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Q99PU5 (ACBG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gonadotropin-regulated long chain acyl CoA synthetase
Short name=GR-LACS
Lipidosin
Gene names
Name:Acsbg1
Synonyms:Kiaa0631, Lpd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence 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 fatty 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.

Sequence caution

The sequence BAC97989.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Long-chain-fatty-acid--CoA ligase ACSBG1
PRO_0000315810

Regions

Nucleotide binding279 – 2879ATP By similarity
Nucleotide binding469 – 4746ATP By similarity

Sites

Binding site5471ATP By similarity
Binding site5621ATP By similarity
Binding site6981ATP By similarity

Amino acid modifications

Modified residue6551Phosphotyrosine Ref.10

Experimental info

Mutagenesis2811G → A: Abolishes enzyme activity; when associated with M-287. Ref.1
Mutagenesis2871K → M: Abolishes enzyme activity; when associated with A-281. Ref.1
Sequence conflict2991T → I in BAC97989. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99PU5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C3A8C91333E984FE

FASTA72180,426
        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 

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References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB050554 mRNA. Translation: BAB32783.1.
DQ009026 expand/collapse EMBL AC list , 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.
PIRJC7557.
RefSeqNP_444408.1. NM_053178.2.
UniGeneMm.20592.

3D structure databases

ProteinModelPortalQ99PU5.
SMRQ99PU5. Positions 131-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220460. 1 interaction.
IntActQ99PU5. 2 interactions.

PTM databases

PhosphoSiteQ99PU5.

Proteomic databases

PaxDbQ99PU5.
PRIDEQ99PU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034822; ENSMUSP00000034822; ENSMUSG00000032281.
GeneID94180.
KEGGmmu:94180.
UCSCuc009prj.1. mouse.

Organism-specific databases

CTD23205.
MGIMGI:2385656. Acsbg1.
RougeSearch...

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000101725.
HOGENOMHOG000230004.
HOVERGENHBG054660.
InParanoidQ99PU5.
KOK15013.
OMATQQPNQC.
OrthoDBEOG7B5WVB.
PhylomeDBQ99PU5.
TreeFamTF354286.

Gene expression databases

BgeeQ99PU5.
CleanExMM_ACSBG1.
GenevestigatorQ99PU5.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACSBG1. mouse.
NextBio352133.
PROQ99PU5.
SOURCESearch...

Entry information

Entry nameACBG1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot