P15090 (FABP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid-binding protein, adipocyte

Alternative name(s):
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

Gene names

Name:

FABP4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 By similarity.
Subunit structure	Homodimer. Interacts with PPARG By similarity. Monomer. Ref.8
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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
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 electronic annotation. Source: Compara cellular response to lithium ion Inferred from electronic annotation. Source: Compara cholesterol homeostasis Inferred from electronic annotation. Source: Compara cytokine production Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of inflammatory response Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome triglyceride catabolic process Traceable author statement. Source: Reactome white fat cell differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	lipid particle Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fatty acid binding Traceable author statement Ref.1. Source: ProtInc 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 – 132

131

Fatty acid-binding protein, adipocyte

PRO_0000067366

Regions

Region

127 – 129

3

Fatty acid binding

Motif

22 – 32

11

Nuclear localization signal By similarity

Amino acid modifications

Modified residue

20

1

Phosphotyrosine; by Tyr-kinases By similarity

Natural variations

Natural variant

23

1

E → D in a breast cancer sample; somatic mutation. Ref.6

VAR_036320

Secondary structure

1

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132

Helix Strand Turn

Details...

Helix

2 – 5

4

Beta strand

7 – 16

10

Helix

17 – 24

8

Helix

28 – 36

9

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)
	P15090 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 819D788FF4BF7235	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

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] [Europe PMC] [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]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Urinary bladder.
[6]	"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. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-23.
[7]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
[8]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID, SUBUNIT, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02874 mRNA. Translation: AAA51689.1.
BT006809 mRNA. Translation: AAP35455.1.
CR456903 mRNA. Translation: CAG33184.1.
CH471068 Genomic DNA. Translation: EAW87092.1.
BC003672 mRNA. Translation: AAH03672.1.

IPI

IPI00215746.

PIR

FZHUF. A33363.

RefSeq

NP_001433.1. NM_001442.2.

UniGene

Hs.391561.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-132	[»]
3FR2	X-ray	2.20	A	2-132	[»]
3FR4	X-ray	2.16	A	1-132	[»]
3FR5	X-ray	2.20	A	2-132	[»]
3P6C	X-ray	1.25	A	1-132	[»]
3P6D	X-ray	1.06	A	1-132	[»]
3P6E	X-ray	1.08	A	1-132	[»]
3P6F	X-ray	1.20	A	1-132	[»]
3P6G	X-ray	1.20	A	1-132	[»]
3P6H	X-ray	1.15	A	1-132	[»]
3Q6L	X-ray	1.40	A	1-132	[»]
3RZY	X-ray	1.08	A	1-132	[»]

ProteinModelPortal

P15090.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15090. 3 interactions.

MINT

MINT-1398507.

STRING

9606.ENSP00000256104.

PTM databases

PhosphoSite

P15090.

Polymorphism databases

DMDM

119781.

2D gel databases

UCD-2DPAGE

P15090.

Proteomic databases

PaxDb

P15090.

PeptideAtlas

P15090.

PRIDE

P15090.

Protocols and materials databases

DNASU

2167.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256104; ENSP00000256104; ENSG00000170323.

GeneID

2167.

KEGG

hsa:2167.

UCSC

uc003ycd.2. human.

Organism-specific databases

CTD

2167.

GeneCards

GC08M082390.

HGNC

HGNC:3559. FABP4.

HPA

CAB024961.
HPA002188.

MIM

600434. gene.

neXtProt

NX_P15090.

PharmGKB

PA27960.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326764.

HOGENOM

HOG000004829.

HOVERGEN

HBG005633.

InParanoid

P15090.

KO

K08753.

OMA

GQEFDEI.

OrthoDB

EOG4QC16R.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P15090.

Bgee

P15090.

CleanEx

HS_FABP4.

Genevestigator

P15090.

GermOnline

ENSG00000170323. Homo sapiens.

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

BindingDB

P15090.

ChEMBL

CHEMBL2083.

ChiTaRS

FABP4. human.

EvolutionaryTrace

P15090.

GenomeRNAi

2167.

NextBio

8751.

SOURCE

Search...

Entry information

Entry name

FABP4_HUMAN

Accession

Primary (citable) accession number: P15090
Secondary accession number(s): Q6IBA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.