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Q6PCB7 (S27A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Long-chain fatty acid transport protein 1

Short name=FATP-1
Short name=Fatty acid transport protein 1
EC=6.2.1.-
Alternative name(s):
Solute carrier family 27 member 1
Gene names
Name:SLC27A1
Synonyms:ACSVL5, FATP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Self-associates. May function as a homodimer By similarity.

Subcellular location

Cell membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein. Cytoplasm By similarity. Note: Plasma membrane and intracellular membranes, at least in adipocytes. Predominantly cytoplasmic in myocytes By similarity. Ref.5

Tissue specificity

Highest levels of expression are detected in muscle and adipose tissue small, intermediate levels in small intestine, and barely detectable in liver. Ref.4

Miscellaneous

FATP1-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.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Lipid transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from electronic annotation. Source: Ensembl

cardiolipin biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid transport

Traceable author statement. Source: Reactome

medium-chain fatty acid transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of phospholipid biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidic acid biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidylcholine biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidylethanolamine biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidylglycerol biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidylinositol biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

phosphatidylserine biosynthetic process

Inferred from mutant phenotype PubMed 19523918. Source: UniProtKB

positive regulation of heat generation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionfatty acid transporter activity

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

very long-chain fatty acid-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 646646Long-chain fatty acid transport protein 1
PRO_0000193201

Regions

Topological domain1 – 1313Extracellular Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 646612Cytoplasmic Potential
Nucleotide binding246 – 25712AMP By similarity
Region191 – 475285Sufficient for oligomerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6PCB7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0E1FBA81922567E0

FASTA64671,108
        10         20         30         40         50         60 
MRAPGAGAAS VVSLALLWLL GLPWTWSAAA ALGVYVGSGG WRFLRIVCKT ARRDLFGLSV 

        70         80         90        100        110        120 
LIRVRLELRR HQRAGHTIPR IFQAVVQRQP ERLALVDAGT GECWTFAQLD AYSNAVANLF 

       130        140        150        160        170        180 
RQLGFAPGDV VAIFLEGRPE FVGLWLGLAK AGMEAALLNV NLRREPLAFC LGTSGAKALI 

       190        200        210        220        230        240 
FGGEMVAAVA EVSGHLGKSL IKFCSGDLGP EGILPDTHLL DPLLKEASTA PLAQIPSKGM 

       250        260        270        280        290        300 
DDRLFYIYTS GTTGLPKAAI VVHSRYYRMA AFGHHAYRMQ AADVLYDCLP LYHSAGNIIG 

       310        320        330        340        350        360 
VGQCLIYGLT VVLRKKFSAS RFWDDCIKYN CTVVQYIGEI CRYLLKQPVR EAERRHRVRL 

       370        380        390        400        410        420 
AVGNGLRPAI WEEFTERFGV RQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILPHVYPIR 

       430        440        450        460        470        480 
LVKVNEDTME LLRDAQGLCI PCQAGEPGLL VGQINQQDPL RRFDGYVSES ATSKKIAHSV 

       490        500        510        520        530        540 
FSKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEGVLSR LLGQTDVAVY 

       550        560        570        580        590        600 
GVAVPGVEGK AGMAAVADPH SLLDPNAIYQ ELQKVLAPYA RPIFLRLLPQ VDTTGTFKIQ 

       610        620        630        640 
KTRLQREGFD PRQTSDRLFF LDLKQGHYLP LNEAVYTRIC SGAFAL 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"The human fatty acid transport protein-1 (SLC27A1; FATP-1) cDNA and gene: organization, chromosomal localization, and expression."
Martin G., Nemoto M., Gelman L., Geffroy S., Najib J., Fruchart J.-C., Roevens P., de Martinville B., Deeb S., Auwerx J.
Genomics 66:296-304(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells."
Hatch G.M., Smith A.J., Xu F.Y., Hall A.M., Bernlohr D.A.
J. Lipid Res. 43:1380-1389(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC010618 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84611.1.
BC059399 mRNA. Translation: AAH59399.1.
CCDSCCDS32953.1.
RefSeqNP_940982.1. NM_198580.1.
UniGeneHs.363138.

3D structure databases

ProteinModelPortalQ6PCB7.
SMRQ6PCB7. Positions 67-605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid132009. 2 interactions.
STRING9606.ENSP00000252595.

Chemistry

ChEMBLCHEMBL2052038.

Protein family/group databases

TCDB4.C.1.1.9. the proposed fatty acid transporter (fat) family.

PTM databases

PhosphoSiteQ6PCB7.

Polymorphism databases

DMDM74749156.

Proteomic databases

MaxQBQ6PCB7.
PaxDbQ6PCB7.
PRIDEQ6PCB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252595; ENSP00000252595; ENSG00000130304.
ENST00000442725; ENSP00000413424; ENSG00000130304.
GeneID376497.
KEGGhsa:376497.
UCSCuc002ngu.1. human.

Organism-specific databases

CTD376497.
GeneCardsGC19P017579.
HGNCHGNC:10995. SLC27A1.
HPAHPA008255.
MIM600691. gene.
neXtProtNX_Q6PCB7.
PharmGKBPA35869.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidQ6PCB7.
KOK08745.
OMAIWEEFTE.
OrthoDBEOG7W6WKB.
PhylomeDBQ6PCB7.
TreeFamTF313430.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ6PCB7.
BgeeQ6PCB7.
CleanExHS_SLC27A1.
GenevestigatorQ6PCB7.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC27A1. human.
GeneWikiSLC27A1.
GenomeRNAi376497.
NextBio100645.
PROQ6PCB7.
SOURCESearch...

Entry information

Entry nameS27A1_HUMAN
AccessionPrimary (citable) accession number: Q6PCB7
Secondary accession number(s): A6NIH2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM