P04117 (FABP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid-binding protein, adipocyte

Alternative name(s):
3T3-L1 lipid-binding protein
Adipocyte lipid-binding protein
Short name=ALBP
Adipocyte-type fatty acid-binding protein
Short name=A-FABP
Short name=AFABP
Fatty acid-binding protein 4
Myelin P2 protein homolog
P15
P2 adipocyte protein
Protein 422

Gene names

Name:	Fabp4
Synonyms:	Ap2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	132 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	Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. Ref.10 Ref.11 Ref.12
Subunit structure	Monomer By similarity. Homodimer. Interacts with PPARG. Ref.10 Ref.11 Ref.19
Subcellular location	Cytoplasm. Nucleus. Note: Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. Ref.10 Ref.11 Ref.12 Ref.19
Domain	Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Nucleus
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	brown fat cell differentiation Inferred from direct assay. Source: MGI cellular response to lithium ion Inferred from direct assay. Source: MGI cholesterol homeostasis Inferred from mutant phenotype. Source: MGI cytokine production Inferred from mutant phenotype. Source: MGI negative regulation of protein kinase activity Inferred from mutant phenotype. Source: MGI negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: MGI positive regulation of inflammatory response Inferred from mutant phenotype. Source: MGI white fat cell differentiation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus 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 Ref.6

Chain

2 – 132

131

Fatty acid-binding protein, adipocyte

PRO_0000067367

Regions

Region

127 – 129

3

Fatty acid binding

Motif

22 – 32

11

Nuclear localization signal

Amino acid modifications

Modified residue

20

1

Phosphotyrosine; by Tyr-kinases By similarity

Experimental info

Mutagenesis

22

1

K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-31 and A-32. Ref.12

Mutagenesis

31

1

R → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-32. Ref.12

Mutagenesis

32

1

K → A: Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-31. Ref.12

Mutagenesis

58

1

F → A: Abolishes ligand-induced translocation to the nucleus. Ref.19

Mutagenesis

67

1

L → A: Abolishes export from nucleus; when associated with A-87 and A-92. Ref.12 Ref.19

Mutagenesis

87

1

L → A: Abolishes export from nucleus; when associated with A-67 and A-92. Ref.12 Ref.19

Mutagenesis

92

1

L → A: Abolishes export from nucleus; when associated with A-67 and A-87. Ref.12 Ref.19

Sequence conflict

40

1

N → T in AAA39870. Ref.1

Sequence conflict

111

1

G → V in AAA39417. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

132

Helix Strand Turn

Details...

