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   24-JAN-2024, entry version 88.
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   PhosphoSitePlus; A1L1K7; -.
DR   PaxDb; 10116-ENSRNOP00000066937; -.
DR   PeptideAtlas; A1L1K7; -.
DR   Ensembl; ENSRNOT00000074555.3; ENSRNOP00000066937.1; ENSRNOG00000045947.4.
DR   Ensembl; ENSRNOT00055024401; ENSRNOP00055019937; ENSRNOG00055014186.
DR   Ensembl; ENSRNOT00060037457; ENSRNOP00060030870; ENSRNOG00060021553.
DR   Ensembl; ENSRNOT00065022892; ENSRNOP00065017784; ENSRNOG00065013883.
DR   GeneID; 301120; -.
DR   KEGG; rno:301120; -.
DR   AGR; RGD:1588580; -.
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; FNRPGPN; -.
DR   OrthoDB; 443463at2759; -.
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 cell type or 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: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   CDD; cd05933; ACSBG_like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF101; LONG-CHAIN-FATTY-ACID--COA LIGASE ACSBG2; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//