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Tchem Long-chain fatty acid transport protein 1

Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (By similarity).

 Comments

Property Summary

Ligand Count 34
NCBI Gene PubMed Count 26
PubMed Score 151.54
PubTator Score 65.87

Knowledge Summary

Patent

No data available

TINX Plot

  Disease (4)

Disease Target Count P-value
inflammatory breast cancer 286 2.9e-04
medulloblastoma, large-cell 6241 4.0e-03
invasive ductal carcinoma 2951 4.1e-03
Disease Target Count Z-score Confidence
Carcinoma 11493 0.0 0.7
Disease Target Count Z-score Confidence
Mental Depression 333 0.0 1.2
Disease Target Count Z-score Confidence
Obesity 678 4.007 2.0
Melkersson-Rosenthal syndrome 4 3.308 1.7

Expression

  Differential Expression (3)

Disease log2 FC p
inflammatory breast cancer -1.400 2.9e-04
invasive ductal carcinoma -1.100 4.1e-03
medulloblastoma, large-cell -1.200 4.0e-03

Synonym

Accession Q6PCB7 A6NIH2 B7Z662 FATP-1
Symbols FATP
FATP1
ACSVL5
FATP-1

Gene

SLC27A1

PANTHER Protein Class (1)

  Ortholog (1)

Species Source Disease
Chimp OMA EggNOG

 UniProt Keyword (14)

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 GO Function (5)

 GO Component (4)

 GO Process (16)

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 Compartment GO Term (19)

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 MGI Phenotype (3)

 GWAS Trait (1)

 HCA RNA Cell Line (56)

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Pathway (12)

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Ligand (34)

Structure of CHEMBL2058345

CHEMBL2058345
pIC50 6.05

Structure of CHEMBL2377618

CHEMBL2377618
pIC50 6.11

Structure of CHEMBL2058344

CHEMBL2058344
pIC50 6.17

Structure of CHEMBL2058346

CHEMBL2058346
pIC50 6.22

Structure of CHEMBL2057220

CHEMBL2057220
pIC50 6.24

Structure of CHEMBL2058078

CHEMBL2058078
pIC50 6.27

Structure of CHEMBL2377623

CHEMBL2377623
pIC50 6.28

Structure of CHEMBL2377762

CHEMBL2377762
pIC50 6.31

Structure of CHEMBL2377765

CHEMBL2377765
pIC50 6.31

Structure of CHEMBL2377612

CHEMBL2377612
pIC50 6.33

Structure of CHEMBL2377767

CHEMBL2377767
pIC50 6.37

Structure of CHEMBL2377619

CHEMBL2377619
pIC50 6.37

Structure of CHEMBL2058091

CHEMBL2058091
pIC50 6.40

Structure of CHEMBL2058339

CHEMBL2058339
pIC50 6.40

Structure of CHEMBL2058358

CHEMBL2058358
pIC50 6.44

Structure of CHEMBL2058076

CHEMBL2058076
pIC50 6.48

Structure of CHEMBL2377614

CHEMBL2377614
pIC50 6.48

Structure of CHEMBL2377760

CHEMBL2377760
pIC50 6.55

Structure of CHEMBL2058349

CHEMBL2058349
pIC50 6.59

Structure of CHEMBL2377761

CHEMBL2377761
pIC50 6.60

Gene RIF (15)

AA Sequence 

MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSVLIRVRLELRR      1 - 70
HQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE     71 - 140
FVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGP    141 - 210
EGILPDTHLLDPLLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQ    211 - 280
AADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVR    281 - 350
EAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR    351 - 420
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSVFSKGDSAYLS    421 - 490
GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPH    491 - 560
SLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGHYLP    561 - 630
LNEAVYTRICSGAFAL                                                          631 - 646
//

Text Mined References (28)

PMID Year Title