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Long-chain fatty acid transport protein 1 (FATP-1) (Fatty acid transport protein 1) (EC 6.2.1.-) (Solute carrier family 27 member 1)

 S27A1_MOUSE             Reviewed;         646 AA.
Q60714;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 155.
RecName: Full=Long-chain fatty acid transport protein 1 {ECO:0000305};
Short=FATP-1;
Short=Fatty acid transport protein 1 {ECO:0000303|PubMed:9671728};
EC=6.2.1.- {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:12235169, ECO:0000269|PubMed:12937175};
AltName: Full=Fatty acid transport protein {ECO:0000303|PubMed:7954810};
AltName: Full=Solute carrier family 27 member 1 {ECO:0000312|MGI:MGI:1347098};
Name=Slc27a1 {ECO:0000312|MGI:MGI:1347098};
Synonyms=Fatp {ECO:0000303|PubMed:7954810},
Fatp1 {ECO:0000303|PubMed:9671728};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
STRAIN=SWR/J;
PubMed=7954810; DOI=10.1016/0092-8674(94)90252-6;
Schaffer J.E., Lodish H.F.;
"Expression cloning and characterization of a novel adipocyte long
chain fatty acid transport protein.";
Cell 79:427-436(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
PubMed=9765271; DOI=10.1074/jbc.273.42.27420;
Hui T.Y., Frohnert B.I., Smith A.J., Schaffer J.E., Bernlohr D.A.;
"Characterization of the murine fatty acid transport protein gene and
its insulin response sequence.";
J. Biol. Chem. 273:27420-27429(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, ATP-BINDING, AND MUTAGENESIS OF
SER-250.
PubMed=9786857; DOI=10.1074/jbc.273.44.28642;
Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.;
"Substitution of alanine for serine 250 in the murine fatty acid
transport protein inhibits long chain fatty acid transport.";
J. Biol. Chem. 273:28642-28650(1998).
[5]
FUNCTION IN FATTY ACID TRANSPORT, AND TISSUE SPECIFICITY.
PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
Hirsch D., Stahl A., Lodish H.F.;
"A family of fatty acid transporters conserved from mycobacterium to
man.";
Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
[6]
FUNCTION AS AN ACYL-COA LIGASE, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 249-THR--GLY-254.
PubMed=10593920; DOI=10.1074/jbc.274.51.36300;
Coe N.R., Smith A.J., Frohnert B.I., Watkins P.A., Bernlohr D.A.;
"The fatty acid transport protein (FATP1) is a very long chain acyl-
CoA synthetase.";
J. Biol. Chem. 274:36300-36304(1999).
[7]
FUNCTION, SUBCELLULAR LOCATION, ATP-BINDING, AND MUTAGENESIS OF
SER-250 AND THR-252.
PubMed=10471110; DOI=10.1016/S0952-3278(99)80001-5;
Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.;
"Molecular aspects of fatty acid transport: mutations in the
IYTSGTTGXPK motif impair fatty acid transport protein function.";
Prostaglandins Leukot. Essent. Fatty Acids 60:285-289(1999).
[8]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=11470793; DOI=10.1074/jbc.M105556200;
Lewis S.E., Listenberger L.L., Ory D.S., Schaffer J.E.;
"Membrane topology of the murine fatty acid transport protein 1.";
J. Biol. Chem. 276:37042-37050(2001).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=12235169; DOI=10.1194/jlr.M200130-JLR200;
Hatch G.M., Smith A.J., Xu F.Y., Hall A.M., Bernlohr D.A.;
"FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-
regulates sphingomyelin and cholesterol metabolism in growing 293
cells.";
J. Lipid Res. 43:1380-1389(2002).
[10]
SUBUNIT, AND REGION.
PubMed=12533547; DOI=10.1074/jbc.M212469200;
Richards M.R., Listenberger L.L., Kelly A.A., Lewis S.E., Ory D.S.,
Schaffer J.E.;
"Oligomerization of the murine fatty acid transport protein 1.";
J. Biol. Chem. 278:10477-10483(2003).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11970897; DOI=10.1016/S1534-5807(02)00143-0;
Stahl A., Evans J.G., Pattel S., Hirsch D., Lodish H.F.;
"Insulin causes fatty acid transport protein translocation and
enhanced fatty acid uptake in adipocytes.";
Dev. Cell 2:477-488(2002).
[12]
FUNCTION AS AN ACYL-COA LIGASE, AND CATALYTIC ACTIVITY.
PubMed=12937175; DOI=10.1074/jbc.M306575200;
Hall A.M., Smith A.J., Bernlohr D.A.;
"Characterization of the acyl-CoA synthetase activity of purified
murine fatty acid transport protein 1.";
J. Biol. Chem. 278:43008-43013(2003).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14991074; DOI=10.1172/JCI200418917;
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.;
"Inactivation of fatty acid transport protein 1 prevents fat-induced
insulin resistance in skeletal muscle.";
J. Clin. Invest. 113:756-763(2004).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15897321; DOI=10.1152/ajpcell.00271.2004;
Garcia-Martinez C., Marotta M., Moore-Carrasco R., Guitart M.,
Camps M., Busquets S., Montell E., Gomez-Foix A.M.;
"Impact on fatty acid metabolism and differential localization of
FATP1 and FAT/CD36 proteins delivered in cultured human muscle
cells.";
Am. J. Physiol. 288:C1264-C1272(2005).
[15]
FUNCTION.
PubMed=15699031; DOI=10.1074/jbc.M409598200;
DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
"Comparative biochemical studies of the murine fatty acid transport
proteins (FATP) expressed in yeast.";
J. Biol. Chem. 280:16829-16837(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
FUNCTION, INTERACTION WITH EPRS, AND SUBCELLULAR LOCATION.
PubMed=28178239; DOI=10.1038/nature21380;
Arif A., Terenzi F., Potdar A.A., Jia J., Sacks J., China A.,
Halawani D., Vasu K., Li X., Brown J.M., Chen J., Kozma S.C.,
Thomas G., Fox P.L.;
"EPRS is a critical mTORC1-S6K1 effector that influences adiposity in
mice.";
Nature 542:357-361(2017).
-!- FUNCTION: Mediates the ATP-dependent import of long-chain fatty
acids (LCFA) into the cell by mediating their translocation at the
plasma membrane (PubMed:7954810, PubMed:9786857, PubMed:9671728,
PubMed:10471110, PubMed:12235169, PubMed:11970897,
PubMed:15699031, PubMed:28178239). Has also an acyl-CoA ligase
activity for long-chain and very-long-chain fatty acids
(PubMed:10593920, PubMed:12235169, PubMed:12937175). 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 (PubMed:14991074,
PubMed:15897321). Plays a pivotal role in regulating available
LCFA substrates from exogenous sources in tissues undergoing high
levels of beta-oxidation or triglyceride synthesis
(PubMed:12235169). May be involved in regulation of cholesterol
metabolism (PubMed:12235169). {ECO:0000269|PubMed:10471110,
ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11970897,
ECO:0000269|PubMed:12235169, ECO:0000269|PubMed:12937175,
ECO:0000269|PubMed:14991074, ECO:0000269|PubMed:15699031,
ECO:0000269|PubMed:15897321, ECO:0000269|PubMed:28178239,
ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9671728,
ECO:0000269|PubMed:9786857}.
-!- ACTIVITY REGULATION: Inhibited by Triacsin C.
{ECO:0000269|PubMed:12235169}.
-!- SUBUNIT: Self-associates. May function as a homodimer
(PubMed:12533547). Interacts with EPRS; mediates the translocation
of SLC27A1 from the cytoplasm to the plasma membrane thereby
increasing the uptake of long-chain fatty acids (PubMed:28178239).
