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Q60714 (S27A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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 transport protein 1

Short name=FATP-1
Short name=Fatty acid transport protein 1
EC=6.2.1.-
Alternative name(s):
Solute carrier family 27 member 1
Gene names
Name:Slc27a1
Synonyms:Fatp, Fatp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

Self-associates. May function as a homodimer. Ref.9

Subcellular location

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. Ref.6 Ref.8 Ref.13 Ref.14

Tissue specificity

Highest expression in skeletal muscle, heart and fat. Lower levels in brain, kidney, lung and liver. No expression in spleen or intestine. Ref.5

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.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Lipid transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from mutant phenotype PubMed 20667975. Source: MGI

cardiolipin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

fatty acid transport

Inferred from direct assay Ref.9Ref.5. Source: MGI

long-chain fatty acid metabolic process

Traceable author statement PubMed 15464426. Source: MGI

long-chain fatty acid transport

Inferred from mutant phenotype PubMed 16611988. Source: MGI

medium-chain fatty acid transport

Inferred from genetic interaction PubMed 18258213. Source: MGI

negative regulation of phospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidic acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylethanolamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylserine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of heat generation

Inferred from mutant phenotype PubMed 17130465. Source: MGI

positive regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 19560442PubMed 20667975. Source: MGI

response to cold

Inferred from mutant phenotype PubMed 17130465. Source: MGI

response to insulin

Inferred from mutant phenotype Ref.12. Source: MGI

   Cellular_componentcytoplasmic vesicle

Traceable author statement PubMed 15464426. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 15496455. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 15496455PubMed 17130465. Source: MGI

   Molecular_functionfatty acid transporter activity

Inferred from direct assay Ref.9Ref.5. Source: MGI

long-chain fatty acid-CoA ligase activity

Traceable author statement PubMed 15464426. Source: MGI

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay PubMed 12566451. Source: MGI

very long-chain fatty acid-CoA ligase activity

Inferred from direct assay PubMed 18258213. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 646646Long-chain fatty acid transport protein 1
PRO_0000193202

Regions

Topological domain1 – 1313Extracellular Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 646612Cytoplasmic Potential
Nucleotide binding246 – 25712AMP Probable
Region191 – 475285Sufficient for oligomerization

Experimental info

Mutagenesis249 – 2546TSGTTG → LEAAA: Abolishes very-long-chain acyl-CoA synthetase activity. Ref.6
Mutagenesis2501S → A: Diminishes LCFA import and decreases nucleotide binding. Ref.4 Ref.7
Mutagenesis2521T → A: Diminishes LCFA import and decreases nucleotide binding. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q60714 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 910B92BA8D985B4C

FASTA64671,276
        10         20         30         40         50         60 
MRAPGAGTAS VASLALLWFL GLPWTWSAAA AFCVYVGGGG WRFLRIVCKT ARRDLFGLSV 

        70         80         90        100        110        120 
LIRVRLELRR HRRAGDTIPC IFQAVARRQP ERLALVDASS GICWTFAQLD TYSNAVANLF 

       130        140        150        160        170        180 
RQLGFAPGDV VAVFLEGRPE FVGLWLGLAK AGVVAALLNV NLRREPLAFC LGTSAAKALI 

       190        200        210        220        230        240 
YGGEMAAAVA EVSEQLGKSL LKFCSGDLGP ESILPDTQLL DPMLAEAPTT PLAQAPGKGM 

       250        260        270        280        290        300 
DDRLFYIYTS GTTGLPKAAI VVHSRYYRIA AFGHHSYSMR AADVLYDCLP LYHSAGNIMG 

       310        320        330        340        350        360 
VGQCVIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLRQPVR DVEQRHRVRL 

       370        380        390        400        410        420 
AVGNGLRPAI WEEFTQRFGV PQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILTHVYPIR 

       430        440        450        460        470        480 
LVKVNEDTME PLRDSEGLCI PCQPGEPGLL VGQINQQDPL RRFDGYVSDS ATNKKIAHSV 

       490        500        510        520        530        540 
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEAVLSR LLGQTDVAVY 

       550        560        570        580        590        600 
GVAVPGVEGK AGMAAIADPH SQLDPNSMYQ ELQKVLASYA RPIFLRLLPQ VDTTGTFKIQ 

       610        620        630        640 
KTRLQREGFD PRQTSDRLFF LDLKQGRYVP LDERVHARIC AGDFSL 

« Hide

References

« Hide 'large scale' references
[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]"Oligomerization of the murine fatty acid transport protein 1."
Richards M.R., Listenberger L.L., Kelly A.A., Lewis S.E., Ory D.S., Schaffer J.E.
J. Biol. Chem. 278:10477-10483(2003) [PubMed] [Europe PMC] [Abstract]
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]"Inactivation of fatty acid transport protein 1 prevents fat-induced insulin resistance in skeletal muscle."
Kim J.K., Gimeno R.E., Higashimori T., Kim H.J., Choi H., Punreddy S., Mozell R.L., Tan G., Stricker-Krongrad A., Hirsch D.J., Fillmore J.J., Liu Z.X., Dong J., Cline G., Stahl A., Lodish H.F., Shulman G.I.
J. Clin. Invest. 113:756-763(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15976 mRNA. Translation: AAC71060.1.
AF023258, AF023256, AF023257 Genomic DNA. Translation: AAC69640.1.
BC028937 mRNA. Translation: AAH28937.1.
CCDSCCDS40386.1.
PIRA55093.
RefSeqNP_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.
UniGeneMm.38165.

3D structure databases

ProteinModelPortalQ60714.
SMRQ60714. Positions 77-607.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60714. 1 interaction.
MINTMINT-4094970.

Chemistry

ChEMBLCHEMBL2052039.

PTM databases

PhosphoSiteQ60714.

Proteomic databases

MaxQBQ60714.
PaxDbQ60714.
PRIDEQ60714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034267; ENSMUSP00000034267; ENSMUSG00000031808.
GeneID26457.
KEGGmmu:26457.
UCSCuc009mdw.1. mouse.

Organism-specific databases

CTD376497.
MGIMGI:1347098. Slc27a1.

Phylogenomic databases

eggNOGCOG0318.
GeneTreeENSGT00550000074420.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidQ60714.
KOK08745.
OMAIWEEFTE.
OrthoDBEOG7W6WKB.
PhylomeDBQ60714.
TreeFamTF313430.

Gene expression databases

ArrayExpressQ60714.
BgeeQ60714.
GenevestigatorQ60714.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC27A1. mouse.
NextBio304565.
PROQ60714.
SOURCESearch...

Entry information

Entry nameS27A1_MOUSE
AccessionPrimary (citable) accession number: Q60714
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 119 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