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Protein

Fatty acid-binding protein, adipocyte

Gene

Fabp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.3 Publications

GO - Molecular functioni

GO - Biological processi

  • brown fat cell differentiation Source: MGI
  • cellular response to lithium ion Source: MGI
  • cellular response to tumor necrosis factor Source: MGI
  • cholesterol homeostasis Source: MGI
  • cytokine production Source: MGI
  • negative regulation of protein kinase activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of inflammatory response Source: MGI
  • white fat cell differentiation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
3T3-L1 lipid-binding protein
Adipocyte lipid-binding protein
Short name:
ALBP
Adipocyte-type fatty acid-binding protein
Short name:
A-FABP
Short name:
AFABP
Fatty acid-binding protein 4
Myelin P2 protein homolog
P15
P2 adipocyte protein
Protein 422
Gene namesi
Name:Fabp4
Synonyms:Ap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88038. Fabp4.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-31 and A-32. 1 Publication1
Mutagenesisi31R → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-32. 1 Publication1
Mutagenesisi32K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-31. 1 Publication1
Mutagenesisi58F → A: Abolishes ligand-induced translocation to the nucleus. 1 Publication1
Mutagenesisi67L → A: Abolishes export from nucleus; when associated with A-87 and A-92. 2 Publications1
Mutagenesisi87L → A: Abolishes export from nucleus; when associated with A-67 and A-92. 2 Publications1
Mutagenesisi92L → A: Abolishes export from nucleus; when associated with A-67 and A-87. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL1075118.
GuidetoPHARMACOLOGYi2534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00000673672 – 132Fatty acid-binding protein, adipocyteAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei20Phosphotyrosine; by Tyr-kinasesBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP04117.
PeptideAtlasiP04117.
PRIDEiP04117.

2D gel databases

SWISS-2DPAGEP04117.

PTM databases

iPTMnetiP04117.
PhosphoSitePlusiP04117.

Expressioni

Gene expression databases

BgeeiENSMUSG00000062515.
CleanExiMM_FABP4.
ExpressionAtlasiP04117. baseline and differential.
GenevisibleiP04117. MM.

Interactioni

Subunit structurei

Monomer (By similarity). Homodimer. Interacts with PPARG.By similarity6 Publications

Protein-protein interaction databases

IntActiP04117. 1 interactor.
MINTiMINT-4094909.
STRINGi10090.ENSMUSP00000029041.

Structurei

Secondary structure

1132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi7 – 16Combined sources10
Helixi17 – 24Combined sources8
Helixi28 – 37Combined sources10
Beta strandi41 – 46Combined sources6
Beta strandi49 – 54Combined sources6
Beta strandi61 – 65Combined sources5
Beta strandi67 – 69Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi80 – 88Combined sources9
Beta strandi91 – 98Combined sources8
Beta strandi101 – 110Combined sources10
Beta strandi113 – 120Combined sources8
Beta strandi123 – 131Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A18X-ray2.40A2-132[»]
1A2DX-ray2.40A/B2-132[»]
1AB0X-ray1.90A3-132[»]
1ACDX-ray2.70A3-132[»]
1ADLX-ray1.60A2-132[»]
1ALBX-ray2.50A2-132[»]
1G74X-ray1.70A2-132[»]
1G7NX-ray1.50A2-132[»]
1LIBX-ray1.70A2-132[»]
1LICX-ray1.60A2-132[»]
1LIDX-ray1.60A2-132[»]
1LIEX-ray1.60A2-132[»]
1LIFX-ray1.60A2-132[»]
2ANSX-ray2.50A/B2-132[»]
2Q9SX-ray2.30A1-132[»]
2QM9X-ray2.31A/B1-132[»]
3HK1X-ray1.70A2-132[»]
3JS1X-ray1.81A/B2-132[»]
3JSQX-ray2.30A2-132[»]
5C0NX-ray3.00A/B1-132[»]
5D8JX-ray3.00A1-132[»]
ProteinModelPortaliP04117.
SMRiP04117.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04117.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 129Fatty acid binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 32Nuclear localization signalAdd BLAST11

