ATPG_BOVIN
ID ATPG_BOVIN Reviewed; 298 AA.
AC P05631; Q3T0B4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit gamma {ECO:0000250|UniProtKB:P36542};
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATP5F1C {ECO:0000250|UniProtKB:P36542}; Synonyms=ATP5C, ATP5C1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2526651; DOI=10.1021/bi00435a008;
RA Dyer M.R., Gay N.J., Powell S.J., Walker J.E.;
RT "ATP synthase from bovine mitochondria: complementary DNA sequence of the
RT mitochondrial import precursor of the gamma-subunit and the genomic
RT sequence of the mature protein.";
RL Biochemistry 28:3670-3680(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 174-297, PROTEIN SEQUENCE OF 26-297, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=2864455; DOI=10.1016/0022-2836(85)90313-4;
RA Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D.,
RA Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.;
RT "Primary structure and subunit stoichiometry of F1-ATPase from bovine
RT mitochondria.";
RL J. Mol. Biol. 184:677-701(1985).
RN [4]
RP PROTEIN SEQUENCE OF 26-30, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 286-298, AND ALTERNATIVE SPLICING.
RC TISSUE=Heart, and Liver;
RX PubMed=8391483; DOI=10.1016/0014-5793(93)81089-i;
RA Matsuda C., Endo H., Hirata H., Morosawa H., Nakanishi M., Kagawa Y.;
RT "Tissue-specific isoforms of the bovine mitochondrial ATP synthase gamma-
RT subunit.";
RL FEBS Lett. 325:281-284(1993).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=95168; DOI=10.1007/bf02785056;
RA Sikerwar S.S., Malhotra S.K.;
RT "Visualization of mitochondrial coupling factor F1(ATPase) by freeze-
RT drying.";
RL Cell Biophys. 1:55-63(1979).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14633978; DOI=10.1093/emboj/cdg608;
RA Rubinstein J.L., Walker J.E., Henderson R.;
RT "Structure of the mitochondrial ATP synthase by electron cryomicroscopy.";
RL EMBO J. 22:6182-6192(2003).
RN [8]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=23407638; DOI=10.1098/rsob.120160;
RA Runswick M.J., Bason J.V., Montgomery M.G., Robinson G.C., Fearnley I.M.,
RA Walker J.E.;
RT "The affinity purification and characterization of ATP synthase complexes
RT from mitochondria.";
RL Open Biol. 3:120160-120160(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=8065448; DOI=10.1038/370621a0;
RA Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.;
RT "Structure at 2.8-A resolution of F1-ATPase from bovine heart
RT mitochondria.";
RL Nature 370:621-628(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=8790345; DOI=10.1073/pnas.93.18.9420;
RA Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G.,
RA Walker J.E.;
RT "The structure of bovine F1-ATPase complexed with the peptide antibiotic
RT efrapeptin.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=9687365; DOI=10.1016/s0969-2126(98)00085-9;
RA Orriss G.L., Leslie A.G., Braig K., Walker J.E.;
RT "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan:
RT the structure provides further support for a rotary catalytic mechanism.";
RL Structure 6:831-837(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1;
RP ATP5F1A AND ATP5F1B, AND SUBUNIT.
RX PubMed=12923572; DOI=10.1038/nsb966;
RA Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "The structure of bovine F1-ATPase in complex with its regulatory protein
RT IF1.";
RL Nat. Struct. Biol. 10:744-750(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1;
RP ATP5F1A; ATP5F1B; ATP5F1D AND ATP5F1E, AND SUBUNIT.
RX PubMed=17895376; DOI=10.1073/pnas.0707326104;
RA Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007).
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. Part of the complex
CC F(1) domain and the central stalk which is part of the complex rotary
CC element. The gamma subunit protrudes into the catalytic domain formed
CC of alpha(3)beta(3). Rotation of the central stalk against the
CC surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC three separate catalytic sites on the beta subunits.
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. 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. {ECO:0000269|PubMed:12923572, ECO:0000269|PubMed:17570365,
CC ECO:0000269|PubMed:17895376, ECO:0000269|PubMed:1827992,
CC ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:25851905,
CC ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448,
CC ECO:0000269|PubMed:8790345, ECO:0000269|PubMed:9687365}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:1827992,
CC ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455,
CC ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14633978,
CC ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455,
CC ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Matrix side
CC {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Liver; Synonyms=L;
CC IsoId=P05631-1; Sequence=Displayed;
CC Name=Heart; Synonyms=H;
CC IsoId=P05631-2; Sequence=VSP_000438;
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; X55389; CAA39064.1; -; mRNA.
DR EMBL; M22463; AAA30398.1; -; Genomic_DNA.
DR EMBL; BC102466; AAI02467.1; -; mRNA.
DR PIR; A32019; PWBOG.
DR RefSeq; NP_001068604.1; NM_001075136.2.
DR RefSeq; XP_005214178.1; XM_005214121.3. [P05631-2]
DR RefSeq; XP_005214179.1; XM_005214122.3. [P05631-2]
DR PDB; 1BMF; X-ray; 2.85 A; G=26-297.
DR PDB; 1COW; X-ray; 3.10 A; G=26-297.
DR PDB; 1E1Q; X-ray; 2.61 A; G=26-297.
DR PDB; 1E1R; X-ray; 2.50 A; G=26-297.
DR PDB; 1E79; X-ray; 2.40 A; G=26-297.
DR PDB; 1EFR; X-ray; 3.10 A; G=26-297.
DR PDB; 1H8E; X-ray; 2.00 A; G=26-297.
DR PDB; 1H8H; X-ray; 2.90 A; G=26-297.
DR PDB; 1NBM; X-ray; 3.00 A; G=26-297.
DR PDB; 1OHH; X-ray; 2.80 A; G=26-297.
DR PDB; 1QO1; X-ray; 3.90 A; G=26-69, G=102-115, G=234-297.
DR PDB; 1W0J; X-ray; 2.20 A; G=26-297.
DR PDB; 1W0K; X-ray; 2.85 A; G=26-297.
DR PDB; 2CK3; X-ray; 1.90 A; G=26-297.
DR PDB; 2JDI; X-ray; 1.90 A; G=26-298.
DR PDB; 2JIZ; X-ray; 2.30 A; G/N=26-297.
DR PDB; 2JJ1; X-ray; 2.70 A; G/N=26-297.
DR PDB; 2JJ2; X-ray; 2.40 A; G/N=26-297.
DR PDB; 2V7Q; X-ray; 2.10 A; G=26-297.
DR PDB; 2W6E; X-ray; 6.50 A; G=1-298.
DR PDB; 2W6F; X-ray; 6.00 A; G=1-298.
DR PDB; 2W6G; X-ray; 6.00 A; G=1-298.
DR PDB; 2W6H; X-ray; 5.00 A; G=1-298.
DR PDB; 2W6I; X-ray; 4.00 A; G=1-298.
DR PDB; 2W6J; X-ray; 3.84 A; G=1-298.
DR PDB; 2WSS; X-ray; 3.20 A; G/P=26-297.
DR PDB; 2XND; X-ray; 3.50 A; G=26-297.
DR PDB; 4ASU; X-ray; 2.60 A; G=26-298.
DR PDB; 4TSF; X-ray; 3.20 A; G=26-298.
DR PDB; 4TT3; X-ray; 3.21 A; G=26-298.
DR PDB; 4YXW; X-ray; 3.10 A; G=26-298.
DR PDB; 4Z1M; X-ray; 3.30 A; G=26-298.
DR PDB; 5ARA; EM; 6.70 A; G=26-298.
DR PDB; 5ARE; EM; 7.40 A; G=26-298.
DR PDB; 5ARH; EM; 7.20 A; G=26-298.
DR PDB; 5ARI; EM; 7.40 A; G=26-298.
DR PDB; 5FIJ; EM; 7.40 A; G=26-298.
DR PDB; 5FIK; EM; 6.40 A; G=26-298.
DR PDB; 5FIL; EM; 7.10 A; G=26-298.
DR PDB; 6TT7; EM; 3.50 A; G=1-298.
DR PDB; 6YY0; EM; 3.23 A; G=26-298.
DR PDB; 6Z1R; EM; 3.29 A; G=26-298.
DR PDB; 6Z1U; EM; 3.47 A; G=26-298.
DR PDB; 6ZG7; EM; 3.49 A; G=26-298.
DR PDB; 6ZG8; EM; 3.49 A; G=26-298.
DR PDB; 6ZIK; EM; 3.66 A; G=26-298.
DR PDB; 6ZPO; EM; 4.00 A; G=26-298.
DR PDB; 6ZQM; EM; 3.29 A; G=26-298.
DR PDB; 6ZQN; EM; 4.00 A; G=26-298.
DR PDB; 7AJB; EM; 9.20 A; AG/G=26-298.
DR PDB; 7AJC; EM; 11.90 A; AG/G=26-298.
DR PDB; 7AJD; EM; 9.00 A; AG/G=26-298.
DR PDB; 7AJE; EM; 9.40 A; AG/G=26-298.
DR PDB; 7AJF; EM; 8.45 A; AG/G=26-298.
DR PDB; 7AJG; EM; 10.70 A; AG/G=26-298.
DR PDB; 7AJH; EM; 9.70 A; AG/G=26-298.
DR PDB; 7AJI; EM; 11.40 A; AG/G=26-298.
DR PDB; 7AJJ; EM; 13.10 A; AG/G=26-298.
DR PDBsum; 1BMF; -.
DR PDBsum; 1COW; -.
DR PDBsum; 1E1Q; -.
DR PDBsum; 1E1R; -.
DR PDBsum; 1E79; -.
DR PDBsum; 1EFR; -.
DR PDBsum; 1H8E; -.
DR PDBsum; 1H8H; -.
DR PDBsum; 1NBM; -.
DR PDBsum; 1OHH; -.
DR PDBsum; 1QO1; -.
DR PDBsum; 1W0J; -.
DR PDBsum; 1W0K; -.
DR PDBsum; 2CK3; -.
DR PDBsum; 2JDI; -.
DR PDBsum; 2JIZ; -.
DR PDBsum; 2JJ1; -.
DR PDBsum; 2JJ2; -.
DR PDBsum; 2V7Q; -.
DR PDBsum; 2W6E; -.
DR PDBsum; 2W6F; -.
DR PDBsum; 2W6G; -.
DR PDBsum; 2W6H; -.
DR PDBsum; 2W6I; -.
DR PDBsum; 2W6J; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 2XND; -.
DR PDBsum; 4ASU; -.
DR PDBsum; 4TSF; -.
DR PDBsum; 4TT3; -.
DR PDBsum; 4YXW; -.
DR PDBsum; 4Z1M; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6TT7; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZG7; -.
DR PDBsum; 6ZG8; -.
DR PDBsum; 6ZIK; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P05631; -.
DR SMR; P05631; -.
DR CORUM; P05631; -.
DR DIP; DIP-47546N; -.
DR IntAct; P05631; 5.
DR MINT; P05631; -.
DR STRING; 9913.ENSBTAP00000018505; -.
DR BindingDB; P05631; -.
DR ChEMBL; CHEMBL612444; -.
DR iPTMnet; P05631; -.
DR PaxDb; P05631; -.
DR PeptideAtlas; P05631; -.
DR PRIDE; P05631; -.
DR Ensembl; ENSBTAT00000018505; ENSBTAP00000018505; ENSBTAG00000013930. [P05631-1]
DR Ensembl; ENSBTAT00000076091; ENSBTAP00000060497; ENSBTAG00000013930. [P05631-2]
DR Ensembl; ENSBTAT00000081996; ENSBTAP00000064321; ENSBTAG00000013930. [P05631-1]
DR GeneID; 327668; -.
DR KEGG; bta:327668; -.
DR CTD; 509; -.
DR VEuPathDB; HostDB:ENSBTAG00000013930; -.
DR eggNOG; KOG1531; Eukaryota.
DR GeneTree; ENSGT00390000006837; -.
DR HOGENOM; CLU_050669_4_0_1; -.
DR InParanoid; P05631; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 841252at2759; -.
DR TreeFam; TF105765; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P05631; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000013930; Expressed in cardiac ventricle and 106 other tissues.
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); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
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; IEA:Ensembl.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP synthesis; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:2864455"
FT CHAIN 26..298
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002684"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 154
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 154
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P36542"
FT MOD_RES 270
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT VAR_SEQ 298
FT /note="Missing (in isoform Heart)"
FT /evidence="ECO:0000305"
FT /id="VSP_000438"
FT CONFLICT 249
FT /note="E -> G (in Ref. 2; AAI02467)"
FT /evidence="ECO:0000305"
FT HELIX 28..60
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6ZG7"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6ZG7"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6YY0"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6ZG7"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 235..295
FT /evidence="ECO:0007829|PDB:1W0K"
SQ SEQUENCE 298 AA; 33072 MW; C1F41767CDABAD92 CRC64;
MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE
RELKPARVYG VGSLALYEKA DIKTPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKSEAAN
LAAAGKEVKI IGVGDKIRSI LHRTHSDQFL VTFKEVGRRP PTFGDASVIA LELLNSGYEF
DEGSIIFNRF RSVISYKTEE KPIFSLDTIS SAESMSIYDD IDADVLRNYQ EYSLANIIYY
SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
