| Tag | Content |
|---|
| CPLM ID | CPLM-017191 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-coenzyme A synthetase ACSM2, mitochondrial |
Protein Synonyms/Alias | Acyl-CoA synthetase medium-chain family member 2; Butyrate--CoA ligase 2; Butyryl-coenzyme A synthetase 2; Middle-chain acyl-CoA synthetase 2 |
Gene Name | Acsm2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 178 | APDCSFLKIKLLVSE | ubiquitination | [1] | | 180 | DCSFLKIKLLVSENS | ubiquitination | [1] | | 199 | LNFKALLKEASTIHQ | ubiquitination | [1] | | 558 | LPKTVTGKIERAKLR | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 221 229 ATP (By similarity).
NP_BIND 360 365 ATP (By similarity).
REGION 470 472 Coenzyme A binding (By similarity).
REGION 541 543 Coenzyme A binding (By similarity).
BINDING 139 139 Coenzyme A (By similarity).
BINDING 365 365 Substrate (By similarity).
BINDING 447 447 ATP (By similarity).
BINDING 462 462 ATP (By similarity).
BINDING 473 473 Substrate (By similarity).
BINDING 502 502 Coenzyme A (By similarity).
BINDING 533 533 Coenzyme A (By similarity).
BINDING 558 558 ATP (By similarity). |
Keyword | Alternative splicing; 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 | 575 AA |
Protein Sequence | MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA 60
GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW 120
LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK 180
LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI 240
KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV 300
LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE 360
IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP 420
IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GYRIGPSEVE 480
NALMEHPAVS ETAVISSPDP SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK 540
YPRKVEFVLD LPKTVTGKIE RAKLRAKEWK TSGRA 575 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:MGI. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0047760; F:butyrate-CoA ligase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |