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Protein

Fatty acid-binding protein, epidermal

Gene

Fabp5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

  • glucose metabolic process Source: MGI
  • glucose transport Source: MGI
  • lipid metabolic process Source: MGI
  • phosphatidylcholine biosynthetic process Source: MGI
  • response to wounding Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, epidermal
Alternative name(s):
Epidermal-type fatty acid-binding protein
Short name:
E-FABP
Fatty acid-binding protein 5
Keratinocyte lipid-binding protein
Psoriasis-associated fatty acid-binding protein homolog
Short name:
PA-FABP
Gene namesi
Name:Fabp5
Synonyms:Fabpe, Klbp, Mal1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:101790. 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_00000673782 – 135Fatty acid-binding protein, epidermalAdd BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphoserineBy similarity1
Disulfide bondi120 ↔ 127By similarity
Modified residuei131PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ05816.
PaxDbiQ05816.
PeptideAtlasiQ05816.
PRIDEiQ05816.

2D gel databases

REPRODUCTION-2DPAGEQ05816.
UCD-2DPAGEQ05816.

PTM databases

iPTMnetiQ05816.
PhosphoSitePlusiQ05816.

Expressioni

Tissue specificityi

Most abundant in keratinocytes and also in stratified epithelia of epidermis and tongue. Relatively high levels found in adipose and mammary tissues and small amounts found in heart, brain, liver, spleen, muscle and lung.

Gene expression databases

BgeeiENSMUSG00000027533.
CleanExiMM_FABP5.
ExpressionAtlasiQ05816. baseline and differential.
GenevisibleiQ05816. MM.

Interactioni

Protein-protein interaction databases

BioGridi200959. 1 interactor.
IntActiQ05816. 4 interactors.
MINTiMINT-1869678.
STRINGi10090.ENSMUSP00000029046.

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Beta strandi9 – 18Combined sources10
Helixi19 – 26Combined sources8
Helixi30 – 37Combined sources8
Beta strandi42 – 48Combined sources7
Beta strandi51 – 57Combined sources7
Beta strandi62 – 68Combined sources7
Beta strandi73 – 76Combined sources4
Beta strandi82 – 90Combined sources9
Beta strandi93 – 100Combined sources8
Beta strandi103 – 112Combined sources10
Beta strandi115 – 122Combined sources8
Beta strandi125 – 133Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AZNX-ray2.51A/B1-135[»]
4AZOX-ray2.33A1-135[»]
4AZPX-ray2.10A1-135[»]
4AZQX-ray2.00A1-135[»]
ProteinModelPortaliQ05816.
SMRiQ05816.
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.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiQ05816.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG091G0QSV.
PhylomeDBiQ05816.
TreeFamiTF316894.

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.

Q05816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLKDLEGK WRLMESHGFE EYMKELGVGL ALRKMAAMAK PDCIITCDGN
60 70 80 90 100
NITVKTESTV KTTVFSCNLG EKFDETTADG RKTETVCTFQ DGALVQHQQW
110 120 130
DGKESTITRK LKDGKMIVEC VMNNATCTRV YEKVQ
Length:135
Mass (Da):15,137
Last modified:January 23, 2007 - v3
Checksum:i6A6C8DBEBB046185
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70100 mRNA. Translation: CAA49703.1.
AJ223066 Genomic DNA. Translation: CAA11069.1.
AF061015, AF061014 Genomic DNA. Translation: AAC82368.1.
AK008782 mRNA. Translation: BAB25890.1.
AK011551 mRNA. Translation: BAB27692.1.
BC002008 mRNA. Translation: AAH02008.1.
CCDSiCCDS38388.1.
PIRiA47497.
RefSeqiNP_034764.1. NM_010634.3.
UniGeneiMm.741.

Genome annotation databases

EnsembliENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
GeneIDi16592.
KEGGimmu:16592.
UCSCiuc008opg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70100 mRNA. Translation: CAA49703.1.
AJ223066 Genomic DNA. Translation: CAA11069.1.
AF061015, AF061014 Genomic DNA. Translation: AAC82368.1.
AK008782 mRNA. Translation: BAB25890.1.
AK011551 mRNA. Translation: BAB27692.1.
BC002008 mRNA. Translation: AAH02008.1.
CCDSiCCDS38388.1.
PIRiA47497.
RefSeqiNP_034764.1. NM_010634.3.
UniGeneiMm.741.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AZNX-ray2.51A/B1-135[»]
4AZOX-ray2.33A1-135[»]
4AZPX-ray2.10A1-135[»]
4AZQX-ray2.00A1-135[»]
ProteinModelPortaliQ05816.
SMRiQ05816.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200959. 1 interactor.
IntActiQ05816. 4 interactors.
MINTiMINT-1869678.
STRINGi10090.ENSMUSP00000029046.

PTM databases

iPTMnetiQ05816.
PhosphoSitePlusiQ05816.

2D gel databases

REPRODUCTION-2DPAGEQ05816.
UCD-2DPAGEQ05816.

Proteomic databases

EPDiQ05816.
PaxDbiQ05816.
PeptideAtlasiQ05816.
PRIDEiQ05816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
GeneIDi16592.
KEGGimmu:16592.
UCSCiuc008opg.2. mouse.

Organism-specific databases

CTDi2171.
MGIiMGI:101790. Fabp5.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiQ05816.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG091G0QSV.
PhylomeDBiQ05816.
TreeFamiTF316894.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ05816.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027533.
CleanExiMM_FABP5.
ExpressionAtlasiQ05816. baseline and differential.
GenevisibleiQ05816. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q05816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 150 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

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.