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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Fatty acidBy similarity

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

ReactomeiREACT_306383. Signaling by Retinoic Acid.
REACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

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
ProteomesiUP000000589 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 135134Fatty acid-binding protein, epidermalPRO_0000067378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Disulfide bondi120 ↔ 127By similarity
Modified residuei131 – 1311PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ05816.
PaxDbiQ05816.
PRIDEiQ05816.

2D gel databases

REPRODUCTION-2DPAGEQ05816.
UCD-2DPAGEQ05816.

PTM databases

PhosphoSiteiQ05816.

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

BgeeiQ05816.
CleanExiMM_FABP5.
ExpressionAtlasiQ05816. baseline and differential.
GenevisibleiQ05816. MM.

Interactioni

Protein-protein interaction databases

BioGridi200959. 1 interaction.
IntActiQ05816. 4 interactions.
MINTiMINT-1869678.
STRINGi10090.ENSMUSP00000029046.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi9 – 1810Combined sources
Helixi19 – 268Combined sources
Helixi30 – 378Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 577Combined sources
Beta strandi62 – 687Combined sources
Beta strandi73 – 764Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AZNX-ray2.51A/B1-135[»]
4AZOX-ray2.33A1-135[»]
4AZPX-ray2.10A1-135[»]
4AZQX-ray2.00A1-135[»]
ProteinModelPortaliQ05816.
SMRiQ05816. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1313Fatty acid bindingBy similarity

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG309791.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiQ05816.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG7NW6BZ.
PhylomeDBiQ05816.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
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.1. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
4AZNX-ray2.51A/B1-135[»]
4AZOX-ray2.33A1-135[»]
4AZPX-ray2.10A1-135[»]
4AZQX-ray2.00A1-135[»]
ProteinModelPortaliQ05816.
SMRiQ05816. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200959. 1 interaction.
IntActiQ05816. 4 interactions.
MINTiMINT-1869678.
STRINGi10090.ENSMUSP00000029046.

PTM databases

PhosphoSiteiQ05816.

2D gel databases

REPRODUCTION-2DPAGEQ05816.
UCD-2DPAGEQ05816.

Proteomic databases

MaxQBiQ05816.
PaxDbiQ05816.
PRIDEiQ05816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
GeneIDi16592.
KEGGimmu:16592.
UCSCiuc008opg.1. mouse.

Organism-specific databases

CTDi2171.
MGIiMGI:101790. Fabp5.

Phylogenomic databases

eggNOGiNOG309791.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiQ05816.
KOiK08754.
OMAiVECDMNG.
OrthoDBiEOG7NW6BZ.
PhylomeDBiQ05816.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_306383. Signaling by Retinoic Acid.
REACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

NextBioi290145.
PROiQ05816.
SOURCEiSearch...

Gene expression databases

BgeeiQ05816.
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.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tumor-specific overexpression of a novel keratinocyte lipid-binding protein. Identification and characterization of a cloned sequence activated during multistage carcinogenesis in mouse skin."
    Krieg P., Feil S., Fuerstenberger G., Bowden T.G.
    J. Biol. Chem. 268:17362-17369(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Keratinocyte.
  2. "Cloning and chromosomal localisation of the murine epidermal-type fatty acid binding protein gene (Fabpe)."
    Bleck B., Hohoff C., Binas B., Rustow B., Dixkens C., Hameister H., Boerchers T., Spener F.
    Gene 215:123-130(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. "Cloning and chromosomal location of the murine Keratinocyte lipid-binding protein gene."
    Hertzel A.V., Bernlohr D.A.
    Gene 221:235-243(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Stomach.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-24, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.

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: June 24, 2015
This is version 136 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

External Data

Dasty 3

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 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.