ACSF2_RAT
ID ACSF2_RAT Reviewed; 615 AA.
AC Q499N5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000305};
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q96CM8};
DE Flags: Precursor;
GN Name=Acsf2 {ECO:0000312|RGD:1562656};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty
CC acid metabolism, by forming a thioester with CoA. Has some preference
CC toward medium-chain substrates. Plays a role in adipocyte
CC differentiation. {ECO:0000250|UniProtKB:Q96CM8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q96CM8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; BC099826; AAH99826.1; -; mRNA.
DR RefSeq; NP_001030123.1; NM_001034951.1.
DR AlphaFoldDB; Q499N5; -.
DR SMR; Q499N5; -.
DR BioGRID; 565998; 3.
DR STRING; 10116.ENSRNOP00000004673; -.
DR iPTMnet; Q499N5; -.
DR PhosphoSitePlus; Q499N5; -.
DR PaxDb; Q499N5; -.
DR PRIDE; Q499N5; -.
DR Ensembl; ENSRNOT00000004673; ENSRNOP00000004673; ENSRNOG00000003330.
DR GeneID; 619561; -.
DR KEGG; rno:619561; -.
DR UCSC; RGD:1562656; rat.
DR CTD; 80221; -.
DR RGD; 1562656; Acsf2.
DR eggNOG; KOG1177; Eukaryota.
DR GeneTree; ENSGT00940000156830; -.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q499N5; -.
DR OMA; KQSDMKA; -.
DR OrthoDB; 386992at2759; -.
DR PhylomeDB; Q499N5; -.
DR TreeFam; TF313466; -.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR PRO; PR:Q499N5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003330; Expressed in heart and 18 other tissues.
DR Genevisible; Q499N5; RN.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..615
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315797"
FT BINDING 263..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 398
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 478
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 599
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
SQ SEQUENCE 615 AA; 67886 MW; 96F95B2186C01348 CRC64;
MAVYLGMLRL GRLCVASLGA RGPRTPLSRP WPNSKLQGVR AFSSGMVDCT NPLPIGGLSY
IQGHTDSHLV NKTVGECLDA TAQRFPNREA LVIIHENIRL NFAQLKEEVD RAASGLLSIG
LRKGDRLGMW GPNSYAWVLI QLATAQAGII LVSVNPAYQA SELEYVLRKV GCKGIVFPKQ
FKTQQYYNIL KQVCPELEKA QPGALKSERL PDLTTVISVD APLPGTLLLD EVVAAGGKEQ
NLAQLRYHQG FLSCYDPINI QFTSGTTGNP KGATLSHHNI VNNSNLIGQR LKMPAKTAEE
LRMVLPCPLY HCLGSVGGTM VSVVHGATLL LSSPSFNGKK ALEAISREKG TLLYGTPTMF
VDILNQPDFS SYDFTTIRGG VIAGSLAPPE LIRAIISKMN MKELVVVYGT TENSPVTFMN
FPEDTLEQKA GSVGRIMPHT EAQIVNMETG ELTKLNMPGE LCIRGYCVMQ GYWGEPQKTF
ETVGQDRWYR TGDIASMDEQ GFCRIVGRSK DMIIRGGENI YPAELEDFFH KHPQVQEAQV
VGVKDDRMGE EICACIRLKS GETTTEEEIK AFCKGKISHF KIPRYIVFVE GYPLTVSGKI
QKFKLREQME QHLKL
