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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311Fatty acid 11 Publication
Binding sitei39 – 391Fatty acid 21 Publication
Binding sitei122 – 1221Fatty acid 21 Publication

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

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

ChEMBLiCHEMBL5738.
GuidetoPHARMACOLOGYi2531.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Fatty acid-binding protein, liverPRO_0000067337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei31 – 311N6-succinyllysineBy similarity
Modified residuei36 – 361N6-succinyllysineBy similarity
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei46 – 461N6-succinyllysineBy similarity
Modified residuei51 – 511PhosphothreonineBy similarity
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei78 – 781N6-succinyllysineBy similarity
Modified residuei84 – 841N6-acetyllysine; alternateBy similarity
Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Cross-linki105 ↔ 106Isoaspartyl glycine isopeptide (Asn-Gly); alternate
Modified residuei105 – 1051Deamidated asparagine; alternate1 Publication
Modified residuei121 – 1211N6-succinyllysineBy similarity

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.
PhosphoSiteiP02692.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006675.
GenevisibleiP02692. RN.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP02692.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi15 – 217Combined sources
Helixi26 – 327Combined sources
Beta strandi38 – 447Combined sources
Beta strandi47 – 548Combined sources
Beta strandi57 – 648Combined sources
Beta strandi67 – 726Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Beta strandi84 – 863Combined sources
Turni87 – 893Combined sources
Beta strandi90 – 956Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi118 – 12710Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP02692.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 563Fatty acid 1 binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1LFOX-ray2.30A1-127[»]
2JU3NMR-A1-127[»]
2JU7NMR-A1-127[»]
2JU8NMR-A1-127[»]
ProteinModelPortaliP02692.
SMRiP02692. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP02692.
ChEMBLiCHEMBL5738.
GuidetoPHARMACOLOGYi2531.
SwissLipidsiSLP:000001517.

PTM databases

iPTMnetiP02692.
PhosphoSiteiP02692.

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: September 7, 2016
This is version 160 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.