2F43; X-ray; 3.00 A; A=44-553.
DR PDBsum; 1MAB; -.
DR PDBsum; 2F43; -.
DR AlphaFoldDB; P15999; -.
DR SMR; P15999; -.
DR BioGRID; 249327; 8.
DR CORUM; P15999; -.
DR IntAct; P15999; 12.
DR MINT; P15999; -.
DR STRING; 10116.ENSRNOP00000022892; -.
DR ChEMBL; CHEMBL2176795; -.
DR CarbonylDB; P15999; -.
DR GlyGen; P15999; 1 site.
DR iPTMnet; P15999; -.
DR PhosphoSitePlus; P15999; -.
DR World-2DPAGE; 0004:P15999; -.
DR jPOST; P15999; -.
DR PaxDb; P15999; -.
DR PRIDE; P15999; -.
DR Ensembl; ENSRNOT00000022892; ENSRNOP00000022892; ENSRNOG00000017032.
DR GeneID; 65262; -.
DR KEGG; rno:65262; -.
DR CTD; 498; -.
DR RGD; 619993; Atp5f1a.
DR eggNOG; KOG1353; Eukaryota.
DR GeneTree; ENSGT00550000074846; -.
DR InParanoid; P15999; -.
DR OrthoDB; 470054at2759; -.
DR PhylomeDB; P15999; -.
DR EvolutionaryTrace; P15999; -.
DR PRO; PR:P15999; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:CAFA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IDA:RGD.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; ISO:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0043532; F:angiostatin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
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_0000002427"
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:0007744|PubMed:22673903"
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:0000269|PubMed:24098488"
FT CONFLICT 11
FT /note="A -> R (in Ref. 2; AAA40784)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="Y -> D (in Ref. 4; CAA39599)"
FT /evidence="ECO:0000305"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2F43"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 424..429
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 430..443
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2F43"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 458..471
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 504..518
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 520..526
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 534..548
FT /evidence="ECO:0007829|PDB:1MAB"
SQ SEQUENCE 553 AA; 59754 MW; D48886ED1245302C CRC64;
MLSVRIAAAV ARALPRRAGL VSKNALGSSF VGTRNLHASN TRLQKTGTAE MSSILEERIL
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
NDKLIKEGDI VKRTGAIVDV PVGDELLGRV VDALGNAIDG KGPVGSKIRR RVGLKAPGII
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDSFG
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA
IEEQVAVIYA GVRGYLDKLE PSKITKFESA FLSHVVSQHQ SLLGNIRSDG KISEQSDAKL
KEIVTNFLAG FEP
