Q05816 (FABP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Fabp5
Synonyms:	Fabpe, Klbp, Mal1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Lipid-binding
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Inferred from mutant phenotype PubMed 12540600. Source: MGI glucose transport Inferred from mutant phenotype PubMed 12540600. Source: MGI phosphatidylcholine biosynthetic process Inferred from genetic interaction PubMed 15164767. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 135	134	Fatty acid-binding protein, epidermal		PRO_0000067378
Regions
	Region	129 – 131	3	Fatty acid binding By similarity
Sites
	Binding site	109	1	Fatty acid By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	131	1	Phosphotyrosine By similarity
	Disulfide bond	120 ↔ 127		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05816 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6A6C8DBEBB046185	FASTA	135	15,137
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.
IPI	IPI00114162.
PIR	A47497.
RefSeq	NP_034764.1. NM_010634.3.
UniGene	Mm.741.
3D structure databases
ProteinModelPortal	Q05816.
SMR	Q05816. Positions 3-135.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05816. 2 interactions.
PTM databases
PhosphoSite	Q05816.
2D gel databases
REPRODUCTION-2DPAGE	Q05816.
UCD-2DPAGE	Q05816.
Proteomic databases
PaxDb	Q05816.
PRIDE	Q05816.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
GeneID	16592.
KEGG	mmu:16592.
Organism-specific databases
CTD	2171.
MGI	MGI:101790. Fabp5.
Phylogenomic databases
eggNOG	NOG309791.
HOGENOM	HOG000004829.
HOVERGEN	HBG005633.
InParanoid	Q05816.
KO	K08754.
OMA	KMGSMAK.
OrthoDB	EOG4V1724.
Gene expression databases
ArrayExpress	Q05816.
Bgee	Q05816.
CleanEx	MM_FABP5.
Genevestigator	Q05816.
Family and domain databases
Gene3D	2.40.128.20. 1 hit.
InterPro	IPR012674. Calycin. IPR011038. Calycin-like. IPR000463. Fatty_acid-bd. IPR000566. Lipocln_cytosolic_FA-bd_dom. [Graphical view]
Pfam	PF00061. Lipocalin. 1 hit. [Graphical view]
PRINTS	PR00178. FATTYACIDBP.
SUPFAM	SSF50814. Calycin. 1 hit.
PROSITE	PS00214. FABP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	290145.
SOURCE	Search...

Entry information

Entry name

FABP5_MOUSE

Accession

Primary (citable) accession number: Q05816

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program