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Long-chain fatty acid transport protein 4 (FATP-4) (Fatty acid transport protein 4) (EC 6.2.1.-) (Solute carrier family 27 member 4)

 S27A4_HUMAN             Reviewed;         643 AA.
Q6P1M0; A8K2F7; O95186; Q96G53;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-OCT-2018, entry version 143.
RecName: Full=Long-chain fatty acid transport protein 4;
Short=FATP-4;
Short=Fatty acid transport protein 4;
EC=6.2.1.-;
AltName: Full=Solute carrier family 27 member 4;
Name=SLC27A4; Synonyms=ACSVL4, FATP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=9878842; DOI=10.1016/S0167-4781(98)00231-0;
Fitscher B.A., Riedel H.D., Young K.C., Stremmel W.;
"Tissue distribution and cDNA cloning of a human fatty acid transport
protein (hsFATP4).";
Biochim. Biophys. Acta 1443:381-385(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
VARIANT SER-209.
PubMed=14715877; DOI=10.1210/jc.2003-030682;
Gertow K., Bellanda M., Eriksson P., Boquist S., Hamsten A.,
Sunnerhagen M., Fisher R.M.;
"Genetic and structural evaluation of fatty acid transport protein-4
in relation to markers of the insulin resistance syndrome.";
J. Clin. Endocrinol. Metab. 89:392-399(2004).
[8]
VARIANTS IPS THR-92; PRO-247; ARG-300 AND HIS-583.
PubMed=19631310; DOI=10.1016/j.ajhg.2009.06.021;
Klar J., Schweiger M., Zimmerman R., Zechner R., Li H., Torma H.,
Vahlquist A., Bouadjar B., Dahl N., Fischer J.;
"Mutations in the fatty acid transport protein 4 gene cause the
ichthyosis prematurity syndrome.";
Am. J. Hum. Genet. 85:248-253(2009).
[9]
VARIANT IPS CYS-374.
PubMed=20815031; DOI=10.1002/ajmg.a.33648;
Morice-Picard F., Leaute-Labreze C., Decor A., Boralevi F.,
Lacombe D., Taieb A., Fischer J.;
"A novel mutation in the fatty acid transport protein 4 gene in a
patient initially described as affected by self-healing congenital
verruciform hyperkeratosis.";
Am. J. Med. Genet. A 152:2664-2665(2010).
-!- FUNCTION: Involved in translocation of long-chain fatty acids
(LFCA) across the plasma membrane. Appears to be the principal
fatty acid transporter in small intestinal enterocytes. Plays a
role in the formation of the epidermal barrier. Required for fat
absorption in early embryogenesis. Has acyl-CoA ligase activity
for long-chain and very-long-chain fatty acids (VLCFAs).
Indirectly inhibits RPE65 via substrate competition and via
production of VLCFA derivatives like lignoceroyl-CoA. Prevents
light-induced degeneration of rods and cones (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Endoplasmic reticulum membrane
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6P1M0-1; Sequence=Displayed;
Name=2;
IsoId=Q6P1M0-2; Sequence=VSP_055808, VSP_055809;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at highest levels in brain, testis,
colon and kidney. Expressed at medium levels in heart and liver,
small intestine and stomach. Expressed at low levels in peripheral
leukocytes, bone marrow, skeletal muscle and aorta. Expressed in
adipose tissue. {ECO:0000269|PubMed:9878842}.
-!- DISEASE: Ichthyosis prematurity syndrome (IPS) [MIM:608649]: A
keratinization disorder characterized by complications in the
second trimester of pregnancy resulting from polyhydramnion, with
premature birth of a child with thick caseous desquamating
epidermis, respiratory complications and transient eosinophilia.
After recovery during the first months of life, the symptoms are
relatively benign and the patients suffer from a lifelong non-
scaly ichthyosis with atopic manifestations.
{ECO:0000269|PubMed:19631310, ECO:0000269|PubMed:20815031}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: SLC27A4/FATP4-mediated fatty acid uptake is
associated to paramaters related to insulin resistance, which is
associated with disturbed fatty acid metabolism and homeostasis,
such as obesity. SLC27A4/FATP4 expression is positively correlated
with acquired obesity.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD11623.1; Type=Frameshift; Positions=362, 387, 612, 619; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF055899; AAD11623.1; ALT_FRAME; mRNA.
EMBL; AK290222; BAF82911.1; -; mRNA.
EMBL; AL359091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87779.1; -; Genomic_DNA.
EMBL; BC009959; AAH09959.1; -; mRNA.
EMBL; BC065003; AAH65003.1; -; mRNA.
CCDS; CCDS6899.1; -. [Q6P1M0-1]
RefSeq; NP_005085.2; NM_005094.3. [Q6P1M0-1]
RefSeq; XP_016869711.1; XM_017014222.1. [Q6P1M0-1]
UniGene; Hs.656699; -.
ProteinModelPortal; Q6P1M0; -.
BioGrid; 116192; 26.
IntAct; Q6P1M0; 22.
MINT; Q6P1M0; -.
STRING; 9606.ENSP00000300456; -.
BindingDB; Q6P1M0; -.
ChEMBL; CHEMBL4327; -.
GuidetoPHARMACOLOGY; 1111; -.
SwissLipids; SLP:000000451; -.
TCDB; 4.C.1.1.10; the fatty acid transporter (fat) family.
iPTMnet; Q6P1M0; -.
PhosphoSitePlus; Q6P1M0; -.
SwissPalm; Q6P1M0; -.
BioMuta; SLC27A4; -.
DMDM; 74749065; -.
EPD; Q6P1M0; -.
MaxQB; Q6P1M0; -.
PaxDb; Q6P1M0; -.
PeptideAtlas; Q6P1M0; -.
PRIDE; Q6P1M0; -.
ProteomicsDB; 66849; -.
Ensembl; ENST00000300456; ENSP00000300456; ENSG00000167114. [Q6P1M0-1]
Ensembl; ENST00000372870; ENSP00000361961; ENSG00000167114. [Q6P1M0-2]
GeneID; 10999; -.
KEGG; hsa:10999; -.
UCSC; uc004but.4; human. [Q6P1M0-1]
CTD; 10999; -.
DisGeNET; 10999; -.
EuPathDB; HostDB:ENSG00000167114.12; -.
GeneCards; SLC27A4; -.
HGNC; HGNC:10998; SLC27A4.
HPA; CAB009771; -.
HPA; HPA007293; -.
MalaCards; SLC27A4; -.
MIM; 604194; gene.
MIM; 608649; phenotype.
neXtProt; NX_Q6P1M0; -.
OpenTargets; ENSG00000167114; -.
Orphanet; 88621; Ichthyosis prematurity syndrome.
PharmGKB; PA35872; -.
eggNOG; KOG1179; Eukaryota.
eggNOG; ENOG410XQ8T; LUCA.
GeneTree; ENSGT00550000074420; -.
HOGENOM; HOG000293292; -.
HOVERGEN; HBG074666; -.
InParanoid; Q6P1M0; -.
KO; K08745; -.
OMA; FQGYYGN; -.
OrthoDB; EOG091G0B76; -.
PhylomeDB; Q6P1M0; -.
TreeFam; TF313430; -.
BRENDA; 6.2.1.3; 2681.
Reactome; R-HSA-5619108; Defective SLC27A4 causes ichthyosis prematurity syndrome (IPS).
Reactome; R-HSA-804914; Transport of fatty acids.
ChiTaRS; SLC27A4; human.
GeneWiki; SLC27A4; -.
GenomeRNAi; 10999; -.
PRO; PR:Q6P1M0; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000167114; Expressed in 169 organ(s), highest expression level in esophagus mucosa.
CleanEx; HS_SLC27A4; -.
ExpressionAtlas; Q6P1M0; baseline and differential.
Genevisible; Q6P1M0; HS.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015245; F:fatty acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:Ensembl.
GO; GO:0015908; P:fatty acid transport; TAS:ProtInc.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0015909; P:long-chain fatty acid transport; TAS:Reactome.
GO; GO:0001579; P:medium-chain fatty acid transport; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043588; P:skin development; IEA:Ensembl.
GO; GO:0042760; P:very long-chain fatty acid catabolic process; IEA:Ensembl.
CDD; cd05939; hsFATP4_like; 1.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR030304; FATP4.
