S27A6_MOUSE
ID S27A6_MOUSE Reviewed; 619 AA.
AC E9Q9W4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Long-chain fatty acid transport protein 6 {ECO:0000305};
DE Short=FATP-6 {ECO:0000303|PubMed:15699031};
DE Short=Fatty acid transport protein 6;
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000269|PubMed:15699031};
DE AltName: Full=Fatty-acid-coenzyme A ligase, very long-chain 2;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000269|PubMed:15699031};
DE AltName: Full=Solute carrier family 27 member 6;
DE AltName: Full=Very long-chain acyl-CoA synthetase homolog 1;
DE Short=VLACS2 {ECO:0000303|PubMed:15699031};
DE Short=VLCSH1 {ECO:0000303|PubMed:15699031};
DE Short=mVLCS-H1;
DE EC=6.2.1.- {ECO:0000269|PubMed:15699031};
GN Name=Slc27a6; Synonyms=Acsvl2, Facvl2, Fatp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=15699031; DOI=10.1074/jbc.m409598200;
RA DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
RT "Comparative biochemical studies of the murine fatty acid transport
RT proteins (FATP) expressed in yeast.";
RL J. Biol. Chem. 280:16829-16837(2005).
RN [3] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport at the plasma membrane (By
CC similarity). Also functions as an acyl-CoA ligase catalyzing the ATP-
CC dependent formation of fatty acyl-CoA using LCFA and very-long-chain
CC fatty acids (VLCFA) as substrates (PubMed:15699031). Plays a pivotal
CC role in regulating available LCFA substrates from exogenous sources in
CC tissues undergoing high levels of beta-oxidation such as the heart (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2P4,
CC ECO:0000269|PubMed:15699031}.
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:Q9Y2P4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q9Y2P4};
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:Q9Y2P4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P4};
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:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000269|PubMed:15699031};
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:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:15699031};
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:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:15699031};
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:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:15699031};
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9Y2P4}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:15699031}; Multi-pass
CC membrane protein {ECO:0000255}. Note=In heart is exclusively located on
CC the sarcolemma in areas juxtaposed with small blood vessels where it
CC colocalizes CD36. {ECO:0000250|UniProtKB:Q9Y2P4}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC102231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37828.1; -.
DR RefSeq; NP_001074541.1; NM_001081072.1.
DR AlphaFoldDB; E9Q9W4; -.
DR SMR; E9Q9W4; -.
DR STRING; 10090.ENSMUSP00000025500; -.
DR SwissLipids; SLP:000001143; -.
DR iPTMnet; E9Q9W4; -.
DR PhosphoSitePlus; E9Q9W4; -.
DR MaxQB; E9Q9W4; -.
DR PaxDb; E9Q9W4; -.
DR PRIDE; E9Q9W4; -.
DR ProteomicsDB; 351306; -.
DR Antibodypedia; 1944; 89 antibodies from 21 providers.
DR DNASU; 225579; -.
DR Ensembl; ENSMUST00000025500; ENSMUSP00000025500; ENSMUSG00000024600.
DR GeneID; 225579; -.
DR KEGG; mmu:225579; -.
DR UCSC; uc008ezp.1; mouse.
DR CTD; 28965; -.
DR MGI; MGI:3036230; Slc27a6.
DR VEuPathDB; HostDB:ENSMUSG00000024600; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000159700; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; E9Q9W4; -.
DR OMA; NIKMCEF; -.
DR OrthoDB; 386992at2759; -.
DR PhylomeDB; E9Q9W4; -.
DR TreeFam; TF313430; -.
DR Reactome; R-MMU-804914; Transport of fatty acids.
DR BioGRID-ORCS; 225579; 3 hits in 72 CRISPR screens.
DR PRO; PR:E9Q9W4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; E9Q9W4; protein.
DR Bgee; ENSMUSG00000024600; Expressed in spermatocyte and 59 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
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; IDA:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; TAS:MGI.
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; IPR030309; FATP6.
DR PANTHER; PTHR43107:SF10; PTHR43107:SF10; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..619
FT /note="Long-chain fatty acid transport protein 6"
FT /id="PRO_0000449573"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 221..232
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 70192 MW; DF3E336D1047D72D CRC64;
MLLSWLTGLG AGLLSLHFLQ KLLFPYFWDD FWYLLKVVRY GIQMEMYKLR GELVTVLDKF
LSHTRKQPRK AFIIYEGDVY TYEDVDKRSN RIAHALLNHS SLKRGDVVAL LMSNEPDFVH
VWFGLAKLGC VVAFLNSNLR FDSLLHCINT CEPTAVVVGG DLLGSIEEIL PSLPKHVRVW
GMKDSVPEGI DSLQEKLSLA SDEPVPPSHH VTSSLKSTCL YIFTSGTTGL PKAAVISQLQ
VLKGSVGLWA FGCTADDIIY ITLPLYHSSG SLLGIGGCVE LGATCVLKKK FSASQFWNDC
KKYNVTVFQY IGELCRYLCK QPQREGEKDH RVRLAVGNGL SSDVWRQFLD RFGNIKMCEL
YGATEGNIVF MNHTGKIGSV GRANFFYSLF FSFELIKYDF QKDEPWRNGQ GWCSCVRKGE
PGLLISRVNK KNPFFGYAGS DTHTKSKLLF DVFRKGDVYF NTGDLMFQDQ ENFVYFWDRL
GDTFRWKGEN VATTEVADVL GRLDFIQEAN VYGVRVPGYE GKAGMTSVIL KPNKSLDLEK
MYNQVVTSLP AYACPLFLRI QDKMETTGTF KLKKLQLVEE GFDPLKISDP LYFMDNLKKS
YVPLTEEIYN QIMSEEVKL
