S27A4_PONAB
ID S27A4_PONAB Reviewed; 643 AA.
AC Q5RDY4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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 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; CR857758; CAH90023.1; -; mRNA.
DR RefSeq; NP_001124962.1; NM_001131490.1.
DR AlphaFoldDB; Q5RDY4; -.
DR SMR; Q5RDY4; -.
DR STRING; 9601.ENSPPYP00000022022; -.
DR GeneID; 100171835; -.
DR KEGG; pon:100171835; -.
DR CTD; 10999; -.
DR eggNOG; KOG1179; Eukaryota.
DR InParanoid; Q5RDY4; -.
DR OrthoDB; 298283at2759; -.
DR Proteomes; UP000001595; 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; 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; IPR030304; FATP4.
DR InterPro; IPR022272; Lipocalin_CS.
DR PANTHER; PTHR43107:SF11; PTHR43107:SF11; 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 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_0000193212"
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"
SQ SEQUENCE 643 AA; 72228 MW; 99B2C878FADD51F8 CRC64;
MLLGASLVGV LLFSKLVLKL PWTQVGFSLL FLYLGSGGWR FIRVFIKTIR RDIFGGLVLL
KVKAKVRQCL RERRTVPILF ASTVRRHPDK TALIFEGTDT LWTFRQLDEY SSSVANFLQA
RGLASGDVAA IFMENRNEFV GLWLGMAKLG VEAALINTNL RRDAQLHCLT TSRARALVFG
SEMASAICEI HASLDPSLSL FCSGSWEPNA VPTSTEHLDP LLKDAPKHLP ICPDKGFTDK
LFYIYTSGTT GLPKAAIVVH SRYYRMAALV YYGFRMRPND IVYDCLPLYH SAGNIVGIGQ
CLLHGMTVVI RKKFSASRFW DDCIKYNCTI VQYIGELCRY LLNQPPREAE NQHQVRMALG
NGLRQSIWTN FSSRFHIPQV AEFYGATECN CSLGNFDSQV GACGFNSRIL SFVYPIRLVR
VNEDTMELIR GPDGICIPCQ PGEPGQLVGR IIQKDPLRRF DGYLNQGAND KKIAKDVFKK
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLD MADVAVYGVE
VPGTEGRAGM AAVASPTGNC DLERFAQVLE KELPLYARPI FLRLLPELHK TGTYKFQKTE
LRKEGFDPAI VKDPLFYLDA RKGRYVPLDQ EAYSRIQAGE EKL
