ACBG2_MOUSE
ID ACBG2_MOUSE Reviewed; 667 AA.
AC Q2XU92;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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};
DE AltName: Full=Bubblegum-related protein;
GN Name=Acsbg2 {ECO:0000312|MGI:MGI:3587728}; Synonyms=Bgr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvEv;
RX PubMed=16371355; DOI=10.1074/jbc.m511558200;
RA Pei Z., Jia Z., Watkins P.A.;
RT "The second member of the human and murine 'bubblegum' family is a
RT testis- and brainstem-specific acyl-CoA synthetase.";
RL J. Biol. Chem. 281:6632-6641(2006).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16762313; DOI=10.1016/j.abb.2006.04.013;
RA Fraisl P., Tanaka H., Forss-Petter S., Lassmann H., Nishimune Y.,
RA Berger J.;
RT "A novel mammalian bubblegum-related acyl-CoA synthetase restricted to
RT testes and possibly involved in spermatogenesis.";
RL Arch. Biochem. Biophys. 451:23-33(2006).
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. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Testis- and brainstem-specific. Expressed in
CC pubertal and adult testis. Enriched in germ cells and Sertoli cells
CC while present at a lower level in Leydig cells. Present in testicular
CC Sertoli cells and large motoneurons in the medulla oblongata and
CC cervical spinal cord (at protein level). {ECO:0000269|PubMed:16371355,
CC ECO:0000269|PubMed:16762313}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
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DR EMBL; DQ250679; ABB54488.1; -; mRNA.
DR CCDS; CCDS28916.1; -.
DR RefSeq; NP_001034203.1; NM_001039114.1.
DR AlphaFoldDB; Q2XU92; -.
DR SMR; Q2XU92; -.
DR STRING; 10090.ENSMUSP00000042352; -.
DR iPTMnet; Q2XU92; -.
DR PhosphoSitePlus; Q2XU92; -.
DR PaxDb; Q2XU92; -.
DR PRIDE; Q2XU92; -.
DR ProteomicsDB; 285639; -.
DR Antibodypedia; 24085; 143 antibodies from 21 providers.
DR Ensembl; ENSMUST00000043062; ENSMUSP00000042352; ENSMUSG00000024207.
DR GeneID; 328845; -.
DR KEGG; mmu:328845; -.
DR UCSC; uc008ddi.1; mouse.
DR CTD; 81616; -.
DR MGI; MGI:3587728; Acsbg2.
DR VEuPathDB; HostDB:ENSMUSG00000024207; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000155332; -.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; Q2XU92; -.
DR OMA; AINECCC; -.
DR OrthoDB; 806831at2759; -.
DR PhylomeDB; Q2XU92; -.
DR TreeFam; TF354286; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 328845; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Acsbg2; mouse.
DR PRO; PR:Q2XU92; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q2XU92; protein.
DR Bgee; ENSMUSG00000024207; Expressed in seminiferous tubule of testis and 7 other tissues.
DR Genevisible; Q2XU92; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IC:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:MGI.
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; -; 1.
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 1: Evidence at protein 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_0000315813"
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; 74319 MW; 70E1D0EC8AC4726F CRC64;
MTQEKKAEDL ERGTDATSAV PRLWSTHCDG EVLLRLSKHG PGHETPMTIP ELFQESAERF
SAYPALASKN GKKWDTLTFS QYYEMCRKAA KSLIKLGLQR FQCVGILGFN SVEWVVTALG
TILAGGLCVG IYATNSAEAC QYVIQQANVS ILIVENDQQL QKILLIPPDK METVKAIVQY
KLPLMESMAN LYSWNDFMEL GNDIPNIQLD RVILSQKANQ CAVILYTSGT TGTPKGVLLS
HDNITWTAGA MSQEMEINRV SGKQNTIVSY LPLSHIAAQL TDIWIPIKIG ALTFFAQPDA
LRGTLVYTLQ EVKPTLFMGV PRIWEKMQDT IKENVARSSR LRKKAFAWAK MLGLKVNTKR
MLGKRDIPMN YRMAKALVFA KVRTSLGLDN CHAFFSSASP LSQDVSEFFL SLDIPIGEIY
GMSECSGPHT VSNKSVYRVL SCGKVLSGCK NMLYNQNKEG VGEVCMWGRH VFMGYLNKEE
ATLEALDENG WLHSGDIGRL DSHDFLYITG RIKEILITAG GENVSPIPIE TLVKEKIPII
SHAMLVGDKA KFLCMLLTLK CETDRKSGEP LNKLSVEAKS FCQMLGSQAT TVSDILKSRD
QVVYTAIQYG IDIVNQQAMS DSHRIRKWII LEKDFSIQGG ELGPTSKLKR SVITQKYKAQ
IDSMYLS
