S27A1_RAT
ID S27A1_RAT Reviewed; 646 AA.
AC P97849;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Long-chain fatty acid transport protein 1 {ECO:0000305};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:Q60714};
DE AltName: Full=Fatty acid transport protein {ECO:0000303|PubMed:9375787};
DE AltName: Full=Fatty acid transport protein 1 {ECO:0000303|PubMed:15848183};
DE Short=FATP-1;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q60714};
DE AltName: Full=Solute carrier family 27 member 1 {ECO:0000312|RGD:620927};
DE AltName: Full=Very long-chain acyl-CoA synthetase;
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q60714};
GN Name=Slc27a1 {ECO:0000312|RGD:620927};
GN Synonyms=Fatp {ECO:0000303|PubMed:9375787},
GN Fatp1 {ECO:0000303|PubMed:15848183};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9375787; DOI=10.1016/s0167-4781(97)00121-8;
RA Schaap F.G., Hamers L., van der Vusse G.J., Glatz J.F.C.;
RT "Molecular cloning of fatty acid-transport protein cDNA from rat.";
RL Biochim. Biophys. Acta 1354:29-34(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=15848183; DOI=10.1016/j.febslet.2004.11.118;
RA Chabowski A., Coort S.L., Calles-Escandon J., Tandon N.N., Glatz J.F.,
RA Luiken J.J., Bonen A.;
RT "The subcellular compartmentation of fatty acid transporters is regulated
RT differently by insulin and by AICAR.";
RL FEBS Lett. 579:2428-2432(2005).
RN [3]
RP FUNCTION, TRANSPORT ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19380575; DOI=10.1074/jbc.m109.004788;
RA Nickerson J.G., Alkhateeb H., Benton C.R., Lally J., Nickerson J.,
RA Han X.X., Wilson M.H., Jain S.S., Snook L.A., Glatz J.F.C., Chabowski A.,
RA Luiken J.J.F.P., Bonen A.;
RT "Greater transport efficiencies of the membrane fatty acid transporters
RT FAT/CD36 and FATP4 compared with FABPpm and FATP1 and differential effects
RT on fatty acid esterification and oxidation in rat skeletal muscle.";
RL J. Biol. Chem. 284:16522-16530(2009).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport at the plasma membrane
CC (PubMed:19380575). Also functions as an acyl-CoA ligase catalyzing the
CC ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-
CC chain fatty acids (VLCFA) as substrates, which prevents fatty acid
CC efflux from cells and might drive more fatty acid uptake. May act
CC directly as a bona fide transporter, or alternatively, in a cytoplasmic
CC or membrane-associated multimeric protein complex to trap and draw
CC fatty acids towards accumulation. Plays a pivotal role in regulating
CC available LCFA substrates from exogenous sources in tissues undergoing
CC high levels of beta-oxidation or triglyceride synthesis. May be
CC involved in regulation of cholesterol metabolism. Probably involved in
CC fatty acid transport across the blood barrier (By similarity).
CC {ECO:0000250|UniProtKB:Q60714, ECO:0000250|UniProtKB:Q6PCB7,
CC ECO:0000269|PubMed:19380575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:19380575};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q6PCB7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000269|PubMed:19380575};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate(out) = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate(in); Xref=Rhea:RHEA:71395, ChEBI:CHEBI:32395;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:Q6PCB7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain
CC fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- ACTIVITY REGULATION: Inhibited by Triacsin C.
CC {ECO:0000250|UniProtKB:Q60714}.
CC -!- SUBUNIT: Self-associates. May function as a homodimer. Interacts with
CC EPRS1; mediates the translocation of SLC27A1 from the cytoplasm to the
CC plasma membrane thereby increasing the uptake of long-chain fatty acids
CC (By similarity). Interacts with DGAT2 and this interaction is enhanced
CC in the presence of ZFYVE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q60714, ECO:0000250|UniProtKB:Q6PCB7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15848183,
CC ECO:0000269|PubMed:19380575}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q60714}. Endomembrane system
CC {ECO:0000269|PubMed:15848183}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q60714}. Cytoplasm
CC {ECO:0000269|PubMed:15848183}. Note=Plasma membrane and intracellular
CC membranes, at least in adipocytes. In adipocytes, but not myocytes,
CC insulin via the mTORC1 signaling pathway induces a rapid translocation
CC of SLC27A1 from intracellular compartments to the plasma membrane,
CC paralleled by increased LCFA uptake. Insulin-dependent translocation
CC from the cytoplasm to the cell membrane is regulated by EPRS1.
CC Predominantly cytoplasmic in myocytes. {ECO:0000250|UniProtKB:Q60714}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle. {ECO:0000269|PubMed:19380575}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U89529; AAC53424.1; -; mRNA.
DR AlphaFoldDB; P97849; -.
DR SMR; P97849; -.
DR STRING; 10116.ENSRNOP00000024659; -.
DR iPTMnet; P97849; -.
DR PhosphoSitePlus; P97849; -.
DR PaxDb; P97849; -.
DR PRIDE; P97849; -.
DR UCSC; RGD:620927; rat.
DR RGD; 620927; Slc27a1.
DR eggNOG; KOG1179; Eukaryota.
DR InParanoid; P97849; -.
DR PhylomeDB; P97849; -.
DR Reactome; R-RNO-804914; Transport of fatty acids.
DR PRO; PR:P97849; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:RGD.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; IEA:RHEA.
DR GO; GO:0090434; F:oleoyl-CoA ligase activity; ISO:RGD.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:RGD.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; ISO:RGD.
DR GO; GO:1905135; P:biotin import across plasma membrane; ISO:RGD.
DR GO; GO:0015878; P:biotin transport; ISO:RGD.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:RGD.
DR GO; GO:0140115; P:export across plasma membrane; ISO:RGD.
DR GO; GO:0015908; P:fatty acid transport; ISO:RGD.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISO:RGD.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:RGD.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISS:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:RGD.
DR GO; GO:0001579; P:medium-chain fatty acid transport; ISO:RGD.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; ISO:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:RGD.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISO:RGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:RGD.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; ISO:RGD.
DR GO; GO:0031652; P:positive regulation of heat generation; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR030308; FATP1.
DR PANTHER; PTHR43107:SF7; PTHR43107:SF7; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Long-chain fatty acid transport protein 1"
FT /id="PRO_0000193203"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT REGION 191..475
FT /note="Sufficient for oligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT BINDING 246..257
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
SQ SEQUENCE 646 AA; 71283 MW; C450CF174CC2EB87 CRC64;
MRTPGAGTAS VASLGLLWLL GLPWTWSAAA AFGVYVGSGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HRRAGDTIPR IFQAVAQRQP ERLALVDASS GICWTFAQLD TYSNAVANLF
LQLGFAPGDV VAVFLEGRPE FVGLWLGLAK AGVVAALLNV NLRREPLAFC LGTSAAKALI
YGGEMAAAVA EVSEQLGKSL LKFCSGDLGP ESVLPDTQLL DPMLAEAPTT PLAQAPGKGM
DDRLFYIYTS GTTGLPKAAI VVHSRYYRIA AFGHHSYSMR ANDVLYDCLP LYHSAGNIMG
VGQCIIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLRQPVR DVERRHRVRL
AVGNGLRPAI WEEFTQGFGV RQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILTHVYPIR
LVKVNEDTME PLRDSQGLCI PCQPGEPGLL VGQINQQDPL RRFDGYVSDS ATNKKIAHSV
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEAVLSR LLGQTDVAVY
GVAVPGVEGK SGMAAIADPH NQLDPNSMYQ ELQKVLASYA QPIFLRLLPQ VDTTGTFKIQ
KTRLQREGFD PRQTSDRLFF LDLKQGRYLP LDERVHARIC AGDFSL
