S27A4_MACFA
ID S27A4_MACFA Reviewed; 643 AA.
AC Q4R3Y4; G8F6C7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Long-chain fatty acid transport protein 4;
DE Short=FATP-4;
DE Short=Fatty acid transport protein 4;
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3;
DE AltName: Full=Solute carrier family 27 member 4;
DE AltName: Full=Very long-chain acyl-CoA synthetase 4;
DE Short=ACSVL4;
DE EC=6.2.1.-;
GN Name=SLC27A4; Synonyms=FATP4; ORFNames=QtsA-13277;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport across cell membranes. Appears to
CC be the principal fatty acid transporter in small intestinal
CC enterocytes. 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, which prevents fatty acid efflux
CC from cells and might drive more fatty acid uptake (By similarity).
CC Plays a role in the formation of the epidermal barrier. Required for
CC fat absorption in early embryogenesis (By similarity). Probably
CC involved in fatty acid transport across the blood barrier (By
CC similarity). Indirectly inhibits RPE65 via substrate competition and
CC via production of VLCFA derivatives like lignoceroyl-CoA. Prevents
CC light-induced degeneration of rods and cones (By similarity).
CC {ECO:0000250|UniProtKB:Q6P1M0, ECO:0000250|UniProtKB:Q91VE0}.
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:Q91VE0};
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:Q6P1M0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q6P1M0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q6P1M0};
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:Q6P1M0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q6P1M0};
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:Q91VE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q91VE0};
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:0000250|UniProtKB:Q91VE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:Q91VE0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q6P1M0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q6P1M0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q6P1M0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000250|UniProtKB:Q6P1M0};
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:Q91VE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000250|UniProtKB:Q91VE0};
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:Q91VE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q91VE0};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q91VE0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB179131; BAE02182.1; -; mRNA.
DR EMBL; JH336389; EHH62841.1; -; Genomic_DNA.
DR RefSeq; NP_001270937.1; NM_001284008.1.
DR RefSeq; XP_015291583.1; XM_015436097.1.
DR RefSeq; XP_015291584.1; XM_015436098.1.
DR RefSeq; XP_015291585.1; XM_015436099.1.
DR AlphaFoldDB; Q4R3Y4; -.
DR SMR; Q4R3Y4; -.
DR STRING; 9541.XP_005580812.1; -.
DR GeneID; 101866618; -.
DR KEGG; mcf:101866618; -.
DR CTD; 10999; -.
DR eggNOG; KOG1179; Eukaryota.
DR OrthoDB; 298283at2759; -.
DR Proteomes; UP000009130; Unassembled WGS sequence.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
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 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; IPR030304; FATP4.
DR InterPro; IPR022272; Lipocalin_CS.
DR PANTHER; PTHR43107:SF11; PTHR43107:SF11; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..643
FT /note="Long-chain fatty acid transport protein 4"
FT /id="PRO_0000193210"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 243..254
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
FT CONFLICT 553
FT /note="G -> V (in Ref. 1; BAE02182)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="L -> P (in Ref. 1; BAE02182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72194 MW; A64F4B8CCF4AD61B CRC64;
MLLGASLVGV LLFSKLVLKL PWTQVGFSLL FLYLGSGGWR FIRVFIKTIR RDIFGGLVLL
KVKAKVRQCL RERRTVPILF ASTVRRHPDK TALIFEGTDT HWTFRQLDEY SSSVANFLQA
RGLASGDVAA IFMENRNEFV GLWLGMAKLG VEAALINTNL RRDALLHCLT TSRARALVFG
SEMASAICEI HASLDPSLSL FCSGSWEPNA VPTSTEHLDP LLEDAPKHLP SCPDKGFTDK
LFYIYTSGTT GLPKAAIVVH SRYYRMAALV YYGFRMRPND IIYDCLPLYH SAGNIVGIGQ
CLLHGMTVVI RKKFSASRFW DDCIKYKCTI VQYIGELCRY LLNQPPREAE NQHQVRMALG
NGLRQSIWTN FSSRFHIPQV AEFYGATECN CSLGNFDSQV GACGFNSRIL SFVYPIRLVR
VNEDTMELIR GPDGICIPCQ PGEPGQLVGR IIQKDPLRRF DGYLNQGANN KKIAKDVFKK
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLD MADVAVYGVE
VPGTEGRAGM AAGASPTGNC DLERFAQDLE KELPLYARPI FLRILPELHK TGTYKLQKTE
LRKEGFDPAI VKDPLFYLDA RKGRYVLLDQ EAYSRIQAGE EKL