{ECO:0000269|PubMed:12533547, ECO:0000269|PubMed:28178239}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10471110,
ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11470793,
ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:28178239,
ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9786857}; Single-
pass membrane protein {ECO:0000269|PubMed:11470793,
ECO:0000269|PubMed:7954810}. Endomembrane system
{ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:15897321};
Single-pass membrane protein {ECO:0000269|PubMed:11470793,
ECO:0000269|PubMed:7954810}. Cytoplasm
{ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:15897321}.
Note=Plasma membrane and intracellular membranes, at least in
adipocytes (PubMed:10593920, PubMed:11970897, PubMed:28178239). In
adipocytes, but not myocytes, insulin via the mTORC1 signaling
pathway induces a rapid translocation of SLC27A1 from
intracellular compartments to the plasma membrane, paralleled by
increased LCFA uptake (PubMed:11970897, PubMed:28178239). Insulin-
dependent translocation from the cytoplasm to the cell membrane is
regulated by EPRS (PubMed:11970897, PubMed:28178239).
Predominantly cytoplasmic in myocytes (PubMed:15897321).
{ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11970897,
ECO:0000269|PubMed:15897321, ECO:0000269|PubMed:28178239}.
-!- TISSUE SPECIFICITY: Highest expression in skeletal muscle, heart
and fat. Lower levels in brain, kidney, lung, liver and testis. No
expression in spleen or intestine. {ECO:0000269|PubMed:7954810,
ECO:0000269|PubMed:9671728}.
-!- DEVELOPMENTAL STAGE: Higher expression in differentiated
adipocytes compared to preadipocytes.
{ECO:0000269|PubMed:7954810}.
-!- INDUCTION: Expression is down-regulated by insulin.
{ECO:0000269|PubMed:9765271}.
-!- DISRUPTION PHENOTYPE: Mice deficient for Slc27a1 are viable and do
not display overt developmental phenotype or alteration in whole-
body adiposity. However, they are protected from fat-induced
accumulation of intramuscular fatty acyl-CoA and insulin
resistance in skeletal muscle. {ECO:0000269|PubMed:14991074}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U15976; AAC71060.1; -; mRNA.
EMBL; AF023258; AAC69640.1; -; Genomic_DNA.
EMBL; AF023256; AAC69640.1; JOINED; Genomic_DNA.
EMBL; AF023257; AAC69640.1; JOINED; Genomic_DNA.
EMBL; BC028937; AAH28937.1; -; mRNA.
CCDS; CCDS40386.1; -.
PIR; A55093; A55093.
RefSeq; NP_036107.1; NM_011977.3.
RefSeq; XP_006509736.1; XM_006509673.2.
RefSeq; XP_006509737.1; XM_006509674.3.
RefSeq; XP_006509738.1; XM_006509675.3.
RefSeq; XP_006509739.1; XM_006509676.3.
UniGene; Mm.38165; -.
ProteinModelPortal; Q60714; -.
SMR; Q60714; -.
BioGrid; 205003; 1.
IntAct; Q60714; 1.
MINT; Q60714; -.
STRING; 10090.ENSMUSP00000034267; -.
BindingDB; Q60714; -.
ChEMBL; CHEMBL2052039; -.
SwissLipids; SLP:000000426; -.
iPTMnet; Q60714; -.
PhosphoSitePlus; Q60714; -.
SwissPalm; Q60714; -.
MaxQB; Q60714; -.
PaxDb; Q60714; -.
PRIDE; Q60714; -.
Ensembl; ENSMUST00000034267; ENSMUSP00000034267; ENSMUSG00000031808.
Ensembl; ENSMUST00000212889; ENSMUSP00000148768; ENSMUSG00000031808.
GeneID; 26457; -.
KEGG; mmu:26457; -.
UCSC; uc009mdw.1; mouse.
CTD; 376497; -.
MGI; MGI:1347098; Slc27a1.
eggNOG; KOG1179; Eukaryota.
eggNOG; ENOG410XQ8T; LUCA.
GeneTree; ENSGT00940000159323; -.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; Q60714; -.
KO; K08745; -.
OMA; IWEEFTE; -.
OrthoDB; EOG091G0B76; -.
PhylomeDB; Q60714; -.
TreeFam; TF313430; -.
Reactome; R-MMU-804914; Transport of fatty acids.
ChiTaRS; Slc27a1; mouse.
PRO; PR:Q60714; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031808; Expressed in 294 organ(s), highest expression level in vibrissa unit.
ExpressionAtlas; Q60714; baseline and differential.
Genevisible; Q60714; MM.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; TAS:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IMP:MGI.
GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:MGI.
GO; GO:0015908; P:fatty acid transport; IDA:MGI.
GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
GO; GO:0001676; P:long-chain fatty acid metabolic process; TAS:MGI.
GO; GO:0015909; P:long-chain fatty acid transport; IMP:MGI.
GO; GO:0001579; P:medium-chain fatty acid transport; IGI:MGI.
GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; ISO:MGI.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:MGI.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:MGI.
GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISO:MGI.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:MGI.
GO; GO:0006659; P:phosphatidylserine biosynthetic process; ISO:MGI.
GO; GO:0031652; P:positive regulation of heat generation; IMP:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:MGI.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
GO; GO:0009409; P:response to cold; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:MGI.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR030308; FATP1.
PANTHER; PTHR43107:SF7; PTHR43107:SF7; 1.
Pfam; PF00501; AMP-binding; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Fatty acid metabolism;
Ligase; Lipid metabolism; Lipid transport; Membrane;
Nucleotide-binding; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 646 Long-chain fatty acid transport protein
1.
/FTId=PRO_0000193202.
TOPO_DOM 1 13 Extracellular.
{ECO:0000305|PubMed:11470793}.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TOPO_DOM 35 646 Cytoplasmic.
{ECO:0000305|PubMed:11470793}.
NP_BIND 246 257 AMP. {ECO:0000269|PubMed:10471110,
ECO:0000269|PubMed:10593920,
ECO:0000269|PubMed:9786857}.
REGION 191 475 Sufficient for oligomerization.
{ECO:0000269|PubMed:12533547}.
MUTAGEN 249 254 TSGTTG->LEAAA: Abolishes very-long-chain
acyl-CoA synthetase activity.
{ECO:0000269|PubMed:10593920}.
MUTAGEN 250 250 S->A: Diminishes LCFA import and
decreases nucleotide binding. No effect
on localization to the cell membrane.
{ECO:0000269|PubMed:10471110,
ECO:0000269|PubMed:9786857}.
MUTAGEN 252 252 T->A: Diminishes LCFA import and
decreases nucleotide binding. No effect
on localization to the cell membrane.
{ECO:0000269|PubMed:10471110}.
SEQUENCE 646 AA; 71276 MW; 910B92BA8D985B4C CRC64;
MRAPGAGTAS VASLALLWFL GLPWTWSAAA AFCVYVGGGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HRRAGDTIPC IFQAVARRQP ERLALVDASS GICWTFAQLD TYSNAVANLF
RQLGFAPGDV VAVFLEGRPE FVGLWLGLAK AGVVAALLNV NLRREPLAFC LGTSAAKALI
YGGEMAAAVA EVSEQLGKSL LKFCSGDLGP ESILPDTQLL DPMLAEAPTT PLAQAPGKGM
DDRLFYIYTS GTTGLPKAAI VVHSRYYRIA AFGHHSYSMR AADVLYDCLP LYHSAGNIMG
VGQCVIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLRQPVR DVEQRHRVRL
AVGNGLRPAI WEEFTQRFGV PQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILTHVYPIR
LVKVNEDTME PLRDSEGLCI PCQPGEPGLL VGQINQQDPL RRFDGYVSDS ATNKKIAHSV
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEAVLSR LLGQTDVAVY
GVAVPGVEGK AGMAAIADPH SQLDPNSMYQ ELQKVLASYA RPIFLRLLPQ VDTTGTFKIQ
KTRLQREGFD PRQTSDRLFF LDLKQGRYVP LDERVHARIC AGDFSL


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