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P55050 (FABPI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Ref.4

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in the small intestine. Highest expression levels in the proximal ileum. Ref.5

Domain

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior By similarity.

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
   LigandLipid-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 132131Fatty acid-binding protein, intestinal
PRO_0000067329

Sites

Binding site831Fatty acid By similarity
Binding site1071Fatty acid By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
P55050 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E02001EE47267456

FASTA13215,126
        10         20         30         40         50         60 
MAFDGTWKVD RNENYEKFME KMGINVMKRK LGAHDNLKLT ITQDGNKFTV KESSNFRNID 

        70         80         90        100        110        120 
VVFELGVNFP YSLADGTELT GAWTIEGNKL IGKFTRVDNG KELIAVREVS GNELIQTYTY 

       130 
EGVEAKRFFK KE 

« Hide

References

« Hide 'large scale' references
[1]"The mouse intestinal fatty acid binding protein gene: nucleotide sequence, pattern of developmental and regional expression, and proposed structure of its protein product."
Green R.P., Sacchettini J.C., Jackson K.E., Cohn S.M., Gordon J.I.
DNA Cell Biol. 11:31-41(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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: Small intestine.
[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].
Tissue: Colon.
[4]"The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice."
Vassileva G., Huwyler L., Poirier K., Agellon L.B., Toth M.J.
FASEB J. 14:2040-2046(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Fatty acid regulation of fatty acid-binding protein expression in the small intestine."
Poirier H., Niot I., Degrace P., Monnot M.C., Bernard A., Besnard P.
Am. J. Physiol. 273:G289-G295(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65034 mRNA. Translation: AAA37589.1.
AK007995 mRNA. Translation: BAB25397.1.
BC013457 mRNA. Translation: AAH13457.1.
RefSeqNP_032006.1. NM_007980.3.
UniGeneMm.28398.

3D structure databases

ProteinModelPortalP55050.
SMRP55050. Positions 2-132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023820.

PTM databases

PhosphoSiteP55050.

Proteomic databases

PaxDbP55050.
PRIDEP55050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023820; ENSMUSP00000023820; ENSMUSG00000023057.
GeneID14079.
KEGGmmu:14079.
UCSCuc008rex.1. mouse.

Organism-specific databases

CTD2169.
MGIMGI:95478. Fabp2.

Phylogenomic databases

eggNOGNOG295259.
HOGENOMHOG000004829.
HOVERGENHBG005633.
InParanoidP55050.
KOK08751.
OMANMVKRKL.
OrthoDBEOG7NW6BZ.
PhylomeDBP55050.
TreeFamTF316894.

Gene expression databases

BgeeP55050.
CleanExMM_FABP2.
GenevestigatorP55050.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285084.
PROP55050.
SOURCESearch...

Entry information

Entry nameFABPI_MOUSE
AccessionPrimary (citable) accession number: P55050
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot