Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fatty acid-binding protein, adipocyte

Gene

Fabp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • fatty acid binding Source: RGD
  • transporter activity Source: InterPro

GO - Biological processi

  • fatty acid metabolic process Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • regulation of inflammatory response Source: InterPro
  • response to drug Source: RGD
  • response to glucocorticoid Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, adipocyte
Alternative name(s):
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
Gene namesi
Name:Fabp4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69309. 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 (By similarity).By similarity

GO - Cellular componenti

  • cytosol Source: RGD
  • lipid particle Source: Reactome
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2021755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 132131Fatty acid-binding protein, adipocytePRO_0000067369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteineBy similarity
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinasesBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP70623.
PRIDEiP70623.

PTM databases

iPTMnetiP70623.
PhosphoSiteiP70623.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with PPARG (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014701.

Chemistry

BindingDBiP70623.

Structurei

3D structure databases

ProteinModelPortaliP70623.
SMRiP70623. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Fatty acid bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi22 – 3211Nuclear localization signalBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOVERGENiHBG005633.
InParanoidiP70623.
PhylomeDBiP70623.

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.

P70623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN LIISVEGDLV
60 70 80 90 100
VIRSESTFKN TEISFKLGVE FDEITPDDRK VKSIITLDGG VLVHVQKWDG
110 120 130
KSTTIKKRRD GDKLVVECVM KGVTSTRVYE RA
Length:132
Mass (Da):14,708
Last modified:January 23, 2007 - v3
Checksum:i5277E995DD99223B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75581 mRNA. Translation: AAB18344.1.
UniGeneiRn.4258.

Genome annotation databases

UCSCiRGD:69309. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75581 mRNA. Translation: AAB18344.1.
UniGeneiRn.4258.

3D structure databases

ProteinModelPortaliP70623.
SMRiP70623. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014701.

Chemistry

BindingDBiP70623.
ChEMBLiCHEMBL2021755.

PTM databases

iPTMnetiP70623.
PhosphoSiteiP70623.

Proteomic databases

PaxDbiP70623.
PRIDEiP70623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:69309. rat.

Organism-specific databases

RGDi69309. Fabp4.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
HOVERGENiHBG005633.
InParanoidiP70623.
PhylomeDBiP70623.

Miscellaneous databases

PROiP70623.

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...

Publicationsi

« Hide 'large scale' publications
  1. Prinsen C., Veerkamp J.H.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFABP4_RAT
AccessioniPrimary (citable) accession number: P70623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 112 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

Complete proteome, Reference proteome

Documents

  1. 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.