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Q60714

- S27A1_MOUSE

UniProt

Q60714 - S27A1_MOUSE

Protein

Long-chain fatty acid transport protein 1

Gene

Slc27a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FatP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids.7 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 25712AMPCuratedAdd
    BLAST

    GO - Molecular functioni

    1. fatty acid transporter activity Source: MGI
    2. long-chain fatty acid-CoA ligase activity Source: MGI
    3. nucleotide binding Source: UniProtKB-KW
    4. protein homodimerization activity Source: MGI
    5. very long-chain fatty acid-CoA ligase activity Source: MGI

    GO - Biological processi

    1. adiponectin-activated signaling pathway Source: MGI
    2. cardiolipin biosynthetic process Source: Ensembl
    3. fatty acid transport Source: MGI
    4. long-chain fatty acid metabolic process Source: MGI
    5. long-chain fatty acid transport Source: MGI
    6. medium-chain fatty acid transport Source: MGI
    7. negative regulation of phospholipid biosynthetic process Source: Ensembl
    8. phosphatidic acid biosynthetic process Source: Ensembl
    9. phosphatidylcholine biosynthetic process Source: Ensembl
    10. phosphatidylethanolamine biosynthetic process Source: Ensembl
    11. phosphatidylinositol biosynthetic process Source: Ensembl
    12. phosphatidylserine biosynthetic process Source: Ensembl
    13. positive regulation of heat generation Source: MGI
    14. positive regulation of protein serine/threonine kinase activity Source: MGI
    15. response to cold Source: MGI
    16. response to insulin Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Lipid transport, Transport

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.
    REACT_198636. Transport of fatty acids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain fatty acid transport protein 1 (EC:6.2.1.-)
    Short name:
    FATP-1
    Short name:
    Fatty acid transport protein 1
    Alternative name(s):
    Solute carrier family 27 member 1
    Gene namesi
    Name:Slc27a1
    Synonyms:Fatp, Fatp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1347098. Slc27a1.

    Subcellular locationi

    Cell membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein. Cytoplasm
    Note: Plasma membrane and intracellular membranes, at least in adipocytes. Predominantly cytoplasmic in myocytes.

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi249 – 2546TSGTTG → LEAAA: Abolishes very-long-chain acyl-CoA synthetase activity. 1 Publication
    Mutagenesisi250 – 2501S → A: Diminishes LCFA import and decreases nucleotide binding. 3 Publications
    Mutagenesisi252 – 2521T → A: Diminishes LCFA import and decreases nucleotide binding. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 646646Long-chain fatty acid transport protein 1PRO_0000193202Add
    BLAST

    Proteomic databases

    MaxQBiQ60714.
    PaxDbiQ60714.
    PRIDEiQ60714.

    PTM databases

    PhosphoSiteiQ60714.

    Expressioni

    Tissue specificityi

    Highest expression in skeletal muscle, heart and fat. Lower levels in brain, kidney, lung and liver. No expression in spleen or intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ60714.
    BgeeiQ60714.
    GenevestigatoriQ60714.

    Interactioni

    Subunit structurei

    Self-associates. May function as a homodimer.

    Protein-protein interaction databases

    IntActiQ60714. 1 interaction.
    MINTiMINT-4094970.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60714.
    SMRiQ60714. Positions 77-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1313ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini35 – 646612CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 475285Sufficient for oligomerizationAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0318.
    GeneTreeiENSGT00550000074420.
    HOGENOMiHOG000044189.
    HOVERGENiHBG005642.
    InParanoidiQ60714.
    KOiK08745.
    OMAiIWEEFTE.
    OrthoDBiEOG7W6WKB.
    PhylomeDBiQ60714.
    TreeFamiTF313430.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60714-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRAPGAGTAS VASLALLWFL GLPWTWSAAA AFCVYVGGGG WRFLRIVCKT    50
    ARRDLFGLSV LIRVRLELRR HRRAGDTIPC IFQAVARRQP ERLALVDASS 100
    GICWTFAQLD TYSNAVANLF RQLGFAPGDV VAVFLEGRPE FVGLWLGLAK 150
    AGVVAALLNV NLRREPLAFC LGTSAAKALI YGGEMAAAVA EVSEQLGKSL 200
    LKFCSGDLGP ESILPDTQLL DPMLAEAPTT PLAQAPGKGM DDRLFYIYTS 250
    GTTGLPKAAI VVHSRYYRIA AFGHHSYSMR AADVLYDCLP LYHSAGNIMG 300
    VGQCVIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLRQPVR 350
    DVEQRHRVRL AVGNGLRPAI WEEFTQRFGV PQIGEFYGAT ECNCSIANMD 400
    GKVGSCGFNS RILTHVYPIR LVKVNEDTME PLRDSEGLCI PCQPGEPGLL 450
    VGQINQQDPL RRFDGYVSDS ATNKKIAHSV FRKGDSAYLS GDVLVMDELG 500
    YMYFRDRSGD TFRWRGENVS TTEVEAVLSR LLGQTDVAVY GVAVPGVEGK 550
    AGMAAIADPH SQLDPNSMYQ ELQKVLASYA RPIFLRLLPQ VDTTGTFKIQ 600
    KTRLQREGFD PRQTSDRLFF LDLKQGRYVP LDERVHARIC AGDFSL 646
    Length:646
    Mass (Da):71,276
    Last modified:November 1, 1996 - v1
    Checksum:i910B92BA8D985B4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15976 mRNA. Translation: AAC71060.1.
    AF023258, AF023256, AF023257 Genomic DNA. Translation: AAC69640.1.
    BC028937 mRNA. Translation: AAH28937.1.
    CCDSiCCDS40386.1.
    PIRiA55093.
    RefSeqiNP_036107.1. NM_011977.3.
    XP_006509736.1. XM_006509673.1.
    XP_006509737.1. XM_006509674.1.
    XP_006509738.1. XM_006509675.1.
    XP_006509739.1. XM_006509676.1.
    UniGeneiMm.38165.

    Genome annotation databases

    EnsembliENSMUST00000034267; ENSMUSP00000034267; ENSMUSG00000031808.
    GeneIDi26457.
    KEGGimmu:26457.
    UCSCiuc009mdw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15976 mRNA. Translation: AAC71060.1 .
    AF023258 , AF023256 , AF023257 Genomic DNA. Translation: AAC69640.1 .
    BC028937 mRNA. Translation: AAH28937.1 .
    CCDSi CCDS40386.1.
    PIRi A55093.
    RefSeqi NP_036107.1. NM_011977.3.
    XP_006509736.1. XM_006509673.1.
    XP_006509737.1. XM_006509674.1.
    XP_006509738.1. XM_006509675.1.
    XP_006509739.1. XM_006509676.1.
    UniGenei Mm.38165.

    3D structure databases

    ProteinModelPortali Q60714.
    SMRi Q60714. Positions 77-607.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q60714. 1 interaction.
    MINTi MINT-4094970.

    Chemistry

    ChEMBLi CHEMBL2052039.

    PTM databases

    PhosphoSitei Q60714.

    Proteomic databases

    MaxQBi Q60714.
    PaxDbi Q60714.
    PRIDEi Q60714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034267 ; ENSMUSP00000034267 ; ENSMUSG00000031808 .
    GeneIDi 26457.
    KEGGi mmu:26457.
    UCSCi uc009mdw.1. mouse.

    Organism-specific databases

    CTDi 376497.
    MGIi MGI:1347098. Slc27a1.

    Phylogenomic databases

    eggNOGi COG0318.
    GeneTreei ENSGT00550000074420.
    HOGENOMi HOG000044189.
    HOVERGENi HBG005642.
    InParanoidi Q60714.
    KOi K08745.
    OMAi IWEEFTE.
    OrthoDBi EOG7W6WKB.
    PhylomeDBi Q60714.
    TreeFami TF313430.

    Enzyme and pathway databases

    Reactomei REACT_198602. PPARA activates gene expression.
    REACT_198636. Transport of fatty acids.

    Miscellaneous databases

    ChiTaRSi SLC27A1. mouse.
    NextBioi 304565.
    PROi Q60714.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60714.
    Bgeei Q60714.
    Genevestigatori Q60714.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein."
      Schaffer J.E., Lodish H.F.
      Cell 79:427-436(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss.
    2. "Characterization of the murine fatty acid transport protein gene and its insulin response sequence."
      Hui T.Y., Frohnert B.I., Smith A.J., Schaffer J.E., Bernlohr D.A.
      J. Biol. Chem. 273:27420-27429(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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: Retina.
    4. "Substitution of alanine for serine 250 in the murine fatty acid transport protein inhibits long chain fatty acid transport."
      Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.
      J. Biol. Chem. 273:28642-28650(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-250.
    5. "A family of fatty acid transporters conserved from mycobacterium to man."
      Hirsch D., Stahl A., Lodish H.F.
      Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FATTY ACID TRANSPORT, TISSUE SPECIFICITY.
    6. "The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase."
      Coe N.R., Smith A.J., Frohnert B.I., Watkins P.A., Bernlohr D.A.
      J. Biol. Chem. 274:36300-36304(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ACYL-COA LIGASE, SUBCELLULAR LOCATION, MUTAGENESIS OF 249-THR--GLY-254.
    7. "Molecular aspects of fatty acid transport: mutations in the IYTSGTTGXPK motif impair fatty acid transport protein function."
      Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.
      Prostaglandins Leukot. Essent. Fatty Acids 60:285-289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-250 AND THR-252.
    8. "Membrane topology of the murine fatty acid transport protein 1."
      Lewis S.E., Listenberger L.L., Ory D.S., Schaffer J.E.
      J. Biol. Chem. 276:37042-37050(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
    9. Cited for: OLIGOMERIZATION.
    10. "Insulin causes fatty acid transport protein translocation and enhanced fatty acid uptake in adipocytes."
      Stahl A., Evans J.G., Pattel S., Hirsch D., Lodish H.F.
      Dev. Cell 2:477-488(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Characterization of the acyl-CoA synthetase activity of purified murine fatty acid transport protein 1."
      Hall A.M., Smith A.J., Bernlohr D.A.
      J. Biol. Chem. 278:43008-43013(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ACYL-COA LIGASE.
    12. Cited for: FUNCTION.
    13. "Impact on fatty acid metabolism and differential localization of FATP1 and FAT/CD36 proteins delivered in cultured human muscle cells."
      Garcia-Martinez C., Marotta M., Moore-Carrasco R., Guitart M., Camps M., Busquets S., Montell E., Gomez-Foix A.M.
      Am. J. Physiol. 288:C1264-C1272(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast."
      DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.
      J. Biol. Chem. 280:16829-16837(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiS27A1_MOUSE
    AccessioniPrimary (citable) accession number: Q60714
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mice deficient for Fatp1 are protected from fat-induced insulin resistance and intramuscular accumulation of fatty acyl-CoA without alteration in whole-body adiposity.

    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