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Protein

Fatty acid-binding protein, epidermal

Gene

Fabp5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

High specificity for fatty acids. Highest affinity for C18 chain length (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei109Fatty acidBy similarity1

GO - Molecular functioni

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

GO - Biological processi

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-5362517. Signaling by Retinoic Acid.
R-RNO-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, epidermal
Alternative name(s):
Cutaneous fatty acid-binding protein
Short name:
C-FABP
DA11
Epidermal-type fatty acid-binding protein
Short name:
E-FABP
Fatty acid-binding protein 5
Gene namesi
Name:Fabp5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi70997. Fabp5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000673792 – 135Fatty acid-binding protein, epidermalAdd BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphoserineCombined sources1
Disulfide bondi120 ↔ 1271 Publication
Modified residuei131PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP55053.
PRIDEiP55053.

PTM databases

iPTMnetiP55053.
PhosphoSitePlusiP55053.

Expressioni

Gene expression databases

BgeeiENSRNOG00000049075.
GenevisibleiP55053. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064809.

Structurei

3D structure databases

ProteinModelPortaliP55053.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 131Fatty acid bindingBy similarity3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOVERGENiHBG005633.
InParanoidiP55053.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG091G0QSV.
PhylomeDBiP55053.

Family and domain databases

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

P55053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLKDLEGK WRLVESHGFE DYMKELGVGL ALRKMGAMAK PDCIITLDGN
60 70 80 90 100
NLTVKTESTV KTTVFSCTLG EKFDETTADG RKTETVCTFT DGALVQHQKW
110 120 130
EGKESTITRK LKDGKMVVEC VMNNAICTRV YEKVQ
Length:135
Mass (Da):15,059
Last modified:January 23, 2007 - v3
Checksum:i978392433DF54358
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49G → N in AAA86680 (PubMed:7607553).Curated1
Sequence conflicti112K → N in AAB46848 (PubMed:8723767).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13253 mRNA. Translation: AAA86680.1.
S69874 mRNA. Translation: AAB30574.1.
S83247 mRNA. Translation: AAB46848.1.
PIRiJC2201.
RefSeqiNP_665885.1. NM_145878.1.
UniGeneiRn.98269.

Genome annotation databases

EnsembliENSRNOT00000075493; ENSRNOP00000064809; ENSRNOG00000049075.
GeneIDi140868.
KEGGirno:140868.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13253 mRNA. Translation: AAA86680.1.
S69874 mRNA. Translation: AAB30574.1.
S83247 mRNA. Translation: AAB46848.1.
PIRiJC2201.
RefSeqiNP_665885.1. NM_145878.1.
UniGeneiRn.98269.

3D structure databases

ProteinModelPortaliP55053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064809.

PTM databases

iPTMnetiP55053.
PhosphoSitePlusiP55053.

Proteomic databases

PaxDbiP55053.
PRIDEiP55053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000075493; ENSRNOP00000064809; ENSRNOG00000049075.
GeneIDi140868.
KEGGirno:140868.

Organism-specific databases

CTDi2171.
RGDi70997. Fabp5.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOVERGENiHBG005633.
InParanoidiP55053.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG091G0QSV.
PhylomeDBiP55053.

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-RNO-5362517. Signaling by Retinoic Acid.
R-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP55053.

Gene expression databases

BgeeiENSRNOG00000049075.
GenevisibleiP55053. RN.

Family and domain databases

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

Entry informationi

Entry nameiFABP5_RAT
AccessioniPrimary (citable) accession number: P55053
Secondary accession number(s): P97757
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 115 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, Direct protein sequencing, 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.