| Tag | Content |
|---|
| CPLM ID | CPLM-024675 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-CoA dehydrogenase family member 11 |
Protein Synonyms/Alias | ACAD-11 |
Gene Name | Acad11 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 17 | VEVLPQHKFDIRSLE | acetylation | [1] | | 81 | SLLPKAHKIDREFKV | acetylation | [1] | | 87 | HKIDREFKVQKALFS | acetylation | [1] | | 390 | TRVKQFMKQHVFPAE | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA (By similarity). |
Sequence Annotation | NP_BIND 503 513 FAD (By similarity).
NP_BIND 503 506 FAD (By similarity).
NP_BIND 511 513 FAD (By similarity).
NP_BIND 537 539 FAD (By similarity).
NP_BIND 726 730 FAD; shared with dimeric partner (By
NP_BIND 755 757 FAD (By similarity).
REGION 628 631 Substrate binding (By similarity).
BINDING 513 513 Substrate; via carbonyl oxygen (By
BINDING 539 539 FAD (By similarity).
BINDING 656 656 FAD (By similarity).
BINDING 656 656 FAD; shared with dimeric partner (By
BINDING 726 726 FAD (By similarity).
BINDING 754 754 Substrate; via amide nitrogen (By
BINDING 757 757 FAD (By similarity).
MOD_RES 323 323 Phosphotyrosine (By similarity). |
Keyword | Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 779 AA |
Protein Sequence | MEMDVTRDTV EVLPQHKFDI RSLEAYLNQH LPGFGSDHRA VLTVTQYRSG QSNPTFFLQK 60
GSQAYVLRKK PPGSLLPKAH KIDREFKVQK ALFSVGFPVP KPLLYCSNAS IIGTEFYVME 120
HVQGRIFRDF SIPGVSPAER AAIYVSLVET LAWLHSLDIH SLGLDRYGTG VGYCKRQVST 180
WTKQYQASAH QSIPAMDQLS TWLMRNLPDS DNEECLVHGD FKLDNIVFHP KECRVIAVLD 240
WELSTFGHPL SDLAHLSLFY FWPRTLPMIN RGSHIQENTG IPLMEELISI YCRRRGIDPN 300
LPNWNFFMAL SFFKLAGIAQ GVYSRYLMGN NSSEDSFLTA NTVQPLAETG LQLSRRTLST 360
VPPQADAKSR LFAQSRRGQE VLTRVKQFMK QHVFPAEKEV AEYYAQNGNS AEKWEHPLVI 420
EKLKEMAKAE GLWNLFLPAV SGLSQVDYAL IAEETGKCFF APDVFNCQAP DTGNMEVLHL 480
YGSEQQKQQW LEPLLRGDIT SVFCMTEPNV SSSDATNMEC SIQRDGGSYI VHGKKWWSSG 540
AGNPKCKIAV VLGRTESPSV SRHKVHSMIL VPMDTPGVEL IRPLSVFGYM DNVHGGHWEV 600
HFNHVRVPAS NLILGEGRGF EISQGRLGPG RIHHCMRSVG LAERILQIMC DRAVQREAFG 660
KKLYEHEVVA HWIAKSRIAI EEIRLLTLKA AHSIDTLGSA AARKEIAMIK VAAPKAVCKI 720
ADRAIQVHGG AGVSQDYPLA NMYAIIRTLR LADGPDEVHL SAIAKMELQD QARQLKARM 779 |
Gene Ontology | GO:0031966; C:mitochondrial membrane; IEA:Compara. GO:0005634; C:nucleus; IEA:Compara. GO:0005777; C:peroxisome; IDA:HGNC. GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:Compara. GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro. GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IEA:Compara. GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |