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Q99PU5

- ACBG1_MOUSE

UniProt

Q99PU5 - ACBG1_MOUSE

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Protein

Long-chain-fatty-acid--CoA ligase ACSBG1

Gene

Acsbg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei547 – 5471ATPBy similarity
Binding sitei562 – 5621ATPBy similarity
Binding sitei698 – 6981ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi279 – 2879ATPBy similarity
Nucleotide bindingi469 – 4746ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: HGNC
  3. very long-chain fatty acid-CoA ligase activity Source: HGNC

GO - Biological processi

  1. long-chain fatty acid metabolic process Source: HGNC
  2. ovarian follicle atresia Source: Ensembl
  3. response to glucocorticoid Source: MGI
  4. very long-chain fatty acid metabolic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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
Gonadotropin-regulated long chain acyl CoA synthetase
Short name:
GR-LACS
Lipidosin
Gene namesi
Name:Acsbg1
Synonyms:Kiaa0631, Lpd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2385656. Acsbg1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi281 – 2811G → A: Abolishes enzyme activity; when associated with M-287. 1 Publication
Mutagenesisi287 – 2871K → M: Abolishes enzyme activity; when associated with A-281. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Long-chain-fatty-acid--CoA ligase ACSBG1PRO_0000315810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei655 – 6551Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99PU5.
PaxDbiQ99PU5.
PRIDEiQ99PU5.

PTM databases

PhosphoSiteiQ99PU5.

Expressioni

Tissue specificityi

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).4 Publications

Developmental stagei

First detected on embryonic day 18 and increases steadily towards adulthood.1 Publication

Gene expression databases

BgeeiQ99PU5.
CleanExiMM_ACSBG1.
ExpressionAtlasiQ99PU5. baseline and differential.
GenevestigatoriQ99PU5.

Interactioni

Protein-protein interaction databases

BioGridi220460. 1 interaction.
IntActiQ99PU5. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ99PU5.
SMRiQ99PU5. Positions 131-636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000230004.
HOVERGENiHBG054660.
InParanoidiQ99PU5.
KOiK15013.
OMAiFYQEQKM.
OrthoDBiEOG7B5WVB.
PhylomeDBiQ99PU5.
TreeFamiTF354286.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99PU5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRGSEAGYC CLSRDSNMPD SRDDQQQGAS LGTSQDNSQT SSLIDGQTLS
60 70 80 90 100
KESPSHGLEL SAPEKARAAS LDGAEEALWT TRADGRVRLR LEPFCTQRPY
110 120 130 140 150
TVHQMFYEAL DKYGNLSALG FKRKDKWERI SYYQYYLIAR KVAKGFLKLG
160 170 180 190 200
LERAHSVAIL GFNSPEWFFS AVGTVFAGGI VTGIYTTSSP EACQYISHDC
210 220 230 240 250
RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM ANVYTMEELI
260 270 280 290 300
ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA
310 320 330 340 350
RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP
360 370 380 390 400
DALKGTLVNT LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW
410 420 430 440 450
AMSVTLEQNL TCPSNDLKPF TSRLADYLVL ARVRQALGFA KCQKNFYGAA
460 470 480 490 500
PMTAETQRFF LGLNIRLYAG YGLSESTGPH FMSSPYNYRL YSSGRVVPGC
510 520 530 540 550
RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTCEAIDSE GWLHTGDMGR
560 570 580 590 600
LDADGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ
610 620 630 640 650
RKFLSMLLTL KCTLDPETSE PTDSLTEQAV EFCQRVGSKA STVSEIVGQR
660 670 680 690 700
DEAVYQAIHE GIQRVNANAA ARPYHIQKWA ILQRDFSISG GELGPTMKLK
710 720
RLTVLEKYKD IIDSFYQEQK Q
Length:721
Mass (Da):80,426
Last modified:June 1, 2001 - v1
Checksum:iC3A8C91333E984FE
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti299 – 2991T → I in BAC97989. (PubMed:14621295)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23192.1.
PIRiJC7557.
RefSeqiNP_444408.1. NM_053178.2.
UniGeneiMm.20592.

Genome annotation databases

EnsembliENSMUST00000034822; ENSMUSP00000034822; ENSMUSG00000032281.
GeneIDi94180.
KEGGimmu:94180.
UCSCiuc009prj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23192.1.
PIRi JC7557.
RefSeqi NP_444408.1. NM_053178.2.
UniGenei Mm.20592.

3D structure databases

ProteinModelPortali Q99PU5.
SMRi Q99PU5. Positions 131-636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 220460. 1 interaction.
IntActi Q99PU5. 2 interactions.

PTM databases

PhosphoSitei Q99PU5.

Proteomic databases

MaxQBi Q99PU5.
PaxDbi Q99PU5.
PRIDEi Q99PU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034822 ; ENSMUSP00000034822 ; ENSMUSG00000032281 .
GeneIDi 94180.
KEGGi mmu:94180.
UCSCi uc009prj.1. mouse.

Organism-specific databases

CTDi 23205.
MGIi MGI:2385656. Acsbg1.
Rougei Search...

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000101725.
HOGENOMi HOG000230004.
HOVERGENi HBG054660.
InParanoidi Q99PU5.
KOi K15013.
OMAi FYQEQKM.
OrthoDBi EOG7B5WVB.
PhylomeDBi Q99PU5.
TreeFami TF354286.

Miscellaneous databases

ChiTaRSi ACSBG1. mouse.
NextBioi 352133.
PROi Q99PU5.
SOURCEi Search...

Gene expression databases

Bgeei Q99PU5.
CleanExi MM_ACSBG1.
ExpressionAtlasi Q99PU5. baseline and differential.
Genevestigatori Q99PU5.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiACBG1_MOUSE
AccessioniPrimary (citable) accession number: Q99PU5
Secondary accession number(s): Q6ZQ79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3