P12104 (FABPI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty acid-binding protein, intestinal

Alternative name(s):
Fatty acid-binding protein 2
Intestinal-type fatty acid-binding protein
Short name=I-FABP

Gene names

Name:	FABP2
Synonyms:	FABPI

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	FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in the small intestine and at much lower levels in the large intestine. Highest expression levels in the jejunum. Ref.4
Induction	By EGF. Ref.5
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
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	digestion Traceable author statement Ref.9. Source: ProtInc fatty acid metabolic process Inferred from electronic annotation. Source: Compara intestinal absorption Inferred from electronic annotation. Source: Compara
Cellular_component	apical cortex Inferred from electronic annotation. Source: Compara microvillus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	fatty acid binding Traceable author statement Ref.1. Source: ProtInc long-chain fatty acid transporter activity Inferred from electronic annotation. Source: Compara
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, intestinal

PRO_0000067328

Sites

Binding site

83

1

Fatty acid By similarity

Binding site

107

1

Fatty acid By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Natural variant

55

1

A → T in 29% of the population; 2-fold greater affinity for long-chain fatty acids; increased fat oxidation and insulin resistance. Ref.3 Ref.8 Ref.9 Ref.10
Corresponds to variant rs1799883 [ dbSNP | Ensembl ].

VAR_002379

Experimental info

Mutagenesis

39

1

L → G: Reduced stability. Ref.6

Mutagenesis

64

1

E → G: Localized reduction in stability. Ref.6

Mutagenesis

65

1

L → A: Reduced stability. Ref.6

Mutagenesis

65

1

L → G: Reduced stability. Ref.6

Mutagenesis

67

1

V → G: Localized reduction in stability. Ref.6

Mutagenesis

90

1

L → G: Reduced stability. Ref.6

Mutagenesis

123

1

V → G: Reduced stability. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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132

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Helix

15 – 22

8

Helix

26 – 32

7

Turn

33 – 35

3

Beta strand

38 – 44

7

Beta strand

47 – 53

7

Beta strand

58 – 64

7

Beta strand

69 – 72

4

Beta strand

74 – 76

3

Beta strand

78 – 86

9

Beta strand

89 – 96

8

Turn

97 – 99

3

Beta strand

102 – 110

9

Beta strand

113 – 120

8

Beta strand

123 – 131

9

Sequences

	Sequence		Length	Mass (Da)
	P12104 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 68330E3D81792CAF	FASTA	132	15,207
	10 20 30 40 50 60 MAFDSTWKVD RSENYDKFME KMGVNIVKRK LAAHDNLKLT ITQEGNKFTV KESSAFRNIE 70 80 90 100 110 120 VVFELGVTFN YNLADGTELR GTWSLEGNKL IGKFKRTDNG NELNTVREII GDELVQTYVY 130 EGVEAKRIFK KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human and rodent intestinal fatty acid binding protein genes. A comparative analysis of their structure, expression, and linkage relationships." Sweetser D.A., Birkenmeier E.H., Klisak I.J., Zollman S., Sparkes R.S., Mohandas T., Lusis A.J., Gordon J.I. J. Biol. Chem. 262:16060-16071(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-55.
[4]	"Intestinal-type and liver-type fatty acid-binding protein in the intestine. Tissue distribution and clinical utility." Pelsers M.M.A.L., Namiot Z., Kisielewski W., Namiot A., Januszkiewicz M., Hermens W.T., Glatz J.F.C. Clin. Biochem. 36:529-535(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells." Darimont C., Gradoux N., de Pover A. Am. J. Physiol. 276:G606-G612(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY EGF.
[6]	"Consequences of single-site mutations in the intestinal fatty acid binding protein." Rajabzadeh M., Kao J., Frieden C. Biochemistry 42:12192-12199(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-39; GLU-64; LEU-65; VAL-67; LEU-90 AND VAL-123.
[7]	"Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit." Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A. J. Biomol. NMR 9:213-228(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR. Tissue: Intestine.
[8]	"Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism." Zhang F., Luecke C., Baier L.J., Sacchettini J.C., Hamilton J.A. Biochemistry 42:7339-7347(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF VARIANT THR-55.
[9]	"An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance." Baier L.J., Sacchettini J.C., Knowler W.C., Eads J., Paolisso G., Tataranni P.A., Mochizuki H., Bennett P.H., Bogardus C., Prochazka M. J. Clin. Invest. 95:1281-1287(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-55.
[10]	"The association of Ala54Thr variant of intestinal fatty acid binding protein gene with general and regional adipose tissue depots." Kunsan X., Taisan Z., Weiping J., Duoqi S., Wei D., Jie L., Junxi L., Rong Z. Chin. Med. Sci. J. 14:46-51(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-55.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18079 Genomic DNA. Translation: AAA52417.1.
AC092656 Genomic DNA. No translation available.
BC069466 mRNA. Translation: AAH69466.1.
BC069617 mRNA. Translation: AAH69617.1.
BC069625 mRNA. Translation: AAH69625.1.
BC069637 mRNA. Translation: AAH69637.1.
BC111791 mRNA. Translation: AAI11792.1.

IPI

IPI00218477.

PIR

FZHUI. A29781.

RefSeq

NP_000125.2. NM_000134.3.

UniGene

Hs.282265.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KZW	NMR	-	A	2-132	[»]
1KZX	NMR	-	A	2-132	[»]
3AKM	X-ray	1.90	A/B/C/D	2-132	[»]
3IFB	NMR	-	A	2-132	[»]

ProteinModelPortal

P12104.

ModBase

Search...

Protein-protein interaction databases

IntAct

P12104. 1 interaction.

STRING

9606.ENSP00000274024.

PTM databases

PhosphoSite

P12104.

Polymorphism databases

DMDM

119805.

Proteomic databases

PaxDb

P12104.

PRIDE

P12104.

Protocols and materials databases

DNASU

2169.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000274024; ENSP00000274024; ENSG00000145384.

GeneID

2169.

KEGG

hsa:2169.

UCSC

uc003icw.3. human.

Organism-specific databases

CTD

2169.

GeneCards

GC04M120238.

H-InvDB

HIX0004469.

HGNC

HGNC:3556. FABP2.

HPA

CAB047325.
HPA034607.

MIM

134640. gene.

neXtProt

NX_P12104.

PharmGKB

PA27957.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295259.

HOGENOM

HOG000004829.

HOVERGEN

HBG005633.

InParanoid

P12104.

KO

K08751.

OrthoDB

EOG45TCPM.

Gene expression databases

Bgee

P12104.

CleanEx

HS_FABP2.

Genevestigator

P12104.

GermOnline

ENSG00000145384. 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

P12104.

ChEMBL

CHEMBL4879.

ChiTaRS

FABP2. human.

EvolutionaryTrace

P12104.

GenomeRNAi

2169.

NextBio

8759.

SOURCE

Search...

Entry information

Entry name

FABPI_HUMAN

Accession

Primary (citable) accession number: P12104
Secondary accession number(s): Q2NKJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 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.