Fatty acid-binding protein, adipocyte

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Reviewed, UniProtKB/Swiss-Prot P15090 (FABP4_HUMAN)

Last modified June 16, 2009. Version 95. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fatty acid-binding protein, adipocyte
Alternative name(s):
    A-FABP
      Short name=AFABP
    Fatty acid-binding protein 4
    Adipocyte lipid-binding protein
      Short name=ALBP

Gene names

Name:

FABP4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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 By similarity.
Subunit structure	Homodimer. Interacts with PPARG By similarity. Monomer.
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 By similarity.
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

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Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	fatty acid binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
EXT2	Q93063	1	EBI-715333,EBI-1047761
OSTF1	Q92882	1	EBI-715333,EBI-1051152
SNCG	O76070	1	EBI-715333,EBI-1053810

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 132

131

Fatty acid-binding protein, adipocyte

PRO_0000067366

Regions

Region

127 – 129

Fatty acid binding

Motif

22 – 32

Nuclear localization signal By similarity

Amino acid modifications

Modified residue

Phosphotyrosine; by Tyr-kinases By similarity

Natural variations

Natural variant

E → D in a breast cancer sample; somatic mutation. Ref.4

VAR_036320

Secondary structure

132

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P15090-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 819D788FF4BF7235
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FASTA

132

14,719

        10         20         30         40         50         60 
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN 

        70         80         90        100        110        120 
TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM 

       130 
KGVTSTRVYE RA

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA." Baxa C.A., Sha R.S., Buelt M.K., Smith A.J., Matarese V., Chinander L.L., Boundy K.L., Bernlohr D.A. Biochemistry 28:8683-8690(1989) [PubMed: 2481498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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]. Tissue: Urinary bladder.
[4]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-23.
[5]	"Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target." Lehmann F., Haile S., Axen E., Medina C., Uppenberg J., Svensson S., Lundbaeck T., Rondahl L., Barf T. Bioorg. Med. Chem. Lett. 14:4445-4448(2004) [PubMed: 15357969] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
[6]	"Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)." Marr E., Tardie M., Carty M., Brown Phillips T., Wang I.-K., Soeller W., Qiu X., Karam G. Acta Crystallogr. F 62:1058-1060(2006) [PubMed: 17077479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
BC003672 mRNA. Translation: AAH03672.1.

IPI

IPI00215746.

PIR

FZHUF. A33363.

RefSeq

NP_001433.1.

UniGene

Hs.391561

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TOU	X-ray	2.00	A	2-131	[»]
1TOW	X-ray	2.00	A	2-132	[»]
2HNX	X-ray	1.50	A	1-132	[»]
2NNQ	X-ray	1.80	A	2-131	[»]
3FR2	X-ray	2.20	A	2-132	[»]
3FR4	X-ray	2.16	A	1-132	[»]
3FR5	X-ray	2.20	A	2-132	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P15090. 4 interactions.

PTM databases

PhosphoSite

P15090.

Proteomic databases

PeptideAtlas

P15090.

PRIDE

P15090.

Genome annotation databases

Ensembl

ENSG00000170323. Homo sapiens. [Contig view]

GeneID

2167.

KEGG

hsa:2167.

Organism-specific databases

GeneCards

GC08M082553.

H-InvDB

HIX0007617.

HGNC

HGNC:3559. FABP4.

HPA

HPA002188.

MIM

600434. gene.

PharmGKB

PA27960.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P15090.

HOVERGEN

P15090.

OMA

P15090. GQEFDEI.

Enzyme and pathway databases

Reactome

REACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpress

P15090.

Bgee

P15090.

CleanEx

HS_FABP4.

GermOnline

ENSG00000170323. Homo sapiens.

Family and domain databases

InterPro

IPR012674. Calycin.
IPR000463. Fatty_acid_bd.
IPR000566. Lipocln_cytFABP.
[Graphical view]

Gene3D

G3DSA:2.40.128.20. Calycin. 1 hit.

PANTHER

PTHR11955. Fatty_acid_bd. 1 hit.

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00178. FATTYACIDBP.

PROSITE

PS00214. FABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8751.

SOURCE

Search...

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Entry information

Entry name

FABP4_HUMAN

Accession

Primary (citable) accession number: P15090

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents