Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99PU5

- ACBG1_MOUSE

UniProt

Q99PU5 - ACBG1_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 membrane-bounded vesicle Source: UniProtKB-SubCell

    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.
    GenevestigatoriQ99PU5.

    Interactioni

    Protein-protein interaction databases

    BioGridi220460. 1 interaction.
    IntActiQ99PU5. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99PU5.
    SMRiQ99PU5. Positions 93-636.
    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

    MPRGSEAGYC CLSRDSNMPD SRDDQQQGAS LGTSQDNSQT SSLIDGQTLS    50
    KESPSHGLEL SAPEKARAAS LDGAEEALWT TRADGRVRLR LEPFCTQRPY 100
    TVHQMFYEAL DKYGNLSALG FKRKDKWERI SYYQYYLIAR KVAKGFLKLG 150
    LERAHSVAIL GFNSPEWFFS AVGTVFAGGI VTGIYTTSSP EACQYISHDC 200
    RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM ANVYTMEELI 250
    ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA 300
    RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP 350
    DALKGTLVNT LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW 400
    AMSVTLEQNL TCPSNDLKPF TSRLADYLVL ARVRQALGFA KCQKNFYGAA 450
    PMTAETQRFF LGLNIRLYAG YGLSESTGPH FMSSPYNYRL YSSGRVVPGC 500
    RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTCEAIDSE GWLHTGDMGR 550
    LDADGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ 600
    RKFLSMLLTL KCTLDPETSE PTDSLTEQAV EFCQRVGSKA STVSEIVGQR 650
    DEAVYQAIHE GIQRVNANAA ARPYHIQKWA ILQRDFSISG GELGPTMKLK 700
    RLTVLEKYKD IIDSFYQEQK Q 721
    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 93-636.
    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.
    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

    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 1, 2014
    This is version 110 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