ACADM_PIG
ID ACADM_PIG Reviewed; 421 AA.
AC P41367; Q58XQ3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|PubMed:8356049};
DE Short=MCAD {ECO:0000303|PubMed:8356049};
DE EC=1.3.8.7 {ECO:0000269|PubMed:3233192};
DE Flags: Precursor;
GN Name=ACADM {ECO:0000303|PubMed:3233192};
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 Suzuki H., Kimura M., Ito T., Murakami Y., Hamasima N., Yasue H.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Jeon J.-T., Park J.-J., Kim J.-H., Lim H.-T., Seo B.-Y., Cho I.-C.;
RT "Mutation detection in the porcine ACADM gene.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 396-408, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP ACTIVE SITE.
RX PubMed=3233192; DOI=10.1021/bi00421a008;
RA Powell P.J., Thorpe C.;
RT "2-octynoyl coenzyme A is a mechanism-based inhibitor of pig kidney medium-
RT chain acyl coenzyme A dehydrogenase: isolation of the target peptide.";
RL Biochemistry 27:8022-8028(1988).
RN [4] {ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 36-420 IN COMPLEX WITH FAD AND
RP SUBSTRATE, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RC TISSUE=Liver;
RX PubMed=8356049; DOI=10.1073/pnas.90.16.7523;
RA Kim J.-J.P., Wang M., Paschke R.;
RT "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver
RT mitochondria with and without substrate.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7523-7527(1993).
RN [5] {ECO:0007744|PDB:1UDY}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-421 IN COMPLEX WITH FAD AND
RP SUBSTRATE ANALOG, COFACTOR, AND ACTIVE SITE.
RX PubMed=12966080; DOI=10.1093/jb/mvg143;
RA Satoh A., Nakajima Y., Miyahara I., Hirotsu K., Tanaka T., Nishina Y.,
RA Shiga K., Tamaoki H., Setoyama C., Miura R.;
RT "Structure of the transition state analog of medium-chain acyl-CoA
RT dehydrogenase. Crystallographic and molecular orbital studies on the
RT charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-
RT thiaoctanoyl-CoA.";
RL J. Biochem. 134:297-304(2003).
CC -!- FUNCTION: Medium-chain specific acyl-CoA dehydrogenase is one of the
CC acyl-CoA dehydrogenases that catalyze the first step of mitochondrial
CC fatty acid beta-oxidation, an aerobic process breaking down fatty acids
CC into acetyl-CoA and allowing the production of energy from fats
CC (PubMed:3233192). The first step of fatty acid beta-oxidation consists
CC in the removal of one hydrogen from C-2 and C-3 of the straight-chain
CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-
CC CoA (PubMed:3233192). Electron transfer flavoprotein (ETF) is the
CC electron acceptor that transfers electrons to the main mitochondrial
CC respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase)
CC (By similarity). Among the different mitochondrial acyl-CoA
CC dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts
CC specifically on acyl-CoAs with saturated 6 to 12 carbons long primary
CC chains (By similarity). {ECO:0000250|UniProtKB:P11310,
CC ECO:0000269|PubMed:3233192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7; Evidence={ECO:0000269|PubMed:3233192};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478;
CC Evidence={ECO:0000305|PubMed:3233192};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000250|UniProtKB:P08503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000250|UniProtKB:P08503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000269|PubMed:3233192};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC Evidence={ECO:0000305|PubMed:3233192};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12966080, ECO:0000269|PubMed:8356049};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:3233192}.
CC -!- SUBUNIT: Homotetramer (PubMed:12966080). Interacts with the
CC heterodimeric electron transfer flavoprotein ETF (By similarity).
CC {ECO:0000250|UniProtKB:P11310, ECO:0000269|PubMed:12966080}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P08503}.
CC -!- PTM: Acetylated. Could occur at proximity of the cofactor-binding sites
CC and reduce the catalytic activity. Could be deacetylated by SIRT3.
CC {ECO:0000250|UniProtKB:P11310}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U40845; AAA83759.1; -; mRNA.
