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, intestinal

Gene

Fabp2

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

Functioni

FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei83Fatty acid1
Binding sitei107Fatty acid1

GO - Molecular functioni

  • fatty acid binding Source: RGD
  • long-chain fatty acid transporter activity Source: RGD

GO - Biological processi

  • fatty acid metabolic process Source: RGD
  • fatty acid transport Source: RGD
  • intestinal absorption Source: RGD
  • long-chain fatty acid transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, intestinal
Alternative name(s):
Fatty acid-binding protein 2
Intestinal-type fatty acid-binding protein
Short name:
I-FABP
Gene namesi
Name:Fabp2
Synonyms:Fabpi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2591. Fabp2.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: RGD
  • cytoplasm Source: RGD
  • microvillus Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45G → V: Small reduction in stability, impaired ligand binding. 1 Publication1
Mutagenesisi55N → V: No reduction in stability. 1 Publication1
Mutagenesisi61V → N: Reduced thermodynamic stability. 1 Publication1
Mutagenesisi66G → V: Large reduction in stability. 1 Publication1
Mutagenesisi76G → V: Reduced stability. 1 Publication1
Mutagenesisi81G → V: Large reduction in stability. 1 Publication1
Mutagenesisi87G → V: No reduction in stability, impaired ligand binding. 1 Publication1
Mutagenesisi98D → V: Reduced stability. 1 Publication1
Mutagenesisi100G → V: Large reduction in stability. 1 Publication1
Mutagenesisi111G → V: Small reduction in stability, impaired ligand binding. 1 Publication1
Mutagenesisi122G → V: Large reduction in stability. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000673302 – 132Fatty acid-binding protein, intestinalAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP02693.

PTM databases

iPTMnetiP02693.
PhosphoSitePlusiP02693.

Expressioni

Tissue specificityi

Expressed in the small intestine. Expression in the mucosal cells of the ileum extends from the midvillar region to the villus tips.1 Publication

Inductioni

By peptide YY.1 Publication

Structurei

Secondary structure

1132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi15 – 22Combined sources8
Helixi26 – 32Combined sources7
Beta strandi38 – 44Combined sources7
Beta strandi47 – 53Combined sources7
Beta strandi55 – 57Combined sources3
Beta strandi58 – 64Combined sources7
Beta strandi69 – 72Combined sources4
Beta strandi73 – 76Combined sources4
Beta strandi78 – 86Combined sources9
Beta strandi89 – 96Combined sources8
Turni97 – 99Combined sources3
Beta strandi102 – 110Combined sources9
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
1A57NMR-A2-132[»]
1AELNMR-A2-132[»]
1DC9X-ray2.10A2-132[»]
1ICMX-ray1.50A2-132[»]
1ICNX-ray1.74A2-132[»]
1IFBX-ray1.96A2-132[»]
1IFCX-ray1.19A1-132[»]
1SA8NMR-A2-9[»]
A37-132[»]
1T8VNMR-A2-132[»]
1URENMR-A2-132[»]
2IFBX-ray2.00A2-132[»]
3AKNX-ray1.60A2-132[»]
DisProtiDP00263.
ProteinModelPortaliP02693.
SMRiP02693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02693.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP02693.
KOiK08751.
PhylomeDBiP02693.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031272. FABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF89. PTHR11955:SF89. 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.

P02693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFDGTWKVD RNENYEKFME KMGINVVKRK LGAHDNLKLT ITQEGNKFTV
60 70 80 90 100
KESSNFRNID VVFELGVDFA YSLADGTELT GTWTMEGNKL VGKFKRVDNG
110 120 130
KELIAVREIS GNELIQTYTY EGVEAKRIFK KE
Length:132
Mass (Da):15,124
Last modified:January 23, 2007 - v4
Checksum:iA652B8494FE8A71E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10D → Y in AAA41138 (PubMed:6582489).Curated1
Sequence conflicti83W → L in AAA41138 (PubMed:6582489).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01180 mRNA. Translation: AAA41138.1.
M35992 mRNA. Translation: AAA41141.1.
M18080 Genomic DNA. Translation: AAA41133.1.
PIRiI65761. FZRTI.
RefSeqiNP_037200.1. NM_013068.1.
UniGeneiRn.91358.

Genome annotation databases

GeneIDi25598.
KEGGirno:25598.
UCSCiRGD:2591. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01180 mRNA. Translation: AAA41138.1.
M35992 mRNA. Translation: AAA41141.1.
M18080 Genomic DNA. Translation: AAA41133.1.
PIRiI65761. FZRTI.
RefSeqiNP_037200.1. NM_013068.1.
UniGeneiRn.91358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A57NMR-A2-132[»]
1AELNMR-A2-132[»]
1DC9X-ray2.10A2-132[»]
1ICMX-ray1.50A2-132[»]
1ICNX-ray1.74A2-132[»]
1IFBX-ray1.96A2-132[»]
1IFCX-ray1.19A1-132[»]
1SA8NMR-A2-9[»]
A37-132[»]
1T8VNMR-A2-132[»]
1URENMR-A2-132[»]
2IFBX-ray2.00A2-132[»]
3AKNX-ray1.60A2-132[»]
DisProtiDP00263.
ProteinModelPortaliP02693.
SMRiP02693.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP02693.
PhosphoSitePlusiP02693.

Proteomic databases

PRIDEiP02693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25598.
KEGGirno:25598.
UCSCiRGD:2591. rat.

Organism-specific databases

CTDi2169.
RGDi2591. Fabp2.

Phylogenomic databases

HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP02693.
KOiK08751.
PhylomeDBiP02693.
TreeFamiTF316894.

Miscellaneous databases

EvolutionaryTraceiP02693.
PROiP02693.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031272. FABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF89. PTHR11955:SF89. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABPI_RAT
AccessioniPrimary (citable) accession number: P02693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 152 of the entry and version 4 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. 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.