Reviewed, UniProtKB/Swiss-Prot Q99PU5 (ACBG1_MOUSE)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase ACSBG1
    EC=6.2.1.3
Alternative name(s):
    Acyl-CoA synthetase bubblegum family member 1
      Short name=mBG1
    Lipodisin
    Gonadotropin-regulated long chain acyl CoA synthetase
      Short name=GR-LACS

Gene names

Name:	Acsbg1
Synonyms:	Kiaa0631, Lpd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	721 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids By similarity. Ref.1 Ref.6 Ref.7
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1 Ref.7
Subcellular location	Cytoplasm By similarity. Cytoplasmic vesicle. Microsome. Endoplasmic reticulum Ref.6 Ref.7.
Tissue specificity	Mainly expressed in brain. Also expressed in adrenal gland and testis. In brain, it is present in cerebral cortical and cerebellar neurons and in steroidogenic cells of the adrenal gland, testis and ovary (at protein level). Ref.1 Ref.6 Ref.7 Ref.8
Developmental stage	First detected on embryonic day 18 and increases steadily towards adulthood. Ref.7
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Microsome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	long-chain fatty acid metabolic process Inferred from sequence or structural similarity. Source: HGNC response to glucocorticoid stimulus Inferred from mutant phenotype. Source: MGI very-long-chain fatty acid metabolic process Inferred from sequence or structural similarity. Source: HGNC
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Ref.7 Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Ref.7 Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Inferred from sequence or structural similarity. Source: HGNC very-long-chain-fatty-acid-CoA ligase activity Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 721	721	Long-chain-fatty-acid--CoA ligase ACSBG1		PRO_0000315810
Regions
	Nucleotide binding	279 – 287	9	ATP By similarity
	Nucleotide binding	469 – 474	6	ATP By similarity
Sites
	Binding site	547	1	ATP By similarity
	Binding site	562	1	ATP By similarity
	Binding site	698	1	ATP By similarity
Amino acid modifications
	Modified residue	132	1	Phosphotyrosine By similarity
	Modified residue	135	1	Phosphotyrosine By similarity
	Modified residue	136	1	Phosphotyrosine By similarity
	Modified residue	655	1	Phosphotyrosine Ref.9
Experimental info
	Mutagenesis	281	1	G → A: Abolishes enzyme activity; when associated with M-287. Ref.1
	Mutagenesis	287	1	K → M: Abolishes enzyme activity; when associated with A-281. Ref.1
	Sequence conflict	299	1	T → I in BAC97989. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q99PU5-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: C3A8C91333E984FE	FASTA	721	80,426
	10 20 30 40 50 60 MPRGSEAGYC CLSRDSNMPD SRDDQQQGAS LGTSQDNSQT SSLIDGQTLS KESPSHGLEL 70 80 90 100 110 120 SAPEKARAAS LDGAEEALWT TRADGRVRLR LEPFCTQRPY TVHQMFYEAL DKYGNLSALG 130 140 150 160 170 180 FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI 190 200 210 220 230 240 VTGIYTTSSP EACQYISHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM 250 260 270 280 290 300 ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA 310 320 330 340 350 360 RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT 370 380 390 400 410 420 LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF 430 440 450 460 470 480 TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH 490 500 510 520 530 540 FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTCEAIDSE 550 560 570 580 590 600 GWLHTGDMGR LDADGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ 610 620 630 640 650 660 RKFLSMLLTL KCTLDPETSE PTDSLTEQAV EFCQRVGSKA STVSEIVGQR DEAVYQAIHE 670 680 690 700 710 720 GIQRVNANAA ARPYHIQKWA ILQRDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel acyl-CoA synthetase in adrenoleukodystrophy target tissues." Moriya-Sato A., Hida A., Inagawa-Ogashiwa M., Wada M.R., Sugiyama K., Shimizu J., Yabuki T., Seyama Y., Hashimoto N. Biochem. Biophys. Res. Commun. 279:62-68(2000) [PubMed: 11112418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-281 AND LYS-287. Tissue: Brain.
[2]	"The gonadotropin-regulated long-chain acyl CoA synthetase gene: a novel downstream Sp1/Sp3 binding element critical for transcriptional promoter activity." Sheng Y., Li J., Dufau M.L., Tsai-Morris C.-H. Gene 360:20-26(2005) [PubMed: 16125341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Oviduct.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[6]	"The acyl-CoA synthetase 'bubblegum' (lipidosin): further characterization and role in neuronal fatty acid beta-oxidation." Pei Z., Oey N.A., Zuidervaart M.M., Jia Z., Li Y., Steinberg S.J., Smith K.D., Watkins P.A. J. Biol. Chem. 278:47070-47078(2003) [PubMed: 12975357] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Murine bubblegum orthologue is a microsomal very long-chain acyl-CoA synthetase." Fraisl P., Forss-Petter S., Zigman M., Berger J. Biochem. J. 377:85-93(2004) [PubMed: 14516277] [Abstract] Cited for: ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"Tissue-cell- and species-specific expression of gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain." Li J., Sheng Y., Tang P.-Z., Tsai-Morris C.-H., Dufau M.L. J. Steroid Biochem. Mol. Biol. 98:207-217(2006) [PubMed: 16469493] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-655, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB050554 mRNA. Translation: BAB32783.1. DQ009026 , DQ009013, DQ009014, DQ009015, DQ009016, DQ009017, DQ009018, DQ009019, DQ009020, DQ009021, DQ009022, DQ009023, DQ009024, DQ009025 Genomic DNA. Translation: AAY58226.1. AK129179 mRNA. Translation: BAC97989.1. Different initiation. AK054103 mRNA. Translation: BAC35657.1. BC057322 mRNA. Translation: AAH57322.1.
IPI	IPI00453834.
PIR	JC7557.
RefSeq	NP_444408.1.
UniGene	Mm.20592
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q99PU5.
PTM databases
PhosphoSite	Q99PU5.
Proteomic databases
PRIDE	Q99PU5.
Genome annotation databases
Ensembl	ENSMUST00000034822; ENSMUSP00000034822; ENSMUSG00000032281; Mus musculus. [Genome view]
GeneID	94180.
KEGG	mmu:94180.
NMPDR	fig|10090.3.peg.20220.
UCSC	uc009prj.1. mouse.
Organism-specific databases
CTD	94180.
MGI	MGI:2385656. Acsbg1.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG05521.
HOGENOM	HBG721674.
HOVERGEN	Q99PU5.
InParanoid	Q99PU5.
OMA	GIQWGAQ.
OrthoDB	EOG95HVGN.
PhylomeDB	Q99PU5.
Enzyme and pathway databases
BRENDA	6.2.1.3. 244.
Gene expression databases
ArrayExpress	Q99PU5.
Bgee	Q99PU5.
CleanEx	MM_ACSBG1.
Genevestigator	Q99PU5.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	352133.
SOURCE	Search...

Entry information

Entry name

ACBG1_MOUSE

Accession

Primary (citable) accession number: Q99PU5
Secondary accession number(s): Q6ZQ79

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2001
Last modified:	January 19, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)