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Q91VE0 (S27A4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 4

Short name=FATP-4
Short name=Fatty acid transport protein 4
EC=6.2.1.-
Alternative name(s):
Solute carrier family 27 member 4
Gene names
Name:Slc27a4
Synonyms:Acsvl4, Fatp4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.8 Ref.10 Ref.11 Ref.13

Subcellular location

Membrane; Multi-pass membrane protein Probable. Endoplasmic reticulum membrane Ref.11 Ref.13.

Tissue specificity

Most abundantly expressed in small intestine, brain, kidney, liver, skin and heart. In small intestine, expressed at high levels on the apical side of mature enterocytes. Highly expressed by the epithelial cells of the visceral endoderm and localized to the brush-border membrane of extraembryonic endodermal cells (at protein level). Expressed in the retinal pigment epithelium and in the retina (at protein level). Expressed in the retinal pigment epithelium and in the retina. Ref.1 Ref.5 Ref.6 Ref.7 Ref.13

Involvement in disease

Defects in Slc27a4 are the cause of wrinkle-free (wrfr) phenotype. It is a spontaneous, autosomal recessive mutation resulting in very tight, thick skin and is secondary characterized by severe breathing difficulties. Mice die shortly after birth. This phenotype is similar to human restrictive dermopathy, a very rare human genetic disorder. Ref.9

Miscellaneous

Slc27a4 deficient mice display features of a neonatally lethal restrictive dermopathy. Their skin is characterized by hyperproliferative hyperkeratosis with a disturbed epidermal barrier, a flat dermal-epidermal junction, a reduced number of pilo-sebaceous structures, and a compact dermis. The rigid skin consistency results in an altered body shape with facial dysmorphia, generalized joint flexion contractures and impaired movement including suckling and breathing deficiencies. Lipid analysis demonstrates a disturbed fatty acid composition of epidermal ceramides, in particular a decrease in the C26:0 and C26:0-OH fatty acid substitutes.

Deletion of Slc27a4 results in embryonic lethality, which has been attributed to a requirement for fat absorption early in embryonic development across the visceral endoderm.

Sequence similarities

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

Sequence caution

The sequence AAC40188.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAC40188.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Lipid transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid metabolic process

Inferred from mutant phenotype PubMed 18843142. Source: MGI

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid metabolic process

Inferred from direct assay Ref.1Ref.10. Source: MGI

long-chain fatty acid transport

Inferred from mutant phenotype Ref.6Ref.7. Source: MGI

medium-chain fatty acid transport

Inferred from direct assay PubMed 17062637. Source: MGI

response to nutrient

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from mutant phenotype Ref.8PubMed 16354193PubMed 17401141. Source: MGI

very long-chain fatty acid catabolic process

Inferred from direct assay PubMed 17522045. Source: MGI

very long-chain fatty acid metabolic process

Inferred from direct assay Ref.10PubMed 17522045. Source: MGI

   Cellular_componentbrush border membrane

Inferred from direct assay Ref.7. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 15496455PubMed 17062637. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microvillus

Inferred from direct assay Ref.6. Source: MGI

plasma membrane

Inferred from direct assay PubMed 15496455. Source: MGI

   Molecular_functionlong-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1Ref.10PubMed 17062637. Source: MGI

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

very long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.10PubMed 17522045PubMed 18258213. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643Long-chain fatty acid transport protein 4
PRO_0000193211

Regions

Transmembrane20 – 4223Helical; Potential
Transmembrane139 – 15618Helical; Potential
Nucleotide binding243 – 25412AMP Potential

Experimental info

Sequence conflict3301I → V in AAC40188. Ref.5
Sequence conflict5421P → S in BAE41756. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q91VE0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 10B3E9730FDF586A

FASTA64372,319
        10         20         30         40         50         60 
MLLGASLVGA LLFSKLVLKL PWTQVGFSLL LLYLGSGGWR FIRVFIKTVR RDIFGGMVLL 

        70         80         90        100        110        120 
KVKTKVRRYL QERKTVPLLF ASMVQRHPDK TALIFEGTDT HWTFRQLDEY SSSVANFLQA 

       130        140        150        160        170        180 
RGLASGNVVA LFMENRNEFV GLWLGMAKLG VEAALINTNL RRDALRHCLD TSKARALIFG 

       190        200        210        220        230        240 
SEMASAICEI HASLEPTLSL FCSGSWEPST VPVSTEHLDP LLEDAPKHLP SHPDKGFTDK 

       250        260        270        280        290        300 
LFYIYTSGTT GLPKAAIVVH SRYYRMASLV YYGFRMRPDD IVYDCLPLYH SAGNIVGIGQ 

       310        320        330        340        350        360 
CLLHGMTVVI RKKFSASRFW DDCIKYNCTI VQYIGELCRY LLNQPPREAE SRHKVRMALG 

