ACBG1_MOUSE
ID ACBG1_MOUSE Reviewed; 721 AA.
AC Q99PU5; Q6ZQ79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000269|PubMed:11112418, ECO:0000269|PubMed:14516277};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 1;
DE Short=mBG1;
DE AltName: Full=Gonadotropin-regulated long chain acyl CoA synthetase;
DE Short=GR-LACS;
DE AltName: Full=Lipidosin;
GN Name=Acsbg1 {ECO:0000312|MGI:MGI:2385656}; Synonyms=Kiaa0631, Lpd;
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], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF GLY-281 AND LYS-287.
RC TISSUE=Brain;
RX PubMed=11112418; DOI=10.1006/bbrc.2000.3897;
RA Moriya-Sato A., Hida A., Inagawa-Ogashiwa M., Wada M.R., Sugiyama K.,
RA Shimizu J., Yabuki T., Seyama Y., Hashimoto N.;
RT "Novel acyl-CoA synthetase in adrenoleukodystrophy target tissues.";
RL Biochem. Biophys. Res. Commun. 279:62-68(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=16125341; DOI=10.1016/j.gene.2005.07.006;
RA Sheng Y., Li J., Dufau M.L., Tsai-Morris C.-H.;
RT "The gonadotropin-regulated long-chain acyl CoA synthetase gene: a novel
RT downstream Sp1/Sp3 binding element critical for transcriptional promoter
RT activity.";
RL Gene 360:20-26(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12975357; DOI=10.1074/jbc.m310075200;
RA Pei Z., Oey N.A., Zuidervaart M.M., Jia Z., Li Y., Steinberg S.J.,
RA Smith K.D., Watkins P.A.;
RT "The acyl-CoA synthetase 'bubblegum' (lipidosin): further characterization
RT and role in neuronal fatty acid beta-oxidation.";
RL J. Biol. Chem. 278:47070-47078(2003).
RN [7]
RP ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14516277; DOI=10.1042/bj20031062;
RA Fraisl P., Forss-Petter S., Zigman M., Berger J.;
RT "Murine bubblegum orthologue is a microsomal very long-chain acyl-CoA
RT synthetase.";
RL Biochem. J. 377:85-93(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16469493; DOI=10.1016/j.jsbmb.2005.10.005;
RA Li J., Sheng Y., Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RT "Tissue-cell- and species-specific expression of gonadotropin-regulated
RT long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain.
RT Identification of novel forms in the brain.";
RL J. Steroid Biochem. Mol. Biol. 98:207-217(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity) (PubMed:11112418, PubMed:12975357, PubMed:14516277). Can
CC activate diverse saturated, monosaturated and polyunsaturated fatty
CC acids (PubMed:11112418, PubMed:14516277).
CC {ECO:0000250|UniProtKB:Q96GR2, ECO:0000269|PubMed:11112418,
CC ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:14516277}.
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:0000269|PubMed:11112418, ECO:0000269|PubMed:14516277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q96GR2};
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:Q96GR2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96GR2}.
CC Cytoplasmic vesicle. Microsome. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96GR2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GR2}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain. Also expressed in
CC adrenal gland and testis. In brain, it is present in cerebral cortical
CC and cerebellar neurons and in steroidogenic cells of the adrenal gland,
CC testis and ovary (at protein level). {ECO:0000269|PubMed:11112418,
CC ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:14516277,
CC ECO:0000269|PubMed:16469493}.
CC -!- DEVELOPMENTAL STAGE: First detected on embryonic day 18 and increases
CC steadily towards adulthood. {ECO:0000269|PubMed:14516277}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97989.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB050554; BAB32783.1; -; mRNA.
DR EMBL; DQ009026; AAY58226.1; -; Genomic_DNA.
DR EMBL; DQ009013; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009014; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009015; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009016; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009017; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009018; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009019; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009020; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009021; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009022; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009023; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009024; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; DQ009025; AAY58226.1; JOINED; Genomic_DNA.
DR EMBL; AK129179; BAC97989.1; ALT_INIT; mRNA.
DR EMBL; AK054103; BAC35657.1; -; mRNA.
DR EMBL; BC057322; AAH57322.1; -; mRNA.
DR CCDS; CCDS23192.1; -.
DR PIR; JC7557; JC7557.
DR RefSeq; NP_444408.1; NM_053178.2.
DR AlphaFoldDB; Q99PU5; -.
DR SMR; Q99PU5; -.
DR BioGRID; 220460; 7.
DR IntAct; Q99PU5; 1.
DR STRING; 10090.ENSMUSP00000034822; -.
DR iPTMnet; Q99PU5; -.
DR PhosphoSitePlus; Q99PU5; -.
DR SwissPalm; Q99PU5; -.
DR MaxQB; Q99PU5; -.
DR PaxDb; Q99PU5; -.
DR PeptideAtlas; Q99PU5; -.
DR PRIDE; Q99PU5; -.
DR ProteomicsDB; 285638; -.
DR Antibodypedia; 27568; 170 antibodies from 22 providers.
DR DNASU; 94180; -.
DR Ensembl; ENSMUST00000034822; ENSMUSP00000034822; ENSMUSG00000032281.
DR GeneID; 94180; -.
DR KEGG; mmu:94180; -.
DR UCSC; uc009prj.1; mouse.
DR CTD; 23205; -.
DR MGI; MGI:2385656; Acsbg1.
DR VEuPathDB; HostDB:ENSMUSG00000032281; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000160380; -.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; Q99PU5; -.
DR OMA; RGMRKYD; -.
DR OrthoDB; 806831at2759; -.
DR PhylomeDB; Q99PU5; -.
DR TreeFam; TF354286; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR BioGRID-ORCS; 94180; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Acsbg1; mouse.
DR PRO; PR:Q99PU5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99PU5; protein.
DR Bgee; ENSMUSG00000032281; Expressed in lip and 139 other tissues.
DR ExpressionAtlas; Q99PU5; baseline and differential.
DR Genevisible; Q99PU5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:HGNC-UCL.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:HGNC-UCL.
DR GO; GO:0001552; P:ovarian follicle atresia; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IMP:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:HGNC-UCL.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Membrane; Microsome; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..721
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG1"
FT /id="PRO_0000315810"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 279..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924N5"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924N5"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MUTAGEN 281
FT /note="G->A: Abolishes enzyme activity; when associated
FT with M-287."
FT /evidence="ECO:0000269|PubMed:11112418"
FT MUTAGEN 287
FT /note="K->M: Abolishes enzyme activity; when associated
FT with A-281."
FT /evidence="ECO:0000269|PubMed:11112418"
FT CONFLICT 299
FT /note="T -> I (in Ref. 3; BAC97989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 80426 MW; C3A8C91333E984FE CRC64;
MPRGSEAGYC CLSRDSNMPD SRDDQQQGAS LGTSQDNSQT SSLIDGQTLS KESPSHGLEL
SAPEKARAAS LDGAEEALWT TRADGRVRLR LEPFCTQRPY TVHQMFYEAL DKYGNLSALG
FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI
VTGIYTTSSP EACQYISHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM
ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA
RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT
LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF
TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH
FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTCEAIDSE
GWLHTGDMGR LDADGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ
RKFLSMLLTL KCTLDPETSE PTDSLTEQAV EFCQRVGSKA STVSEIVGQR DEAVYQAIHE
GIQRVNANAA ARPYHIQKWA ILQRDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK
Q
