S27A1_BOVIN
ID S27A1_BOVIN Reviewed; 646 AA.
AC Q3ZKN0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 1;
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:0000250|UniProtKB:Q6PCB7};
DE AltName: Full=Very long-chain acyl-CoA synthetase;
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q60714};
GN Name=SLC27A1 {ECO:0000250|UniProtKB:Q6PCB7}; Synonyms=FATP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ordovas L., Zaragoza P., Rodellar C.;
RT "Bovine solute carrier family 27 member 1 (SLC27A1) gene: structural and
RT functional analysis.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport at the plasma membrane. Also
CC functions as an acyl-CoA ligase catalyzing the ATP-dependent formation
CC of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as
CC substrates, which prevents fatty acid efflux from cells and might drive
CC more fatty acid uptake. May act directly as a bona fide transporter, or
CC alternatively, in a cytoplasmic or membrane-associated multimeric
CC protein complex to trap and draw fatty acids towards accumulation.
CC Plays a pivotal role in regulating available LCFA substrates from
CC exogenous sources in tissues undergoing high levels of beta-oxidation
CC or triglyceride synthesis. May be involved in regulation of cholesterol
CC metabolism. Probably involved in fatty acid transport across the blood
CC barrier (By similarity). {ECO:0000250|UniProtKB:Q60714,
CC ECO:0000250|UniProtKB:Q6PCB7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC ChEBI:CHEBI:28868; Evidence={ECO:0000250|UniProtKB:Q60714};
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:0000250|UniProtKB:Q6PCB7};
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:0000250|UniProtKB:Q60714};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q60714}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q60714}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:Q60714}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q60714}. 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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY738459; AAW68434.1; -; mRNA.
DR AlphaFoldDB; Q3ZKN0; -.
DR SMR; Q3ZKN0; -.
DR STRING; 9913.ENSBTAP00000050547; -.
DR PaxDb; Q3ZKN0; -.
DR PRIDE; Q3ZKN0; -.
DR eggNOG; KOG1179; Eukaryota.
DR InParanoid; Q3ZKN0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
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:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISS:UniProtKB.
DR GO; GO:0001579; P:medium-chain fatty acid transport; IBA:GO_Central.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IBA:GO_Central.
DR GO; GO:0031652; P:positive regulation of heat generation; IBA:GO_Central.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
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 Pfam; PF13193; AMP-binding_C; 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_0000193200"
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; 71123 MW; 59BA7D8CF6B05684 CRC64;
MRAPGAGSAS VASLVLLWLL GLPWTWSTAA ALGVYVGGGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HQRARHTIPQ IFQAVVQRQP ERLALVDAGS GACWTFAQLD AYSNAVANLF
RRLGFAPGDV VAIFMEGRPE FVGLWLGLAK AGVEAALLNV NLRREPLAFC LGTSGAKALV
FGGELAAAVA EMSGELGKSL VKFCSGDVGP DGVFPDTQLL DPLLKETSTA PLAQPPGKGM
DDRLFYIYTS GTTGLPKAAI IVHSRYYRIA AFGHYSYSMQ AADVLYDCLP LYHSAGNIMG
VGQCLIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLKQPVR EAEGRHRVRL
AVGNGLRPSI WEEFTERFGV RQIGEFYGAT ECNCSIANMD GKVGSRGFNS RILPHVYPIR
LVKVNEDTME LLRDAQGLCI PCQTGEPGLL VGQINQQDPL RRFDGYISES ATSKKIAHSV
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEGVLSR LLGQTDVAVY
GVAVPGVEGK ACMAAIADPH GRLSPNALYE ELQKVLAPYA RPIFLRLLPQ VDTTGTFKIQ
KTRLQHEGFD PRQTSDRLFF LDLKQGHYLP LDQGVYTRIC SGAFAL