InterPro; IPR022272; Lipocalin_CS.
PANTHER; PTHR43107:SF11; PTHR43107:SF11; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Endoplasmic reticulum; Fatty acid metabolism; Ichthyosis; Ligase;
Lipid metabolism; Lipid transport; Membrane; Nucleotide-binding;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 643 Long-chain fatty acid transport protein
4.
/FTId=PRO_0000193209.
TRANSMEM 20 42 Helical. {ECO:0000255}.
TRANSMEM 139 156 Helical. {ECO:0000255}.
NP_BIND 243 254 AMP. {ECO:0000255}.
VAR_SEQ 1 76 MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRF
IRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTV -> MP
LTLSTLLQPGRIWTGRRAAEPTPGHNAAWSLSGGGAAVLQA
GAETALDPGGILPVVPLLGIWRLALHPGLHQDH (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055808.
VAR_SEQ 77 482 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055809.
VARIANT 92 92 A -> T (in IPS; dbSNP:rs137853132).
{ECO:0000269|PubMed:19631310}.
/FTId=VAR_063192.
VARIANT 209 209 G -> S (correlates with lower body mass
index, triglyceride concentrations,
systolic blood pressure, insulin
concentrations and homeostasis model
assessment index; dbSNP:rs2240953).
{ECO:0000269|PubMed:14715877}.
/FTId=VAR_023783.
VARIANT 247 247 S -> P (in IPS; dbSNP:rs137853133).
{ECO:0000269|PubMed:19631310}.
/FTId=VAR_063193.
VARIANT 300 300 Q -> R (in IPS; dbSNP:rs137853134).
{ECO:0000269|PubMed:19631310}.
/FTId=VAR_063194.
VARIANT 374 374 R -> C (in IPS; dbSNP:rs768495407).
{ECO:0000269|PubMed:20815031}.
/FTId=VAR_064500.
VARIANT 583 583 R -> H (in IPS; dbSNP:rs137853135).
{ECO:0000269|PubMed:19631310}.
/FTId=VAR_063195.
CONFLICT 194 194 L -> P (in Ref. 1; AAD11623).
{ECO:0000305}.
CONFLICT 605 605 G -> A (in Ref. 1; AAD11623).
{ECO:0000305}.
SEQUENCE 643 AA; 72064 MW; 95E677DB3CEB9A14 CRC64;
MLLGASLVGV LLFSKLVLKL PWTQVGFSLL FLYLGSGGWR FIRVFIKTIR RDIFGGLVLL
KVKAKVRQCL QERRTVPILF ASTVRRHPDK TALIFEGTDT HWTFRQLDEY SSSVANFLQA
RGLASGDVAA IFMENRNEFV GLWLGMAKLG VEAALINTNL RRDALLHCLT TSRARALVFG
SEMASAICEV HASLDPSLSL FCSGSWEPGA VPPSTEHLDP LLKDAPKHLP SCPDKGFTDK
LFYIYTSGTT GLPKAAIVVH SRYYRMAALV YYGFRMRPND IVYDCLPLYH SAGNIVGIGQ
CLLHGMTVVI RKKFSASRFW DDCIKYNCTI VQYIGELCRY LLNQPPREAE NQHQVRMALG
NGLRQSIWTN FSSRFHIPQV AEFYGATECN CSLGNFDSQV GACGFNSRIL SFVYPIRLVR
VNEDTMELIR GPDGVCIPCQ PGEPGQLVGR IIQKDPLRRF DGYLNQGANN KKIAKDVFKK
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLD MADVAVYGVE
VPGTEGRAGM AAVASPTGNC DLERFAQVLE KELPLYARPI FLRLLPELHK TGTYKFQKTE
LRKEGFDPAI VKDPLFYLDA QKGRYVPLDQ EAYSRIQAGE EKL


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E07F0031 Porcine Fatty Acid Transport Protein ELISA , FATP 96 Tests/kit
E03F0031 Mouse Fatty Acid Transport Protein ELISA ,FATP 96 Tests/kit
E09F0031 Monkey Fatty Acid Transport Protein ELISA , FATP
E06F0031 Goat Fatty Acid Transport Protein ELISA , FATP 96 Tests/kit


 

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