ID S27A4_MOUSE Reviewed; 643 AA.
AC Q91VE0; O88562; Q3TD48;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 173.
DE RecName: Full=Long-chain fatty acid transport protein 4 {ECO:0000303|PubMed:20448275};
DE Short=FATP-4 {ECO:0000303|PubMed:20448275};
DE Short=Fatty acid transport protein 4 {ECO:0000303|PubMed:15699031};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000269|PubMed:15699031};
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 4;
DE AltName: Full=Very long-chain acyl-CoA synthetase 4 {ECO:0000250|UniProtKB:Q6P1M0};
DE Short=ACSVL4 {ECO:0000250|UniProtKB:Q6P1M0};
DE EC=6.2.1.- {ECO:0000269|PubMed:15699031};
GN Name=Slc27a4 {ECO:0000312|MGI:MGI:1347347};
GN Synonyms=Acsvl4, Fatp4 {ECO:0000303|PubMed:15699031};
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 [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11404000; DOI=10.1016/s0378-1119(01)00489-9;
RA Herrmann T., Buchkremer F., Gosch I., Hall A.M., Bernlohr D.A.,
RA Stremmel W.;
RT "Mouse fatty acid transport protein 4 (FATP4): characterization of the gene
RT and functional assessment as a very long chain acyl-CoA synthetase.";
RL Gene 270:31-40(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-643, AND TISSUE SPECIFICITY.
RX PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
RA Hirsch D., Stahl A., Lodish H.F.;
RT "A family of fatty acid transporters conserved from mycobacterium to man.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
RN [6]
RP FUNCTION IN FATTY ACID TRANSPORT, AND TISSUE SPECIFICITY.
RX PubMed=10518211; DOI=10.1016/s1097-2765(00)80332-9;
RA Stahl A., Hirsch D.J., Gimeno R.E., Punreddy S., Ge P., Watson N.,
RA Patel S., Kotler M., Raimondi A., Tartaglia L.A., Lodish H.F.;
RT "Identification of the major intestinal fatty acid transport protein.";
RL Mol. Cell 4:299-308(1999).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=14512415; DOI=10.1074/jbc.m309759200;
RA Gimeno R.E., Hirsch D.J., Punreddy S., Sun Y., Ortegon A.M., Wu H.,
RA Daniels T., Stricker-Krongrad A., Lodish H.F., Stahl A.;
RT "Targeted deletion of fatty acid transport protein-4 results in early
RT embryonic lethality.";
RL J. Biol. Chem. 278:49512-49516(2003).
RN [8]
RP FUNCTION.
RX PubMed=12821645; DOI=10.1083/jcb.200207080;
RA Herrmann T., van der Hoeven F., Grone H.J., Stewart A.F., Langbein L.,
RA Kaiser I., Liebisch G., Gosch I., Buchkremer F., Drobnik W., Schmitz G.,
RA Stremmel W.;
RT "Mice with targeted disruption of the fatty acid transport protein 4 (Fatp
RT 4, Slc27a4) gene show features of lethal restrictive dermopathy.";
RL J. Cell Biol. 161:1105-1115(2003).
RN [9]
RP DISEASE.
RX PubMed=12697906; DOI=10.1073/pnas.0431186100;
RA Moulson C.L., Martin D.R., Lugus J.J., Schaffer J.E., Lind A.C.,
RA Miner J.H.;
RT "Cloning of wrinkle-free, a previously uncharacterized mouse mutation,
RT reveals crucial roles for fatty acid transport protein 4 in skin and hair
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5274-5279(2003).
RN [10]
RP FUNCTION AS AN ACYL-COA LIGASE.
RX PubMed=15653672; DOI=10.1074/jbc.m412629200;
RA Hall A.M., Wiczer B.M., Herrmann T., Stremmel W., Bernlohr D.A.;
RT "Enzymatic properties of purified murine fatty acid transport protein 4 and
RT analysis of acyl-CoA synthetase activities in tissues from FATP4 null
RT mice.";
RL J. Biol. Chem. 280:11948-11954(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRANSPORT ACTIVITY.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [14]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=20448275; DOI=10.1177/1087057110369700;
RA Zhou W., Madrid P., Fluitt A., Stahl A., Xie X.S.;
RT "Development and validation of a high-throughput screening assay for human
RT long-chain fatty acid transport proteins 4 and 5.";
RL J. Biomol. Screen. 15:488-497(2010).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23407971; DOI=10.1523/jneurosci.2428-12.2013;
RA Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G., Miner J.H.,
RA Jin M.;
RT "Fatty acid transport protein 4 (FATP4) prevents light-induced degeneration
RT of cone and rod photoreceptors by inhibiting RPE65 isomerase.";
RL J. Neurosci. 33:3178-3189(2013).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport across cell membranes
CC (PubMed:10518211, PubMed:20448275). Appears to be the principal fatty
CC acid transporter in small intestinal enterocytes (PubMed:20448275).
CC Also functions as an acyl-CoA ligase catalyzing the ATP-dependent
CC formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids
CC (VLCFA) as substrates, which prevents fatty acid efflux from cells and
CC might drive more fatty acid uptake (By similarity). Plays a role in the
CC formation of the epidermal barrier. Required for fat absorption in
CC early embryogenesis (PubMed:11404000, PubMed:12821645, PubMed:15653672,
CC PubMed:15699031). Probably involved in fatty acid transport across the
CC blood barrier (By similarity). Indirectly inhibits RPE65 via substrate
CC competition and via production of VLCFA derivatives like lignoceroyl-
CC CoA. Prevents light-induced degeneration of rods and cones
CC (PubMed:23407971). {ECO:0000250|UniProtKB:Q6P1M0,
CC ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000,
CC ECO:0000269|PubMed:12821645, ECO:0000269|PubMed:15653672,
CC ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20448275,
CC ECO:0000269|PubMed:23407971}.
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:15699031,
CC ECO:0000269|PubMed:20448275};
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:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
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 -!- 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=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: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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23407971}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in small intestine,
CC brain, kidney, liver, skin and heart. In small intestine, expressed at
CC high levels on the apical side of mature enterocytes. Highly expressed
CC by the epithelial cells of the visceral endoderm and localized to the
CC brush-border membrane of extraembryonic endodermal cells (at protein
CC level). Expressed in the retinal pigment epithelium and in the retina
CC (at protein level). Expressed in the retinal pigment epithelium and in
CC the retina. {ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000,
CC ECO:0000269|PubMed:14512415, ECO:0000269|PubMed:23407971,
CC ECO:0000269|PubMed:9671728}.
CC -!- DISEASE: Note=Defects in Slc27a4 are the cause of wrinkle-free (wrfr)
CC phenotype. It is a spontaneous, autosomal recessive mutation resulting
CC in very tight, thick skin and is secondary characterized by severe
CC breathing difficulties. Mice die shortly after birth. This phenotype is
CC similar to human restrictive dermopathy, a very rare human genetic
CC disorder. {ECO:0000269|PubMed:12697906}.
CC -!- MISCELLANEOUS: Slc27a4 deficient mice display features of a neonatally
CC lethal restrictive dermopathy. Their skin is characterized by
CC hyperproliferative hyperkeratosis with a disturbed epidermal barrier, a
CC flat dermal-epidermal junction, a reduced number of pilo-sebaceous
CC structures, and a compact dermis. The rigid skin consistency results in
CC an altered body shape with facial dysmorphia, generalized joint flexion
CC contractures and impaired movement including suckling and breathing
CC deficiencies. Lipid analysis demonstrates a disturbed fatty acid
CC composition of epidermal ceramides, in particular a decrease in the
CC C26:0 and C26:0-OH fatty acid substitutes.
CC -!- MISCELLANEOUS: Deletion of Slc27a4 results in embryonic lethality,
CC which has been attributed to a requirement for fat absorption early in
CC embryonic development across the visceral endoderm.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC40188.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC40188.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AJ251113; CAC42082.1; -; mRNA.
DR EMBL; AJ276492; CAC42083.1; -; Genomic_DNA.
DR EMBL; AK036919; BAC29639.1; -; mRNA.
DR EMBL; AK155388; BAE33236.1; -; mRNA.
DR EMBL; AK170377; BAE41756.1; -; mRNA.
DR EMBL; CT010312; CAJ18520.1; -; mRNA.
DR EMBL; BC023114; AAH23114.1; -; mRNA.
DR EMBL; AF072759; AAC40188.1; ALT_SEQ; mRNA.
DR CCDS; CCDS15858.1; -.
DR RefSeq; NP_036119.1; NM_011989.4.
