ID ACADM_RAT Reviewed; 421 AA.
AC P08503;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|PubMed:2029527};
DE Short=MCAD {ECO:0000303|PubMed:2029527};
DE EC=1.3.8.7 {ECO:0000269|PubMed:3968063};
DE Flags: Precursor;
GN Name=Acadm {ECO:0000312|RGD:2012};
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND TRANSIT PEPTIDE.
RC TISSUE=Liver;
RX PubMed=3611054; DOI=10.1016/s0021-9258(18)61083-x;
RA Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y.,
RA Mole J., Rosenberg L.E., Tanaka K.;
RT "Molecular cloning and nucleotide sequence of cDNA encoding the entire
RT precursor of rat liver medium chain acyl coenzyme A dehydrogenase.";
RL J. Biol. Chem. 262:10104-10108(1987).
RN [2]
RP PROTEIN SEQUENCE OF 11-81.
RX PubMed=2029527; DOI=10.1016/0167-4838(91)90542-8;
RA Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.;
RT "Structurally different rat liver medium-chain acyl CoA dehydrogenases
RT directed by complementary DNAs differing in their 5'-region.";
RL Biochim. Biophys. Acta 1077:285-290(1991).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=3968063; DOI=10.1016/s0021-9258(20)71245-7;
RA Ikeda Y., Okamura-Ikeda K., Tanaka K.;
RT "Purification and characterization of short-chain, medium-chain, and long-
RT chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the
RT holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.";
RL J. Biol. Chem. 260:1311-1325(1985).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=3813556; DOI=10.1016/0003-9861(87)90072-5;
RA Ikeda Y., Keese S.M., Fenton W.A., Tanaka K.;
RT "Biosynthesis of four rat liver mitochondrial acyl-CoA dehydrogenases: in
RT vitro synthesis, import into mitochondria, and processing of their
RT precursors in a cell-free system and in cultured cells.";
RL Arch. Biochem. Biophys. 252:662-674(1987).
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:3968063). 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:3968063). 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 (PubMed:3968063). {ECO:0000250|UniProtKB:P11310,
CC ECO:0000269|PubMed:3968063}.
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:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478;
CC Evidence={ECO:0000305|PubMed:3968063};
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:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000305|PubMed:3968063};
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:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000305|PubMed:3968063};
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:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC Evidence={ECO:0000305|PubMed:3968063};
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:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000305|PubMed:3968063};
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:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000305|PubMed:3968063};
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:3968063};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=135 uM for butanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=39.6 uM for pentanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=9.4 uM for hexanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=4 uM for octanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=5.4 uM for decanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=5.7 uM for dodecanoyl-CoA {ECO:0000269|PubMed:3968063};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:3968063}.
CC -!- SUBUNIT: Homotetramer (PubMed:3968063, PubMed:3813556). Interacts with
CC the heterodimeric electron transfer flavoprotein ETF (By similarity).
CC {ECO:0000250|UniProtKB:P11310, ECO:0000269|PubMed:3813556,
CC ECO:0000269|PubMed:3968063}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:3813556,
CC ECO:0000269|PubMed:3968063}.
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; J02791; AAA40670.1; -; mRNA.
DR PIR; A28436; DERTCM.
DR RefSeq; NP_058682.2; NM_016986.2.
DR AlphaFoldDB; P08503; -.
DR SMR; P08503; -.
DR BioGRID; 246350; 1.
DR IntAct; P08503; 1.
DR STRING; 10116.ENSRNOP00000013238; -.
DR ChEMBL; CHEMBL2176828; -.
DR GlyGen; P08503; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08503; -.
DR PhosphoSitePlus; P08503; -.
DR jPOST; P08503; -.
DR PaxDb; 10116-ENSRNOP00000013238; -.
DR Ensembl; ENSRNOT00055049201; ENSRNOP00055040485; ENSRNOG00055028387.
DR Ensembl; ENSRNOT00060002450; ENSRNOP00060001585; ENSRNOG00060001604.
DR Ensembl; ENSRNOT00065020681; ENSRNOP00065015918; ENSRNOG00065012684.
DR GeneID; 24158; -.
DR KEGG; rno:24158; -.
DR AGR; RGD:2012; -.
DR CTD; 34; -.
DR RGD; 2012; Acadm.
DR eggNOG; KOG0140; Eukaryota.
DR InParanoid; P08503; -.
DR OrthoDB; 275353at2759; -.
DR PhylomeDB; P08503; -.
DR Reactome; R-RNO-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR Reactome; R-RNO-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-RNO-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR SABIO-RK; P08503; -.
DR UniPathway; UPA00660; -.
DR PRO; PR:P08503; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:RGD.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
DR GO; GO:0016853; F:isomerase activity; IDA:RGD.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0045329; P:carnitine biosynthetic process; ISO:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISO:RGD.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; ISO:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IDA:RGD.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISO:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR CDD; cd01157; MCAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf.
DR InterPro; IPR034180; MCAD.
DR PANTHER; PTHR48083:SF2; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
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; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3611054"
FT CHAIN 26..421
FT /note="Medium-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000506"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41367"
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:0000250|UniProtKB:P41367"
FT BINDING 167
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
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:0000250|UniProtKB:P41367"
FT BINDING 216
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 278
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 281
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 306..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P41367"
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:0000250|UniProtKB:P41367"
FT BINDING 349
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 351
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 374..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P41367"
FT BINDING 401
FT /ligand="octanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57386"
FT /evidence="ECO:0000250|UniProtKB:P41367"
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:0000250|UniProtKB:P41367"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
FT MOD_RES 69
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45952"
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 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P45952"
SQ SEQUENCE 421 AA; 46555 MW; 2CF076F8C919BDE8 CRC64;
MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT IARKFAREEI
IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL GTFDACLITE ELAYGCTGVQ
TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG
DEYVINGQKM WITNGGKANW YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM
GQRCSDTRGI TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYFASIAKAF
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK
N
//
