Tag | Content |
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CPLM ID | CPLM-001075 |
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; Kidney-specific protein KS; Middle-chain acyl-CoA synthetase 2 |
Gene Name | Acsm2 |
Gene Synonyms/Alias | Ks |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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59 | DHWASLEKAGKRSPG | acetylation | [1] | 141 | MPGTTQMKSTDILYR | acetylation | [1] | 180 | DCSFLKIKLLVSEKN | acetylation | [1] | 186 | IKLLVSEKNREGWLN | acetylation | [1] | 195 | REGWLNFKALLKDAS | acetylation | [1] | 406 | GNVLPPGKEGDMALR | acetylation | [1] | 415 | GDMALRVKPIRPIGM | acetylation | [1] | 450 | LLGDRGIKDTEGYFH | acetylation | [1] | 532 | KVLQEHVKSVTAPYK | acetylation | [1] | 557 | LPKTITGKIERAKLR | acetylation | [1] |
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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 221 229 ATP (By similarity). NP_BIND 359 364 ATP (By similarity). REGION 469 471 Coenzyme A binding (By similarity). REGION 540 542 Coenzyme A binding (By similarity). BINDING 139 139 Coenzyme A (By similarity). BINDING 364 364 Substrate (By similarity). BINDING 446 446 ATP (By similarity). BINDING 461 461 ATP (By similarity). BINDING 472 472 Substrate (By similarity). BINDING 501 501 Coenzyme A (By similarity). BINDING 532 532 Coenzyme A (By similarity). BINDING 557 557 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 | 572 AA |
Protein Sequence | MHWLWKIPRL CTFWGTEMFH RTFHMNIKKL MPIQWGHQEV PAKFNFASDV IDHWASLEKA 60 GKRSPGPALW WMNGSGEELK WNFRELSEIS KQTANVLTGA CGLQRGDRVA VVLPRVPEWW 120 LVTLGCMRSG LVFMPGTTQM KSTDILYRLQ SSKARAIVAG DEVVQEVDAV APDCSFLKIK 180 LLVSEKNREG WLNFKALLKD ASPIHQCVET VSQESAAIYF TSGTSGPPKM AEHSHCSLGL 240 KAKMDAGWTG LGPSDTMWTI SDTGWILNIL GSFLEPWVLG TCIFVHLLPK FDPQTVLKVL 300 SSYPINTLLG APLIYRMLLQ QDLSSYKFPH LHSCFSGGET LLPETLESWK AKTGLEIREI 360 YGQTETGITC RVSRTMKVKP GYLGTAIVPY DVQVIDEQGN VLPPGKEGDM ALRVKPIRPI 420 GMFSGYVDNP KKTQANIRGD FWLLGDRGIK DTEGYFHFMG RTDDIINSSG YRIGPSEVEN 480 ALMEHPAVVE TAVISSPDPI RREVVKAFVV LAPEFLSHDQ DQLTKVLQEH VKSVTAPYKY 540 PRKVEFVLDL PKTITGKIER AKLRAKEWKT SG 572 |
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:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. |
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