DR EMBL; AY705916; AAW30430.1; -; mRNA.
DR RefSeq; NP_999204.1; NM_214039.1.
DR PDB; 1UDY; X-ray; 2.40 A; A/B/C/D=26-421.
DR PDB; 3MDD; X-ray; 2.40 A; A/B=36-420.
DR PDB; 3MDE; X-ray; 2.40 A; A/B=36-420.
DR PDBsum; 1UDY; -.
DR PDBsum; 3MDD; -.
DR PDBsum; 3MDE; -.
DR AlphaFoldDB; P41367; -.
DR SMR; P41367; -.
DR IntAct; P41367; 2.
DR STRING; 9823.ENSSSCP00000004085; -.
DR PaxDb; P41367; -.
DR PeptideAtlas; P41367; -.
DR PRIDE; P41367; -.
DR Ensembl; ENSSSCT00025019283; ENSSSCP00025007814; ENSSSCG00025014343.
DR Ensembl; ENSSSCT00070034689; ENSSSCP00070028978; ENSSSCG00070017536.
DR GeneID; 397104; -.
DR KEGG; ssc:397104; -.
DR CTD; 34; -.
DR eggNOG; KOG0140; Eukaryota.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; P41367; -.
DR OMA; AMEELFW; -.
DR OrthoDB; 589058at2759; -.
DR TreeFam; TF105020; -.
DR BRENDA; 1.3.8.7; 6170.
DR Reactome; R-SSC-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR Reactome; R-SSC-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-SSC-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR SABIO-RK; P41367; -.
DR UniPathway; UPA00660; -.
DR EvolutionaryTrace; P41367; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; P41367; SS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:Ensembl.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IEA:Ensembl.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR CDD; cd01157; MCAD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034180; MCAD.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P08503"
FT CHAIN 26..421
FT /note="Medium-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000505"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049"
FT BINDING 158..167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY,
FT ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:3233192, ECO:0000269|PubMed:8356049"
FT BINDING 191..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY,
FT ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:8356049"
FT BINDING 278..281
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049"
FT BINDING 306..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY,
FT ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE"
FT BINDING 316..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY,
FT ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12966080"
FT BINDING 374..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:8356049"
FT BINDING 402..405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12966080,
FT ECO:0000269|PubMed:8356049, ECO:0007744|PDB:1UDY,
FT ECO:0007744|PDB:3MDD, ECO:0007744|PDB:3MDE"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12966080"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 179
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 212
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 212
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 271
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT CONFLICT 8
FT /note="S -> G (in Ref. 1; AAA83759)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="E -> K (in Ref. 1; AAA83759)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="P -> S (in Ref. 1; AAA83759)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> G (in Ref. 1; AAA83759)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> D (in Ref. 1; AAA83759)"
FT /evidence="ECO:0000305"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3MDD"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 180..193
FT /evidence="ECO:0007829|PDB:1UDY"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 269..303
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 317..345
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 351..376
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1UDY"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1UDY"
FT HELIX 404..417
FT /evidence="ECO:0007829|PDB:1UDY"
SQ SEQUENCE 421 AA; 46485 MW; 73BC66092D5E02CB CRC64;
MAAMFRRSCR VLRSLSHFGW RSQHTKAVPQ CEPGSGFSFE LTEQQKEFQA TARKFAREEI
IPVAAEYDRT GEYPVPLLKR AWELGLMNTH IPESFGGLGL GIIDSCLITE ELAYGCTGVQ
TAIEANTLGQ VPLIIGGNYQ QQKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKEINM
GQRCSDTRGI VFEDVRVPKE NVLTGEGAGF KIAMGTFDKT RPPVAAGAVG LAQRALDEAT
KYALERKTFG KLLAEHQGIS FLLADMAMKV ELARLSYQRA AWEIDSGRRN TYYASIAKAY
AADIANQLAT DAVQVFGGNG FNTEYPVEKL MRDAKIYQIY EGTAQIQRII IAREHIGRYK
N