       370        380        390        400        410        420 
NGLRQSIWTD FSSRFHIPQV AEFYGATECN CSLGNFDSRV GACGFNSRIL SFVYPIRLVR 

       430        440        450        460        470        480 
VNEDTMELIR GPDGVCIPCQ PGQPGQLVGR IIQQDPLRRF DGYLNQGANN KKIANDVFKK 

       490        500        510        520        530        540 
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLH MADVAVYGVE 

       550        560        570        580        590        600 
VPGTEGRAGM AAVASPISNC DLESFAQTLK KELPLYARPI FLRFLPELHK TGTFKFQKTE 

       610        620        630        640 
LRKEGFDPSV VKDPLFYLDA RKGCYVALDQ EAYTRIQAGE EKL 

« Hide

References

« Hide 'large scale' references
[1]"Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase."
Herrmann T., Buchkremer F., Gosch I., Hall A.M., Bernlohr D.A., Stremmel W.
Gene 270:31-40(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell and Vagina.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Strain: FVB/N.
Tissue: Liver.
[5]"A family of fatty acid transporters conserved from mycobacterium to man."
Hirsch D., Stahl A., Lodish H.F.
Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-643, TISSUE SPECIFICITY.
[6]"Identification of the major intestinal fatty acid transport protein."
Stahl A., Hirsch D.J., Gimeno R.E., Punreddy S., Ge P., Watson N., Patel S., Kotler M., Raimondi A., Tartaglia L.A., Lodish H.F.
Mol. Cell 4:299-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FATTY ACID TRANSPORT, TISSUE SPECIFICITY.
[7]"Targeted deletion of fatty acid transport protein-4 results in early embryonic lethality."
Gimeno R.E., Hirsch D.J., Punreddy S., Sun Y., Ortegon A.M., Wu H., Daniels T., Stricker-Krongrad A., Lodish H.F., Stahl A.
J. Biol. Chem. 278:49512-49516(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Mice with targeted disruption of the fatty acid transport protein 4 (Fatp 4, Slc27a4) gene show features of lethal restrictive dermopathy."
Herrmann T., van der Hoeven F., Grone H.J., Stewart A.F., Langbein L., Kaiser I., Liebisch G., Gosch I., Buchkremer F., Drobnik W., Schmitz G., Stremmel W.
J. Cell Biol. 161:1105-1115(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development."
Moulson C.L., Martin D.R., Lugus J.J., Schaffer J.E., Lind A.C., Miner J.H.
Proc. Natl. Acad. Sci. U.S.A. 100:5274-5279(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[10]"Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice."
Hall A.M., Wiczer B.M., Herrmann T., Stremmel W., Bernlohr D.A.
J. Biol. Chem. 280:11948-11954(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ACYL-COA LIGASE.
[11]"Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast."
DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.
J. Biol. Chem. 280:16829-16837(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[13]"Fatty acid transport protein 4 (FATP4) prevents light-induced degeneration of cone and rod photoreceptors by inhibiting RPE65 isomerase."
Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G., Miner J.H., Jin M.
J. Neurosci. 33:3178-3189(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251113 mRNA. Translation: CAC42082.1.
AJ276492 Genomic DNA. Translation: CAC42083.1.
AK036919 mRNA. Translation: BAC29639.1.
AK155388 mRNA. Translation: BAE33236.1.
AK170377 mRNA. Translation: BAE41756.1.
CT010312 mRNA. Translation: CAJ18520.1.
BC023114 mRNA. Translation: AAH23114.1.
AF072759 mRNA. Translation: AAC40188.1. Sequence problems.
RefSeqNP_036119.1. NM_011989.4.
UniGeneMm.330113.

3D structure databases

ProteinModelPortalQ91VE0.
SMRQ91VE0. Positions 74-607.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB4.C.1.1.1. the proposed fatty acid transporter (fat) family.

PTM databases

PhosphoSiteQ91VE0.

Proteomic databases

PaxDbQ91VE0.
PRIDEQ91VE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080065; ENSMUSP00000078971; ENSMUSG00000059316.
GeneID26569.
KEGGmmu:26569.
UCSCuc008jaf.1. mouse.

Organism-specific databases

CTD10999.
MGIMGI:1347347. Slc27a4.

Phylogenomic databases

eggNOGCOG0318.
GeneTreeENSGT00550000074420.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidQ91VE0.
KOK08745.
OMAVMYDCLP.
OrthoDBEOG7W6WKB.
PhylomeDBQ91VE0.
TreeFamTF313430.

Enzyme and pathway databases

BRENDA6.2.1.3. 3474.

Gene expression databases

BgeeQ91VE0.
GenevestigatorQ91VE0.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR022272. Lipocalin_CS.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304651.
PROQ91VE0.
SOURCESearch...

Entry information

Entry nameS27A4_MOUSE
AccessionPrimary (citable) accession number: Q91VE0
Secondary accession number(s): O88562, Q3TD48
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot