ACBG2_RAT
ID ACBG2_RAT Reviewed; 667 AA.
AC A1L1K7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG2 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q5FVE4};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 2;
DE AltName: Full=Arachidonate--CoA ligase ACSBG2 {ECO:0000250|UniProtKB:Q5FVE4};
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:Q5FVE4};
GN Name=Acsbg2 {ECO:0000312|RGD:1588580};
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=Testis;
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: Catalyzes the conversion of fatty acids such as long chain
CC and very long-chain fatty acids to their active form acyl-CoAs for both
CC synthesis of cellular lipids, and degradation via beta-oxidation. Can
CC activate diverse saturated, monosaturated and polyunsaturated fatty
CC acids. Has increased ability to activate oleic and linoleic acid. May
CC play a role in spermatogenesis. {ECO:0000250|UniProtKB:Q5FVE4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
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DR EMBL; BC129110; AAI29111.1; -; mRNA.
DR RefSeq; NP_001073565.1; NM_001080096.1.
DR AlphaFoldDB; A1L1K7; -.
DR SMR; A1L1K7; -.
DR STRING; 10116.ENSRNOP00000066937; -.
DR PaxDb; A1L1K7; -.
DR PeptideAtlas; A1L1K7; -.
DR PRIDE; A1L1K7; -.
DR Ensembl; ENSRNOT00000074555; ENSRNOP00000066937; ENSRNOG00000045947.
DR GeneID; 301120; -.
DR KEGG; rno:301120; -.
DR CTD; 81616; -.
DR RGD; 1588580; Acsbg2.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000155332; -.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; A1L1K7; -.
DR OMA; AINECCC; -.
DR OrthoDB; 806831at2759; -.
DR PhylomeDB; A1L1K7; -.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:A1L1K7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000045947; Expressed in testis and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISO:RGD.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; -; 2.
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 PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Reference proteome; Spermatogenesis.
FT CHAIN 1..667
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG2"
FT /id="PRO_0000315814"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 418..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 667 AA; 74266 MW; CE929821D95D6700 CRC64;
MTQEKKAEDP DRGMDTTSAA PRLWSTHCDG EVLLRLSKHG PGHETPMTIP ELFQESVERF
GAYPALASKN GKKWDTLTFS QYYDVCRKAA RSLIKLGLQR FHGVGILGFN SVEWVVAALG
AILAGGLCVG IYATNSAEAC QYVIKQANVN VLIVENDQQL QKILSIPPDK METVKAIVQY
RLPLMENSTN LYSWQDFMEL GNAIPNIQLD RVILSQKANQ CAVIIYTSGT TGSPKGVMLS
HDNITWTAGA MAREIELIHV SGKQDTIVSY LPLSHIAAQL MDIWIPIKVG VLTFFAQPDA
LRGTLVYTLQ EVKPTYFLGV PRVWEKMQDT IKENVAKSSN LRKKAFAWAK MLGLKVNTKK
MLGKRDIPMN YRMAKALVFT KVRTSLGLDN CHTFFSGASP LSQDVSEFFL SLDIPIGEIY
GMTECSGPHT VSCKSIYRVL SCGKVLNGCK NMLYKQNKDG VGEVCMWGRH VFMGYLGKED
ATLEVLDEDG WLHSGDIGRL DSHDFLYITG RIKEVLITAG GENIWPIPIE TLVKEKIPII
SHAMLVGDKA KFLSMLLTLK CETDQMSGEP LDKLNLEAIS FCQMLGSQAV TVSDILKIRD
PVVYTAIQYG IDIVNQQAVS DSHRIRKWII LEKDFSIQGG ELGPTSKLKR DLITQKYKAQ
IDNMYSS