DR AlphaFoldDB; Q91VE0; -.
DR SMR; Q91VE0; -.
DR BioGRID; 205025; 6.
DR IntAct; Q91VE0; 2.
DR MINT; Q91VE0; -.
DR STRING; 10090.ENSMUSP00000078971; -.
DR SwissLipids; SLP:000001141; -.
DR TCDB; 4.C.1.1.1; the fatty acid group translocation (fat) family.
DR iPTMnet; Q91VE0; -.
DR PhosphoSitePlus; Q91VE0; -.
DR SwissPalm; Q91VE0; -.
DR EPD; Q91VE0; -.
DR MaxQB; Q91VE0; -.
DR PaxDb; 10090-ENSMUSP00000078971; -.
DR PeptideAtlas; Q91VE0; -.
DR ProteomicsDB; 260770; -.
DR Pumba; Q91VE0; -.
DR Antibodypedia; 1947; 222 antibodies from 31 providers.
DR DNASU; 26569; -.
DR Ensembl; ENSMUST00000080065.3; ENSMUSP00000078971.3; ENSMUSG00000059316.3.
DR GeneID; 26569; -.
DR KEGG; mmu:26569; -.
DR UCSC; uc008jaf.1; mouse.
DR AGR; MGI:1347347; -.
DR CTD; 10999; -.
DR MGI; MGI:1347347; Slc27a4.
DR VEuPathDB; HostDB:ENSMUSG00000059316; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000158646; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q91VE0; -.
DR OMA; WRFIRIF; -.
DR OrthoDB; 1650656at2759; -.
DR PhylomeDB; Q91VE0; -.
DR TreeFam; TF313430; -.
DR BRENDA; 6.2.1.3; 3474.
DR Reactome; R-MMU-804914; Transport of fatty acids.
DR BioGRID-ORCS; 26569; 6 hits in 78 CRISPR screens.
DR ChiTaRS; Slc27a4; mouse.
DR PRO; PR:Q91VE0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91VE0; Protein.
DR Bgee; ENSMUSG00000059316; Expressed in small intestine Peyer's patch and 247 other cell types or tissues.
DR Genevisible; Q91VE0; MM.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ARUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
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; IDA:ARUK-UCL.
DR GO; GO:0090433; F:palmitoyl-CoA ligase activity; ISO:MGI.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IMP:ARUK-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:ARUK-UCL.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:MGI.
DR GO; GO:0001579; P:medium-chain fatty acid transport; IDA:MGI.
DR GO; GO:0062003; P:negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity; IDA:CACAO.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:MGI.
DR CDD; cd05939; hsFATP4_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR022272; Lipocalin_CS.
DR PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR43107:SF11; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN 4; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein 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_0000193211"
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 330
FT /note="I -> V (in Ref. 5; AAC40188)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="P -> S (in Ref. 2; BAE41756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72319 MW; 10B3E9730FDF586A CRC64;
MLLGASLVGA LLFSKLVLKL PWTQVGFSLL LLYLGSGGWR FIRVFIKTVR RDIFGGMVLL
KVKTKVRRYL QERKTVPLLF ASMVQRHPDK TALIFEGTDT HWTFRQLDEY SSSVANFLQA
RGLASGNVVA LFMENRNEFV GLWLGMAKLG VEAALINTNL RRDALRHCLD TSKARALIFG
SEMASAICEI HASLEPTLSL FCSGSWEPST VPVSTEHLDP LLEDAPKHLP SHPDKGFTDK
LFYIYTSGTT GLPKAAIVVH SRYYRMASLV YYGFRMRPDD IVYDCLPLYH SAGNIVGIGQ
CLLHGMTVVI RKKFSASRFW DDCIKYNCTI VQYIGELCRY LLNQPPREAE SRHKVRMALG
NGLRQSIWTD FSSRFHIPQV AEFYGATECN CSLGNFDSRV GACGFNSRIL SFVYPIRLVR
VNEDTMELIR GPDGVCIPCQ PGQPGQLVGR IIQQDPLRRF DGYLNQGANN KKIANDVFKK
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLH MADVAVYGVE
VPGTEGRAGM AAVASPISNC DLESFAQTLK KELPLYARPI FLRFLPELHK TGTFKFQKTE
LRKEGFDPSV VKDPLFYLDA RKGCYVALDQ EAYTRIQAGE EKL
//
