ACSF2_BOVIN
ID ACSF2_BOVIN Reviewed; 615 AA.
AC Q17QJ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000250|UniProtKB:Q96CM8};
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q96CM8};
DE Flags: Precursor;
GN Name=ACSF2 {ECO:0000250|UniProtKB:Q96CM8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC118331; AAI18332.1; -; mRNA.
DR RefSeq; NP_001071580.1; NM_001078112.1.
DR AlphaFoldDB; Q17QJ1; -.
DR SMR; Q17QJ1; -.
DR STRING; 9913.ENSBTAP00000028385; -.
DR PaxDb; Q17QJ1; -.
DR PRIDE; Q17QJ1; -.
DR Ensembl; ENSBTAT00000028385; ENSBTAP00000028385; ENSBTAG00000021301.
DR GeneID; 768237; -.
DR KEGG; bta:768237; -.
DR CTD; 80221; -.
DR VEuPathDB; HostDB:ENSBTAG00000021301; -.
DR VGNC; VGNC:25562; ACSF2.
DR eggNOG; KOG1177; Eukaryota.
DR GeneTree; ENSGT00940000156830; -.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q17QJ1; -.
DR OMA; KQSDMKA; -.
DR OrthoDB; 386992at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021301; Expressed in ruminant reticulum and 104 other tissues.
DR ExpressionAtlas; Q17QJ1; baseline and differential.
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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..615
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315792"
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; 68201 MW; A04B6C4300AA8991 CRC64;
MAVYVGMLRV ARLCARSPRV LGARVGLSRV WQEARLWGVR PLSSGELDHT VPLPVGGFSY
VQGHVGLHLS NKTVGRCLDA TAQRVPDQEA LVVHHENIRL TFAQLKEEVD KAASGLLSIG
LRKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYALKKV GCKALVFPKQ
FKTQQYYNIL KQICPEVEKA QPGALKSQRL PDLTTVISVD AHLPGTLLLD EVVAAGSQEQ
NLTRLRHTQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNANMIGQR LRLHQKTPEE
SRVVLPSPLY HCLGSVGGTM VSLMHGVTLI LCSPVFEGKK TLEAISRERG CFLYGTPTMF
VDVLNQPDFS SYDISTMRGG VIAGSPAPPE LIRAIINKLN MKELVVAYGT TENSPVTFMN
FTEDTVEQKA ESVGRVMPHT EAQIVNTETG TLTELNTPGE LCIRGYCVML GYWGEPQKTE
EAIGQDKWYR TGDIAMMDEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPQVQEVQV
VGVKDDRMGE EICACIRLKE GEKTTAEEIK AFCKGKISHF KIPRYIVFVT NYPLTVSGKI
QKFKLREQME QHLNL
