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, liver

Gene

Fabp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (By similarity). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei31Fatty acid 11 Publication1
Binding sitei39Fatty acid 21 Publication1
Binding sitei122Fatty acid 21 Publication1

GO - Molecular functioni

  • antioxidant activity Source: Ensembl
  • bile acid binding Source: RGD
  • chromatin binding Source: Ensembl
  • drug binding Source: RGD
  • fatty acid binding Source: RGD
  • long-chain fatty acid transporter activity Source: RGD
  • lysophospholipid transporter activity Source: RGD
  • phospholipid binding Source: RGD

GO - Biological processi

  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to hypoxia Source: Ensembl
  • intestinal absorption Source: RGD
  • long-chain fatty acid transport Source: RGD
  • mitophagy in response to mitochondrial depolarization Source: Ensembl
  • mitotic nuclear division Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of defense response to virus by host Source: Ensembl
  • positive regulation of fatty acid beta-oxidation Source: RGD
  • positive regulation of hydrolase activity Source: RGD
  • transport Source: RGD
  • xenophagy Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-RNO-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Chemistry databases

SwissLipidsiSLP:000001517.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, liver
Alternative name(s):
Fatty acid-binding protein 1
Liver-type fatty acid-binding protein
Short name:
L-FABP
Squalene- and sterol-carrier protein
Short name:
SCP
Z-protein
p14
Gene namesi
Name:Fabp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2590. Fabp1.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • peroxisomal matrix Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5738.
GuidetoPHARMACOLOGYi2531.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000673371 – 127Fatty acid-binding protein, liverAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine2 Publications1
Modified residuei11PhosphoserineCombined sources1
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei36N6-succinyllysineBy similarity1
Modified residuei39PhosphoserineCombined sources1
Modified residuei46N6-succinyllysineBy similarity1
Modified residuei51PhosphothreonineBy similarity1
Modified residuei56PhosphoserineCombined sources1
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei78N6-succinyllysineBy similarity1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei90N6-succinyllysineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Cross-linki105 ↔ 106Isoaspartyl glycine isopeptide (Asn-Gly); alternate
Modified residuei105Deamidated asparagine; alternate1 Publication1
Modified residuei121N6-succinyllysineBy similarity1

Post-translational modificationi

Deamidation and transpeptidation at the beta carboxyl of Asn-105 forms an isoaspartyl residue found in an isoform of the DE-III fraction. This rearrangement gives rise to an extra negative charge carried by the acid form.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

PaxDbiP02692.
PRIDEiP02692.

PTM databases

iPTMnetiP02692.
PhosphoSitePlusiP02692.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006675.
GenevisibleiP02692. RN.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Hnf4aP224493EBI-1209448,EBI-5261592

Protein-protein interaction databases

IntActiP02692. 2 interactors.
MINTiMINT-4567871.
STRINGi10116.ENSRNOP00000008841.

Chemistry databases

BindingDBiP02692.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi15 – 21Combined sources7
Helixi26 – 32Combined sources7
Beta strandi38 – 44Combined sources7
Beta strandi47 – 54Combined sources8
Beta strandi57 – 64Combined sources8
Beta strandi67 – 72Combined sources6
Beta strandi74 – 76Combined sources3
Beta strandi78 – 82Combined sources5
Beta strandi84 – 86Combined sources3
Turni87 – 89Combined sources3
Beta strandi90 – 95Combined sources6
Beta strandi98 – 105Combined sources8
Beta strandi108 – 115Combined sources8
Beta strandi118 – 127Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LFOX-ray2.30A1-127[»]
2JU3NMR-A1-127[»]
2JU7NMR-A1-127[»]
2JU8NMR-A1-127[»]
ProteinModelPortaliP02692.
SMRiP02692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02692.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 56Fatty acid 1 binding3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP02692.
KOiK08750.
OMAiFTLGEEC.
OrthoDBiEOG091G16BV.
PhylomeDBiP02692.
TreeFamiTF330348.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFSGKYQVQ SQENFEPFMK AMGLPEDLIQ KGKDIKGVSE IVHEGKKVKL
60 70 80 90 100
TITYGSKVIH NEFTLGEECE LETMTGEKVK AVVKMEGDNK MVTTFKGIKS
110 120
VTEFNGDTIT NTMTLGDIVY KRVSKRI
Length:127
Mass (Da):14,273
Last modified:August 13, 1987 - v1
Checksum:i08C7F59A99FE0D3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01235 mRNA. Translation: CAA24545.1.
M13501 Genomic DNA. Translation: AAA41140.1.
M35991 mRNA. Translation: AAA41135.1.
S55929 Other DNA. Translation: AAB19788.1.
BC086947 mRNA. Translation: AAH86947.1.
M17899 mRNA. Translation: AAA41134.1.
M10951 mRNA. Translation: AAA42119.1.
PIRiA92416. FZRTL.
I52354.
I52850.
I55238.
RefSeqiNP_036688.1. NM_012556.2.
UniGeneiRn.36412.

Genome annotation databases

EnsembliENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675.
GeneIDi24360.
KEGGirno:24360.
UCSCiRGD:2590. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01235 mRNA. Translation: CAA24545.1.
M13501 Genomic DNA. Translation: AAA41140.1.
M35991 mRNA. Translation: AAA41135.1.
S55929 Other DNA. Translation: AAB19788.1.
BC086947 mRNA. Translation: AAH86947.1.
M17899 mRNA. Translation: AAA41134.1.
M10951 mRNA. Translation: AAA42119.1.
PIRiA92416. FZRTL.
I52354.
I52850.
I55238.
RefSeqiNP_036688.1. NM_012556.2.
UniGeneiRn.36412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LFOX-ray2.30A1-127[»]
2JU3NMR-A1-127[»]
2JU7NMR-A1-127[»]
2JU8NMR-A1-127[»]
ProteinModelPortaliP02692.
SMRiP02692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02692. 2 interactors.
MINTiMINT-4567871.
STRINGi10116.ENSRNOP00000008841.

Chemistry databases

BindingDBiP02692.
ChEMBLiCHEMBL5738.
GuidetoPHARMACOLOGYi2531.
SwissLipidsiSLP:000001517.

PTM databases

iPTMnetiP02692.
PhosphoSitePlusiP02692.

Proteomic databases

PaxDbiP02692.
PRIDEiP02692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675.
GeneIDi24360.
KEGGirno:24360.
UCSCiRGD:2590. rat.

Organism-specific databases

CTDi2168.
RGDi2590. Fabp1.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00390000012034.
HOGENOMiHOG000004830.
HOVERGENiHBG005633.
InParanoidiP02692.
KOiK08750.
OMAiFTLGEEC.
OrthoDBiEOG091G16BV.
PhylomeDBiP02692.
TreeFamiTF330348.

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-RNO-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

EvolutionaryTraceiP02692.
PROiP02692.

Gene expression databases

BgeeiENSRNOG00000006675.
GenevisibleiP02692. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABPL_RAT
AccessioniPrimary (citable) accession number: P02692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are three fractions of Z-protein: DE-I, DE-II and DE-III. DE-I is virtually lipid free, DE-II binds palmitic, stearic, oleic, linoleic and arachidonic acids and DE-III binds mainly arachidonic acid.

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.