Beta strand

7 – 16

10

Helix

17 – 24

8

Helix

28 – 35

8

Beta strand

40 – 46

7

Beta strand

49 – 55

7

Beta strand

61 – 65

5

Beta strand

71 – 74

4

Beta strand

80 – 88

9

Beta strand

91 – 98

8

Beta strand

101 – 110

10

Beta strand

113 – 120

8

Beta strand

123 – 131

9

Sequences

	Sequence		Length	Mass (Da)
	P04117 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: ED08EDDBBE2D7E32	FASTA	132	14,650
	10 20 30 40 50 60 MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDLV TIRSESTFKN 70 80 90 100 110 120 TEISFKLGVE FDEITADDRK VKSIITLDGG ALVQVQKWDG KSTTIKRKRD GDKLVVECVM 130 KGVTSTRVYE RA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of specific mRNAs during adipose differentiation: identification of an mRNA encoding a homologue of myelin P2 protein." Bernlohr D.A., Angus C.W., Lane M.D., Bolanowski M.A., Kelly T.J. Jr. Proc. Natl. Acad. Sci. U.S.A. 81:5468-5472(1984) [PubMed: 6206497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Adipocyte P2 gene: developmental expression and homology of 5'-flanking sequences among fat cell-specific genes." Hunt C.R., Ro J.H.-S., Dobson D.E., Min H.Y., Spiegelman B.M. Proc. Natl. Acad. Sci. U.S.A. 83:3786-3790(1986) [PubMed: 3520554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of three genes participating in the adipose differentiation of 3T3 cells." Phillips M., Djian P., Green H. J. Biol. Chem. 261:10821-10827(1986) [PubMed: 3015943] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland.
[6]	"Purification of murine adipocyte lipid-binding protein. Characterization as a fatty acid- and retinoic acid-binding protein." Matarese V., Bernlohr D.A. J. Biol. Chem. 263:14544-14551(1988) [PubMed: 2844775] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-132.
[7]	"Expression of the differentiation-induced gene for fatty acid-binding protein is activated by glucocorticoid and cAMP." Cook J.S., Lucas J.J., Sibley E., Bolanowski M.A., Christy R.J., Kelly T.J. Jr., Lane M.D. Proc. Natl. Acad. Sci. U.S.A. 85:2949-2953(1988) [PubMed: 2452440] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[8]	"Developmentally regulated mRNAs in 3T3-adipocytes: analysis of transcriptional control." Cook K.S., Hunt C.R., Spiegelman B.M. J. Cell Biol. 100:514-520(1985) [PubMed: 3968175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-132.
[9]	"Expression of fatty acid-binding proteins in the developing mouse mammary gland." Bansal M.P., Medina D. Biochem. Biophys. Res. Commun. 191:61-69(1993) [PubMed: 8447836] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-35; 37-51 AND 59-88. Tissue: Mammary gland.
[10]	"Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription." Tan N.-S., Shaw N.S., Vinckenbosch N., Liu P., Yasmin R., Desvergne B., Wahli W., Noy N. Mol. Cell. Biol. 22:5114-5127(2002) [PubMed: 12077340] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARG.
[11]	"Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor gamma agonists in cultured cell." Adida A., Spener F. Biochim. Biophys. Acta 1761:172-181(2006) [PubMed: 16574478] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARG.
[12]	"Continuous nucleocytoplasmic shuttling underlies transcriptional activation of PPARgamma by FABP4." Ayers S.D., Nedrow K.L., Gillilan R.E., Noy N. Biochemistry 46:6744-6752(2007) [PubMed: 17516629] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-22; ARG-31; LYS-32; LEU-67; LEU-87 AND LEU-92.
[13]	"Crystal structure of recombinant murine adipocyte lipid-binding protein." Xu Z., Bernlohr D.A., Banaszak L.J. Biochemistry 31:3484-3492(1992) [PubMed: 1554730] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[14]	"The adipocyte lipid-binding protein at 1.6-A resolution. Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids." Xu Z., Bernlohr D.A., Banaszak L.J. J. Biol. Chem. 268:7874-7884(1993) [PubMed: 8463311] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[15]	"Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate." Ory J.J., Banaszak L.J. Biophys. J. 77:1107-1116(1999) [PubMed: 10423455] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[16]	"X-ray crystallographic structures of adipocyte lipid-binding protein complexed with palmitate and hexadecanesulfonic acid. Properties of cavity binding sites." LaLonde J.M., Bernlohr D.A., Banaszak L.J. Biochemistry 33:4885-4895(1994) [PubMed: 8161548] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
[17]	"Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies." LaLonde J.M., Levenson M.A., Roe J.J., Bernlohr D.A., Banaszak L.J. J. Biol. Chem. 269:25339-25347(1994) [PubMed: 7929228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
[18]	"Specificity determinants for lipids bound to beta-barrel proteins." Reese A.J., Banaszak L.J. J. Lipid Res. 45:232-243(2004) [PubMed: 14594993] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
[19]	"Structural basis for activation of fatty acid-binding protein 4." Gillilan R.E., Ayers S.D., Noy N. J. Mol. Biol. 372:1246-1260(2007) [PubMed: 17761196] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH TROGLITAZONE AND LINOLEIC ACID, SUBUNIT, MUTAGENESIS OF PHE-58; LEU-67; LEU-87 AND LEU-92, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02109 mRNA. Translation: AAA39416.1.
M13264 , M13261, M13262, M13263 Genomic DNA. Translation: AAA39870.1.
M13385 Genomic DNA. Translation: AAA39417.1.
AK003143 mRNA. Translation: BAB22601.1.
BC054426 mRNA. Translation: AAH54426.1.
M20497 Genomic DNA. Translation: AAA37188.1.
M28726 mRNA. Translation: AAA37112.1.

IPI

IPI00116705.

PIR

B25952.

RefSeq

NP_077717.1. NM_024406.2.

UniGene

Mm.582.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A18	X-ray	2.40	A	2-131	[»]
1A2D	X-ray	2.40	A/B	2-131	[»]
1AB0	X-ray	1.90	A	3-131	[»]
1ACD	X-ray	2.70	A	3-131	[»]
1ADL	X-ray	1.60	A	2-132	[»]
1ALB	X-ray	2.50	A	2-132	[»]
1G74	X-ray	1.70	A	2-132	[»]
1G7N	X-ray	1.50	A	2-132	[»]
1LIB	X-ray	1.70	A	2-132	[»]
1LIC	X-ray	1.60	A	2-132	[»]
1LID	X-ray	1.60	A	2-132	[»]
1LIE	X-ray	1.60	A	2-132	[»]
1LIF	X-ray	1.60	A	2-132	[»]
2ANS	X-ray	2.50	A/B	2-132	[»]
2Q9S	X-ray	2.30	A	1-132	[»]
2QM9	X-ray	2.31	A/B	1-132	[»]
3HK1	X-ray	1.70	A	2-132	[»]
3JS1	X-ray	1.81	A/B	2-132	[»]
3JSQ	X-ray	2.30	A	2-132	[»]

ProteinModelPortal

P04117.

SMR

P04117. Positions 2-132.

ModBase

Search...

Protein-protein interaction databases

STRING

P04117.

PTM databases

PhosphoSite

P04117.

2D gel databases

SWISS-2DPAGE

P04117.

Proteomic databases

PRIDE

P04117.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.

GeneID

11770.

KEGG

mmu:11770.

Organism-specific databases

CTD

2167.

MGI

MGI:88038. Fabp4.

Phylogenomic databases

HOGENOM

HBG714759.

HOVERGEN

HBG005633.

InParanoid

P04117.

OMA

GQEFDEI.

OrthoDB

EOG4QC16R.

PhylomeDB

P04117.

Gene expression databases

ArrayExpress

P04117.

Bgee

P04117.

CleanEx

MM_FABP4.

Genevestigator

P04117.

GermOnline

ENSMUSG00000062515. Mus musculus.

Family and domain databases

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Gene3D

G3DSA:2.40.128.20. Calycin. 1 hit.

KO

K08753.

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

279545.

SOURCE

Search...

Entry information

Entry name

FABP4_MOUSE

Accession

Primary (citable) accession number: P04117

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program