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Q9JID6

- ACSL1_CAVPO

UniProt

Q9JID6 - ACSL1_CAVPO

Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

ACSL1

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase 1
    Short name:
    LACS 1
    Palmitoyl-CoA ligase
    Gene namesi
    Name:ACSL1
    Synonyms:FACL1, LACS1
    OrganismiCavia porcellus (Guinea pig)
    Taxonomic identifieri10141 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
    ProteomesiUP000005447: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. mitochondrial outer membrane Source: UniProtKB-SubCell
    3. peroxisomal membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 698698Long-chain-fatty-acid--CoA ligase 1PRO_0000193103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei9 – 91Nitrated tyrosineBy similarity
    Modified residuei84 – 841PhosphotyrosineBy similarity
    Glycosylationi135 – 1351O-linked (GlcNAc)By similarity
    Modified residuei356 – 3561N6-acetyllysineBy similarity
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei620 – 6201PhosphoserineBy similarity
    Modified residuei632 – 6321N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Nitration, Phosphoprotein

    Proteomic databases

    PRIDEiQ9JID6.

    Interactioni

    Protein-protein interaction databases

    STRINGi10141.ENSCPOP00000002483.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JID6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000101725.
    HOGENOMiHOG000159459.
    HOVERGENiHBG050452.
    OrthoDBiEOG71CFKN.

    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.

    Q9JID6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQAHELLQYF RLPELVDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA    50
    LKPPCDLSMQ SVEVAGSDGA RRSTLLDSDE PLVYFYDDVR TLYDVFQRGI 100
    QVSNNGPCLG SRKPDQPYEW LSYKQVEDLS ECIGSALLQK GFQASPDQFI 150
    GIFAQNRPEW VIIEQACFAY SMVVVPLYDT LGADAITYIV NKAELSVIFA 200
    DKPEKARILL ESVENKLTPG LKIIVVMDSY GSELVEQGKK CGVEVISLKA 250
    MEGLGRANRR KPKPPEPDDL AVICFTSGTT GNPKGAMITH KNVVSDCSAF 300
    VKATEKALVL NASDIHISFL PLAHMYEQLL QCVMLCHGAK IGFFQGDIRL 350
    LMDDLKALQP TIFPVVPRLL NRMFDRIFAQ ANTTVKRWLL DFASKRKEAE 400
    LRSGIIRNNS VWDKLIFHKI QSSLGGKVRL MVTGAAPVSA TVLTFLRAAL 450
    GCQFYEGYGQ TECTAGCSLS VPGDWTAGHV GAPMPCNFIK LVDVEEMNYM 500
    AAMGEGEVCV KGPNVFKGYL KDPAKTAEAL DKDGWLHTGD IGKWLPNGTL 550
    KIIDRKKHIF KLAQGEYIAP EKIENIYVRS EPVAQVFVHG ESLQAFLIAI 600
    VVPDAESLAS WARKRGFEGS FEELCRNKDV KKAILEDMVR IGKDSGLKSF 650
    EQVRGIALHP ELFSVDNGLL TPTMKAKRPE LRNYFRSQID ELYSTIKV 698
    Length:698
    Mass (Da):77,698
    Last modified:October 1, 2000 - v1
    Checksum:iCF8CB413209476AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF236818 mRNA. Translation: AAF91295.1.
    RefSeqiNP_001166379.1. NM_001172908.1.

    Genome annotation databases

    EnsembliENSCPOT00000002769; ENSCPOP00000002484; ENSCPOG00000002734.
    GeneIDi100135469.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF236818 mRNA. Translation: AAF91295.1 .
    RefSeqi NP_001166379.1. NM_001172908.1.

    3D structure databases

    ProteinModelPortali Q9JID6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10141.ENSCPOP00000002483.

    Proteomic databases

    PRIDEi Q9JID6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCPOT00000002769 ; ENSCPOP00000002484 ; ENSCPOG00000002734 .
    GeneIDi 100135469.

    Organism-specific databases

    CTDi 2180.

    Phylogenomic databases

    eggNOGi COG1022.
    GeneTreei ENSGT00690000101725.
    HOGENOMi HOG000159459.
    HOVERGENi HBG050452.
    OrthoDBi EOG71CFKN.

    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. "Molecular characterization and expression of guinea-pig acyl-CoA synthetase 1."
      Sevoz C., Benoit E., Buronfosse T.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiACSL1_CAVPO
    AccessioniPrimary (citable) accession number: Q9JID6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 80 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3