Q9Y2P5 · S27A5_HUMAN
- ProteinLong-chain fatty acid transport protein 5
- GeneSLC27A5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids690 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May mediate the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes (PubMed:20448275, PubMed:20530735).
Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:10479480).
Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine (PubMed:10749848, PubMed:11980911).
Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (PubMed:10749848, PubMed:11980911).
In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911).
Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity).
Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:10479480).
Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine (PubMed:10749848, PubMed:11980911).
Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (PubMed:10749848, PubMed:11980911).
In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911).
Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity).
Catalytic activity
- a fatty acid(in) = a fatty acid(out)
- ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA + diphosphateThis reaction proceeds in the forward direction.
- ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA + diphosphateThis reaction proceeds in the forward direction.
- ATP + CoA + lithocholate = AMP + diphosphate + lithocholoyl-CoAThis reaction proceeds in the forward direction.
- a very long-chain fatty acid + ATP + CoA = a very long-chain fatty acyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoAThis reaction proceeds in the forward direction.
- ATP + CoA + hexacosanoate = AMP + diphosphate + hexacosanoyl-CoAThis reaction proceeds in the forward direction.
- ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-CoAThis reaction proceeds in the forward direction.
- ATP + CoA + eicosanoate = AMP + diphosphate + eicosanoyl-CoAThis reaction proceeds in the forward direction.
Activity regulation
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA) inhibits the activation of cholate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.8 μM | cholate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3.8 nmol/min/mg | with cholate as substrate for bile acyl-CoA synthetase activity |
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameLong-chain fatty acid transport protein 5
- Short namesFATP-5 ; Fatty acid transport protein 5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y2P5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-30 | Cytoplasmic | ||||
Sequence: MGVRQQLALLLLLLLLLWGLGQPVWPVAVA | ||||||
Transmembrane | 31-51 | Helical | ||||
Sequence: LTLRWLLGDPTCCVLLGLAML | ||||||
Transmembrane | 56-76 | Helical | ||||
Sequence: LGPWVPHGLSLAAAALALTLL | ||||||
Topological domain | 77-690 | Cytoplasmic | ||||
Sequence: PARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048243 | 50 | in dbSNP:rs35350976 | |||
Sequence: M → T | ||||||
Natural variant | VAR_048244 | 53 | in dbSNP:rs34415062 | |||
Sequence: R → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 894 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193213 | 1-690 | Long-chain fatty acid transport protein 5 | |||
Sequence: MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL | ||||||
Modified residue | 501 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Predominantly expressed in liver.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y2P5 | MEOX2 Q6FHY5 | 3 | EBI-12176609, EBI-16439278 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y2P5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length690
- Mass (Da)75,385
- Last updated1999-11-01 v1
- Checksum011313424D794546
Q9Y2P5-2
- Name2
- Differences from canonical
- 146-229: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0R075 | M0R075_HUMAN | SLC27A5 | 95 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055810 | 146-229 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF064255 EMBL· GenBank· DDBJ | AAD29444.1 EMBL· GenBank· DDBJ | mRNA | ||
AK123036 EMBL· GenBank· DDBJ | BAG53858.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298446 EMBL· GenBank· DDBJ | BAG60663.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012313 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471135 EMBL· GenBank· DDBJ | EAW72601.1 EMBL· GenBank· DDBJ | Genomic DNA |