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Database: UniProt
Entry: P45953
LinkDB: P45953
Original site: P45953 
ID   ACADV_RAT               Reviewed;         655 AA.
AC   P45953;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   19-MAR-2014, entry version 116.
DE   RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=VLCAD;
DE            EC=1.3.8.9;
DE   Flags: Precursor;
GN   Name=Acadvl; Synonyms=Vlcad;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=8034667;
RA   Aoyama T., Ueno I., Kamijo T., Hashimoto T.;
RT   "Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial
RT   acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in
RT   long-chain fatty acid beta-oxidation system. cDNA and deduced amino
RT   acid sequence and distinct specificities of the cDNA-expressed
RT   protein.";
RL   J. Biol. Chem. 269:19088-19094(1994).
CC   -!- FUNCTION: Active toward esters of long-chain and very long chain
CC       fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA.
CC       Can accommodate substrate acyl chain lengths as long as 24
CC       carbons, but shows little activity for substrates of less than 12
CC       carbons.
CC   -!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + electron-transfer
CC       flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA +
CC       reduced electron-transfer flavoprotein.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
CC       oxidation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- PTM: S-nitrosylation at Cys-237 in liver improves catalytic
CC       efficiency (By similarity).
CC   -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
CC       of different substrate specificities are present in mammalian
CC       tissues.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; D30647; BAA06331.1; -; mRNA.
DR   PIR; A54872; A54872.
DR   RefSeq; NP_037023.1; NM_012891.2.
DR   UniGene; Rn.33319; -.
DR   ProteinModelPortal; P45953; -.
DR   SMR; P45953; 69-653.
DR   MINT; MINT-4996754; -.
DR   STRING; 10116.ENSRNOP00000024973; -.
DR   ChEMBL; CHEMBL2176830; -.
DR   PaxDb; P45953; -.
DR   PRIDE; P45953; -.
DR   GeneID; 25363; -.
DR   KEGG; rno:25363; -.
DR   UCSC; RGD:2014; rat.
DR   CTD; 37; -.
DR   RGD; 2014; Acadvl.
DR   eggNOG; COG1960; -.
DR   HOGENOM; HOG000131665; -.
DR   HOVERGEN; HBG050448; -.
DR   InParanoid; P45953; -.
DR   KO; K09479; -.
DR   UniPathway; UPA00660; -.
DR   NextBio; 606351; -.
DR   PRO; PR:P45953; -.
DR   Genevestigator; P45953; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; 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:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IDA:RGD.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:RGD.
DR   GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:RGD.
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_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
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; Complete proteome; Direct protein sequencing; FAD;
KW   Fatty acid metabolism; Flavoprotein; Isopeptide bond;
KW   Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   S-nitrosylation; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     40       Mitochondrion.
FT   CHAIN        41    655       Very long-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000518.
FT   NP_BIND     214    223       FAD (By similarity).
FT   NP_BIND     249    251       FAD (By similarity).
FT   NP_BIND     435    439       FAD (By similarity).
FT   NP_BIND     464    466       FAD (By similarity).
FT   REGION       41    482       Catalytic.
FT   REGION      338    341       Substrate binding (By similarity).
FT   REGION      462    463       Substrate binding (By similarity).
FT   REGION      483    516       Membrane-anchoring (Probable).
FT   ACT_SITE    462    462       Proton acceptor (By similarity).
FT   BINDING     223    223       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     366    366       FAD (By similarity).
FT   BINDING     463    463       Substrate; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      51     51       N6-acetyllysine (By similarity).
FT   MOD_RES      71     71       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      71     71       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     127    127       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     127    127       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     195    195       N6-succinyllysine (By similarity).
FT   MOD_RES     237    237       S-nitrosocysteine (By similarity).
FT   MOD_RES     239    239       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     239    239       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     268    268       N6-succinyllysine (By similarity).
FT   MOD_RES     276    276       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     276    276       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     278    278       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     278    278       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     298    298       N6-acetyllysine (By similarity).
FT   MOD_RES     316    316       N6-acetyllysine (By similarity).
FT   MOD_RES     331    331       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     331    331       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     372    372       N6-succinyllysine (By similarity).
FT   MOD_RES     482    482       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     482    482       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     550    550       N6-acetyllysine (By similarity).
FT   MOD_RES     556    556       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     556    556       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     639    639       N6-succinyllysine (By similarity).
FT   CROSSLNK    331    331       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
SQ   SEQUENCE   655 AA;  70749 MW;  E808EDEB0E4595D7 CRC64;
     MQSARMTPSV GRQLLRLGAR SSRSAALQGQ PRPTSAQRLY ASEATQAVLE KPETLSSDAS
     TREKPARAES KSFAVGMFKG QLTTDQVFPY PSVLNEGQTQ FLKELVGPVA RFFEEVNDPA
     KNDSLEKVEE DTLQGLKELG AFGLQVPSEL GGLGLSNTQY ARLAEIVGMH DLGVSVTLGA
     HQSIGFKGIL LYGTKAQKEK YLPRVASGQA LAAFCLTEPS SGSDVASIRS SAVPSPCGKY
     YTLNGSKIWI SNGGLADIFT VFAKTPIKDA ATGAVKEKIT AFVVERSFGG VTHGLPEKKM
     GIKASNTSEV YFDGVKVPAE NVLGEVGDGF KVAVNILNNG RFGMAATLAG TMKAIIAKAV
     DHATNRTQFG DKIHNFGVIQ EKLARMAILQ YVTESMAYML SANMDQGFKD FQIEAAISKI
     FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDIRIFRI FEGTNDILRL FVALQGCMDK
     GKELTGLGNA LKNPLGNVGL LIGEASKQLR RRTGIGSGLS LSGIVHPELS RSGELAVQAL
     EQFATVVEAK LMKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGYPTAQHEK
     MLCDSWCIEA ATRIRENMAS LQSNPQQQEL FRNFRSISKA MVENGGLVTS NPLRV
//
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