| Tag | Content |
|---|
| CPLM ID | CPLM-015372 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-coenzyme A synthetase ACSM3, mitochondrial |
Protein Synonyms/Alias | Acyl-CoA synthetase medium-chain family member 3; Butyrate--CoA ligase 3; Butyryl-coenzyme A synthetase 3; Middle-chain acyl-CoA synthetase 3; SA rat hypertension-associated protein; Protein SA |
Gene Name | Acsm3 |
Gene Synonyms/Alias | Sah |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 85 | WWVDGNGKEVRWSFE | acetylation | [1] | | 151 | GTTQLTQKDILYRLQ | acetylation | [1] | | 203 | REGWGNLKEMMKYAS | acetylation | [1] | | 336 | QNDITSYKFNSLKHC | 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 | Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) (By similarity). |
Sequence Annotation | NP_BIND 229 237 ATP (By similarity).
NP_BIND 368 373 ATP (By similarity).
BINDING 455 455 ATP (By similarity).
BINDING 470 470 ATP (By similarity).
BINDING 566 566 ATP (By similarity). |
Keyword | ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 580 AA |
Protein Sequence | MAMLLRARCF HRLAIPDPRR ILYKDYRTAI PQNFSNYESM KHDFKIEIPE YFNFAKDVLD 60
QWTNTEKTGK RLSNPAFWWV DGNGKEVRWS FEELGSLSRK FANILTEACS LQRGDRVMVI 120
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KSKCIITDDT LAPAVDIVAA 180
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH NELMAIYFTS GTTGPPKMIG 240
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF 300
DSTSILQTLS KFPITVFCSA PTAYRMLIQN DITSYKFNSL KHCVSAGEPI NPEVMEQWKK 360
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFN VEILDENGTI LPPGQEGDIA 420
VQVLPDRPFG LFTHYVDNPS KTASTLRGNF YITGDRGYMD EDGYFWFVAR SDDVILSSGY 480
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKLHDQE QLKKEIQEHV 540
KKTTAPYKYP RKIEFIEELP KTVSGKVKRN ELRRKEWTTT 580 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0047760; F:butyrate-CoA ligase activity; IEA:EC. GO:0015645; F:fatty acid ligase activity; IEA:Compara. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006633; P:fatty acid biosynthetic process; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |