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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.
28-MAR-2018, entry version 150.
RecName: Full=Long-chain fatty acid transport protein 1;
Short=FATP-1;
Short=Fatty acid transport protein 1;
EC=6.2.1.-;
AltName: Full=Solute carrier family 27 member 1;
Name=Slc27a1; Synonyms=Fatp, Fatp1;
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].
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].
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]
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, 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]
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]
OLIGOMERIZATION.
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).
[10]
FUNCTION.
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).
[11]
FUNCTION AS AN ACYL-COA LIGASE.
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).
[12]
FUNCTION.
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).
[13]
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).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[15]
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).
-!- 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.
{ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11970897,
ECO:0000269|PubMed:12937175, ECO:0000269|PubMed:14991074,
ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:15897321,
ECO:0000269|PubMed:9671728}.
-!- SUBUNIT: Self-associates. May function as a homodimer.
-!- 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.
-!- TISSUE SPECIFICITY: Highest expression in skeletal muscle, heart
and fat. Lower levels in brain, kidney, lung and liver. No
expression in spleen or intestine. {ECO:0000269|PubMed:9671728}.
-!- 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.
-!- 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; ENSGT00550000074420; -.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; Q60714; -.
KO; K08745; -.
OMA; YTRICSG; -.
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; -.
ExpressionAtlas; Q60714; baseline and differential.
Genevisible; Q60714; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:MGI.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; TAS:MGI.
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: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: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:0000255}.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TOPO_DOM 35 646 Cytoplasmic. {ECO:0000255}.
NP_BIND 246 257 AMP. {ECO:0000305}.
REGION 191 475 Sufficient for oligomerization.
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.
{ECO:0000269|PubMed:10471110,
ECO:0000269|PubMed:9786857}.
MUTAGEN 252 252 T->A: Diminishes LCFA import and
decreases nucleotide binding.
{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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