| Tag | Content |
|---|
| CPLM ID | CPLM-013247 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-CoA synthetase family member 2, mitochondrial |
Protein Synonyms/Alias | |
Gene Name | Acsf2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 179 | CKGIVFPKQFKTQQY | acetylation | [1] | | 182 | IVFPKQFKTQQYYNI | acetylation | [1] | | 191 | QQYYNILKQVCPELE | acetylation | [1] | | 199 | QVCPELEKAQPGALK | acetylation | [1] | | 206 | KAQPGALKSERLPDL | acetylation | [1] | | 340 | SPSFNGKKALEAISR | acetylation | [1] | | 398 | LIRAIISKMNMKELV | acetylation | [1] | | 581 | KGKISHFKIPRYIVF | 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 synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipodyte differentiation (By similarity). |
Sequence Annotation | NP_BIND 263 271 ATP (By similarity).
BINDING 493 493 ATP (By similarity).
BINDING 508 508 ATP (By similarity).
BINDING 599 599 ATP (By similarity). |
Keyword | ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 615 AA |
Protein Sequence | MAVYLGMLRL GRLCVASLGA RGPRTPLSRP WPNSKLQGVR AFSSGMVDCT NPLPIGGLSY 60
IQGHTDSHLV NKTVGECLDA TAQRFPNREA LVIIHENIRL NFAQLKEEVD RAASGLLSIG 120
LRKGDRLGMW GPNSYAWVLI QLATAQAGII LVSVNPAYQA SELEYVLRKV GCKGIVFPKQ 180
FKTQQYYNIL KQVCPELEKA QPGALKSERL PDLTTVISVD APLPGTLLLD EVVAAGGKEQ 240
NLAQLRYHQG FLSCYDPINI QFTSGTTGNP KGATLSHHNI VNNSNLIGQR LKMPAKTAEE 300
LRMVLPCPLY HCLGSVGGTM VSVVHGATLL LSSPSFNGKK ALEAISREKG TLLYGTPTMF 360
VDILNQPDFS SYDFTTIRGG VIAGSLAPPE LIRAIISKMN MKELVVVYGT TENSPVTFMN 420
FPEDTLEQKA GSVGRIMPHT EAQIVNMETG ELTKLNMPGE LCIRGYCVMQ GYWGEPQKTF 480
ETVGQDRWYR TGDIASMDEQ GFCRIVGRSK DMIIRGGENI YPAELEDFFH KHPQVQEAQV 540
VGVKDDRMGE EICACIRLKS GETTTEEEIK AFCKGKISHF KIPRYIVFVE GYPLTVSGKI 600
QKFKLREQME QHLKL 615 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0016874; F:ligase activity; IEA:UniProtKB-KW. GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |