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Q05816 (FABP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Fabp5
Synonyms:Fabpe, Klbp, Mal1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm.

Tissue specificity

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.

Domain

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

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 135134Fatty acid-binding protein, epidermal
PRO_0000067378

Regions

Region129 – 1313Fatty acid binding By similarity

Sites

Binding site1091Fatty acid By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1311Phosphotyrosine By similarity
Disulfide bond120 ↔ 127 By similarity

Secondary structure

.......................... 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05816 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6A6C8DBEBB046185

FASTA13515,137
        10         20         30         40         50         60 
MASLKDLEGK WRLMESHGFE EYMKELGVGL ALRKMAAMAK PDCIITCDGN NITVKTESTV 

        70         80         90        100        110        120 
KTTVFSCNLG EKFDETTADG RKTETVCTFQ DGALVQHQQW DGKESTITRK LKDGKMIVEC 

       130 
VMNNATCTRV YEKVQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA47497.
RefSeqNP_034764.1. NM_010634.3.
UniGeneMm.741.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AZNX-ray2.51A/B1-135[»]
4AZOX-ray2.33A1-135[»]
4AZPX-ray2.10A1-135[»]
4AZQX-ray2.00A1-135[»]
ProteinModelPortalQ05816.
SMRQ05816. Positions 2-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200959. 1 interaction.
IntActQ05816. 4 interactions.
MINTMINT-1869678.

PTM databases

PhosphoSiteQ05816.

2D gel databases

REPRODUCTION-2DPAGEQ05816.
UCD-2DPAGEQ05816.

Proteomic databases

PaxDbQ05816.
PRIDEQ05816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
GeneID16592.
KEGGmmu:16592.
UCSCuc008opg.1. mouse.

Organism-specific databases

CTD2171.
MGIMGI:101790. Fabp5.

Phylogenomic databases

eggNOGNOG309791.
HOGENOMHOG000004829.
HOVERGENHBG005633.
InParanoidQ05816.
KOK08754.
OMATCHRVYE.
OrthoDBEOG7NW6BZ.
PhylomeDBQ05816.
TreeFamTF316894.

Gene expression databases

BgeeQ05816.
CleanExMM_FABP5.
GenevestigatorQ05816.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio290145.
PROQ05816.
SOURCESearch...

Entry information

Entry nameFABP5_MOUSE
AccessionPrimary (citable) accession number: Q05816
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot