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Protein

Fatty acid-binding protein, heart

Gene

Fabp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271Fatty acidBy similarity
Binding sitei129 – 1291Fatty acidBy similarity

GO - Molecular functioni

  • fatty acid binding Source: RGD
  • icosatetraenoic acid binding Source: RGD
  • long-chain fatty acid transporter activity Source: RGD
  • oleic acid binding Source: Ensembl

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
  • fatty acid metabolic process Source: RGD
  • long-chain fatty acid transport Source: RGD
  • response to drug Source: RGD
  • response to fatty acid Source: RGD
  • response to insulin Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, heart
Alternative name(s):
Fatty acid-binding protein 3
Heart-type fatty acid-binding protein
Short name:
H-FABP
Gene namesi
Name:Fabp3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi69048. Fabp3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • sarcoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 133132Fatty acid-binding protein, heartPRO_0000067325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei8 – 81PhosphothreonineCombined sources
Modified residuei20 – 201Phosphotyrosine; by Tyr-kinases1 Publication
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei30 – 301PhosphothreonineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07483.
PRIDEiP07483.

PTM databases

iPTMnetiP07483.
PhosphoSiteiP07483.

Expressioni

Tissue specificityi

Heart, but also skeletal muscle, kidney, brain and mammary gland.

Gene expression databases

GenevisibleiP07483. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017325.

Structurei

3D structure databases

ProteinModelPortaliP07483.
SMRiP07483. Positions 3-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP07483.
KOiK08752.
OMAiTWNLKES.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP07483.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDTI
60 70 80 90 100
TIKTHSTFKN TEISFQLGVE FDEVTADDRK VKSVVTLDGG KLVHVQKWDG
110 120 130
QETTLTRELS DGKLILTLTH GNVVSTRTYE KEA
Length:133
Mass (Da):14,775
Last modified:January 23, 2007 - v2
Checksum:i31B49953B232234E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641S → SN AA sequence (PubMed:3162235).Curated
Sequence conflicti70 – 701E → Q AA sequence (PubMed:2775193).Curated
Sequence conflicti71 – 711F → D AA sequence (PubMed:3162235).Curated
Sequence conflicti116 – 1161L → LL in AAF19003 (PubMed:10561574).Curated

Mass spectrometryi

Molecular mass is 14683.9±3 Da from positions 2 - 133. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18034 mRNA. Translation: AAA41137.1.
J02773 mRNA. Translation: AAA41136.1.
AF144090 Genomic DNA. Translation: AAF19003.1.
PIRiA28458. A27452.
RefSeqiNP_077076.1. NM_024162.1.
UniGeneiRn.32566.

Genome annotation databases

EnsembliENSRNOT00000017325; ENSRNOP00000017325; ENSRNOG00000012879.
GeneIDi79131.
KEGGirno:79131.
UCSCiRGD:69048. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18034 mRNA. Translation: AAA41137.1.
J02773 mRNA. Translation: AAA41136.1.
AF144090 Genomic DNA. Translation: AAF19003.1.
PIRiA28458. A27452.
RefSeqiNP_077076.1. NM_024162.1.
UniGeneiRn.32566.

3D structure databases

ProteinModelPortaliP07483.
SMRiP07483. Positions 3-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017325.

PTM databases

iPTMnetiP07483.
PhosphoSiteiP07483.

Proteomic databases

PaxDbiP07483.
PRIDEiP07483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017325; ENSRNOP00000017325; ENSRNOG00000012879.
GeneIDi79131.
KEGGirno:79131.
UCSCiRGD:69048. rat.

Organism-specific databases

CTDi2170.
RGDi69048. Fabp3.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP07483.
KOiK08752.
OMAiTWNLKES.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP07483.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-RNO-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

PROiP07483.

Gene expression databases

GenevisibleiP07483. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and tissue distribution of rat heart fatty acid binding protein mRNA: identical forms in heart and skeletal muscle."
    Claffey K.P., Herrera V.L., Brecher P., Ruiz-Opazo N.
    Biochemistry 26:7900-7904(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Analysis of the tissue-specific expression, developmental regulation, and linkage relationships of a rodent gene encoding heart fatty acid binding protein."
    Heuckeroth R.O., Birkenmeier E.H., Levin M.S., Gordon J.I.
    J. Biol. Chem. 262:9709-9717(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure and chromosomal location of the rat gene encoding the heart fatty acid-binding protein."
    Zhang J., Rickers-Haunerland J., Dawe I., Haunerland N.H.
    Eur. J. Biochem. 266:347-351(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
    Tissue: Heart.
  4. "Revision of the blocked N-terminus of rat heart fatty acid-binding protein by liquid secondary ion mass spectrometry."
    Gibson B.W., Yu Z., Aberth W., Burlingame A.L., Bass N.M.
    J. Biol. Chem. 263:4182-4185(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-133.
  5. "Primary structure and cellular distribution of two fatty acid-binding proteins in adult rat kidneys."
    Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.
    J. Biol. Chem. 266:5963-5972(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-133, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    Tissue: Kidney.
  6. "Rat heart fatty acid-binding protein is highly homologous to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin."
    Sacchettini J.C., Said B., Schulz H., Gordon J.I.
    J. Biol. Chem. 261:8218-8223(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-133.
  7. "Rat heart fatty acid-binding protein. Evidence that supports the amino acid sequence predicted from the cDNA."
    Kimura H., Hitomi M., Odani S., Koide T., Arakawa M., Ono T.
    Biochem. J. 260:303-306(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 59-87.
  8. Lubec G., Diao W.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 60-80 AND 114-127, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  9. "Purification and characterization of a fatty-acid-binding protein from the gastric mucosa of rats. Possible identity with heart fatty-acid-binding protein and its parietal cell localization."
    Kanda T., Iseki S., Hitomi M., Kimura H., Odani S., Kondo H., Matsubara Y., Muto T., Ono T.
    Eur. J. Biochem. 185:27-33(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Stomach.
  10. "Isolation and characterization of fatty acid binding proteins from mammary tissue of lactating rats."
    Jones P.D., Carne A., Bass N.M., Grigor M.R.
    Biochem. J. 251:919-925(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Mammary gland.
  11. "Differentiational regulation and phosphorylation of the fatty acid-binding protein from rat mammary epithelial cells."
    Nielsen S.U., Rump R., Hoejrup P., Roepstorff P., Spener F.
    Biochim. Biophys. Acta 1211:189-197(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-20.
    Tissue: Mammary gland.
  12. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-23; THR-30 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFABPH_RAT
AccessioniPrimary (citable) accession number: P07483
Secondary accession number(s): Q9QY04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.