Domaini

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP04117.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG091G0QSV.
PhylomeDBiP04117.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04117-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDLV
60 70 80 90 100
TIRSESTFKN TEISFKLGVE FDEITADDRK VKSIITLDGG ALVQVQKWDG
110 120 130
KSTTIKRKRD GDKLVVECVM KGVTSTRVYE RA
Length:132
Mass (Da):14,650
Last modified:January 23, 2007 - v3
Checksum:iED08EDDBBE2D7E32
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40N → T in AAA39870 (PubMed:6206497).Curated1
Sequence conflicti111G → V in AAA39417 (PubMed:3520554).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02109 mRNA. Translation: AAA39416.1.
M13264
, M13261, M13262, M13263 Genomic DNA. Translation: AAA39870.1.
M13385 Genomic DNA. Translation: AAA39417.1.
AK003143 mRNA. Translation: BAB22601.1.
BC054426 mRNA. Translation: AAH54426.1.
M20497 Genomic DNA. Translation: AAA37188.1.
M28726 mRNA. Translation: AAA37112.1.
CCDSiCCDS17238.1.
PIRiB25952.
RefSeqiNP_077717.1. NM_024406.2.
UniGeneiMm.582.

Genome annotation databases

EnsembliENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
GeneIDi11770.
KEGGimmu:11770.
UCSCiuc008opl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02109 mRNA. Translation: AAA39416.1.
M13264
, M13261, M13262, M13263 Genomic DNA. Translation: AAA39870.1.
M13385 Genomic DNA. Translation: AAA39417.1.
AK003143 mRNA. Translation: BAB22601.1.
BC054426 mRNA. Translation: AAH54426.1.
M20497 Genomic DNA. Translation: AAA37188.1.
M28726 mRNA. Translation: AAA37112.1.
CCDSiCCDS17238.1.
PIRiB25952.
RefSeqiNP_077717.1. NM_024406.2.
UniGeneiMm.582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A18X-ray2.40A2-132[»]
1A2DX-ray2.40A/B2-132[»]
1AB0X-ray1.90A3-132[»]
1ACDX-ray2.70A3-132[»]
1ADLX-ray1.60A2-132[»]
1ALBX-ray2.50A2-132[»]
1G74X-ray1.70A2-132[»]
1G7NX-ray1.50A2-132[»]
1LIBX-ray1.70A2-132[»]
1LICX-ray1.60A2-132[»]
1LIDX-ray1.60A2-132[»]
1LIEX-ray1.60A2-132[»]
1LIFX-ray1.60A2-132[»]
2ANSX-ray2.50A/B2-132[»]
2Q9SX-ray2.30A1-132[»]
2QM9X-ray2.31A/B1-132[»]
3HK1X-ray1.70A2-132[»]
3JS1X-ray1.81A/B2-132[»]
3JSQX-ray2.30A2-132[»]
5C0NX-ray3.00A/B1-132[»]
5D8JX-ray3.00A1-132[»]
ProteinModelPortaliP04117.
SMRiP04117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04117. 1 interactor.
MINTiMINT-4094909.
STRINGi10090.ENSMUSP00000029041.

Chemistry databases

ChEMBLiCHEMBL1075118.
GuidetoPHARMACOLOGYi2534.

PTM databases

iPTMnetiP04117.
PhosphoSitePlusiP04117.

2D gel databases

SWISS-2DPAGEP04117.

Proteomic databases

PaxDbiP04117.
PeptideAtlasiP04117.
PRIDEiP04117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
GeneIDi11770.
KEGGimmu:11770.
UCSCiuc008opl.2. mouse.

Organism-specific databases

CTDi2167.
MGIiMGI:88038. Fabp4.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP04117.
KOiK08753.
OMAiGQEFDEI.
OrthoDBiEOG091G0QSV.
PhylomeDBiP04117.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

EvolutionaryTraceiP04117.
PROiP04117.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000062515.
CleanExiMM_FABP4.
ExpressionAtlasiP04117. baseline and differential.
GenevisibleiP04117. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR033073. FABP4.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF83. PTHR11955:SF83. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABP4_MOUSE
AccessioniPrimary (citable) accession number: P04117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.