位置:首页 > 蛋白库 > ACADM_RAT
ACADM_RAT
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   03-AUG-2022, entry version 165.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   iPTMnet; P08503; -.
DR   PhosphoSitePlus; P08503; -.
DR   jPOST; P08503; -.
DR   PaxDb; P08503; -.
DR   PRIDE; P08503; -.
DR   GeneID; 24158; -.
DR   KEGG; rno:24158; -.
DR   CTD; 34; -.
DR   RGD; 2012; Acadm.
DR   eggNOG; KOG0140; Eukaryota.
DR   InParanoid; P08503; -.
DR   OrthoDB; 589058at2759; -.
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; IDA: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; -; 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   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="substrate"
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="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         278..281
FT                   /ligand="substrate"
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         351
FT                   /ligand="substrate"
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         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   BINDING         413
FT                   /ligand="substrate"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024