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Fatty acid-binding protein, heart (Fatty acid-binding protein 3) (Heart-type fatty acid-binding protein) (H-FABP)

 FABPH_RAT               Reviewed;         133 AA.
P07483; Q9QY04;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 144.
RecName: Full=Fatty acid-binding protein, heart;
AltName: Full=Fatty acid-binding protein 3;
AltName: Full=Heart-type fatty acid-binding protein;
Short=H-FABP;
Name=Fabp3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3427112; DOI=10.1021/bi00398a054;
Claffey K.P., Herrera V.L., Brecher P., Ruiz-Opazo N.;
"Cloning and tissue distribution of rat heart fatty acid binding
protein mRNA: identical forms in heart and skeletal muscle.";
Biochemistry 26:7900-7904(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3036869;
Heuckeroth R.O., Birkenmeier E.H., Levin M.S., Gordon J.I.;
"Analysis of the tissue-specific expression, developmental regulation,
and linkage relationships of a rodent gene encoding heart fatty acid
binding protein.";
J. Biol. Chem. 262:9709-9717(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar; TISSUE=Heart;
PubMed=10561574; DOI=10.1046/j.1432-1327.1999.00860.x;
Zhang J., Rickers-Haunerland J., Dawe I., Haunerland N.H.;
"Structure and chromosomal location of the rat gene encoding the heart
fatty acid-binding protein.";
Eur. J. Biochem. 266:347-351(1999).
[4]
PROTEIN SEQUENCE OF 2-133.
PubMed=3162235;
Gibson B.W., Yu Z., Aberth W., Burlingame A.L., Bass N.M.;
"Revision of the blocked N-terminus of rat heart fatty acid-binding
protein by liquid secondary ion mass spectrometry.";
J. Biol. Chem. 263:4182-4185(1988).
[5]
PROTEIN SEQUENCE OF 2-133, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT ALA-2.
TISSUE=Kidney;
PubMed=2005132;
Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.;
"Primary structure and cellular distribution of two fatty acid-binding
proteins in adult rat kidneys.";
J. Biol. Chem. 266:5963-5972(1991).
[6]
PRELIMINARY PROTEIN SEQUENCE OF 2-133.
PubMed=2424895;
Sacchettini J.C., Said B., Schulz H., Gordon J.I.;
"Rat heart fatty acid-binding protein is highly homologous to the
murine adipocyte 422 protein and the P2 protein of peripheral nerve
myelin.";
J. Biol. Chem. 261:8218-8223(1986).
[7]
PROTEIN SEQUENCE OF 59-87.
PubMed=2775193; DOI=10.1042/bj2600303;
Kimura H., Hitomi M., Odani S., Koide T., Arakawa M., Ono T.;
"Rat heart fatty acid-binding protein. Evidence that supports the
amino acid sequence predicted from the cDNA.";
Biochem. J. 260:303-306(1989).
[8]
PROTEIN SEQUENCE OF 60-80 AND 114-127, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Diao W.;
Submitted (NOV-2006) to UniProtKB.
[9]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Stomach;
PubMed=2806260; DOI=10.1111/j.1432-1033.1989.tb15076.x;
Kanda T., Iseki S., Hitomi M., Kimura H., Odani S., Kondo H.,
Matsubara Y., Muto T., Ono T.;
"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.";
Eur. J. Biochem. 185:27-33(1989).
[10]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Mammary gland;
PubMed=3415652; DOI=10.1042/bj2510919;
Jones P.D., Carne A., Bass N.M., Grigor M.R.;
"Isolation and characterization of fatty acid binding proteins from
mammary tissue of lactating rats.";
Biochem. J. 251:919-925(1988).
[11]
PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT
TYR-20.
TISSUE=Mammary gland;
PubMed=8117746; DOI=10.1016/0005-2760(94)90268-2;
Nielsen S.U., Rump R., Hoejrup P., Roepstorff P., Spener F.;
"Differentiational regulation and phosphorylation of the fatty acid-
binding protein from rat mammary epithelial cells.";
Biochim. Biophys. Acta 1211:189-197(1994).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-23; THR-30 AND
SER-83, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: FABP are thought to play a role in the intracellular
transport of long-chain fatty acids and their acyl-CoA esters.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Heart, but also skeletal muscle, kidney, brain
and mammary gland.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=14683.9; Mass_error=3;
Method=Electrospray; Range=2-133;
Evidence={ECO:0000269|PubMed:8117746};
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M18034; AAA41137.1; -; mRNA.
EMBL; J02773; AAA41136.1; -; mRNA.
EMBL; AF144090; AAF19003.1; -; Genomic_DNA.
PIR; A28458; A27452.
RefSeq; NP_077076.1; NM_024162.1.
UniGene; Rn.32566; -.
ProteinModelPortal; P07483; -.
STRING; 10116.ENSRNOP00000017325; -.
iPTMnet; P07483; -.
PhosphoSitePlus; P07483; -.
PaxDb; P07483; -.
PRIDE; P07483; -.
Ensembl; ENSRNOT00000017325; ENSRNOP00000017325; ENSRNOG00000012879.
GeneID; 79131; -.
KEGG; rno:79131; -.
UCSC; RGD:69048; rat.
CTD; 2170; -.
RGD; 69048; Fabp3.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P07483; -.
KO; K08752; -.
OMA; TWNLKES; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; P07483; -.
TreeFam; TF316894; -.
Reactome; R-RNO-163560; Triglyceride catabolism.
PRO; PR:P07483; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000012879; -.
Genevisible; P07483; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016528; C:sarcoplasm; IDA:RGD.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0005504; F:fatty acid binding; IPI:RGD.
GO; GO:0050543; F:icosatetraenoic acid binding; IPI:RGD.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IPI:RGD.
GO; GO:0070538; F:oleic acid binding; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0006635; P:fatty acid beta-oxidation; NAS:RGD.
GO; GO:0006631; P:fatty acid metabolic process; IEP:RGD.
GO; GO:0044539; P:long-chain fatty acid import; IEA:Ensembl.
GO; GO:0015909; P:long-chain fatty acid transport; IDA:RGD.
GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
GO; GO:0046320; P:regulation of fatty acid oxidation; IEA:Ensembl.
GO; GO:2001245; P:regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Lipid-binding; Phosphoprotein; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2005132,
ECO:0000269|PubMed:3162235}.
CHAIN 2 133 Fatty acid-binding protein, heart.
/FTId=PRO_0000067325.
BINDING 127 127 Fatty acid. {ECO:0000250}.
BINDING 129 129 Fatty acid. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:2005132}.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 20 20 Phosphotyrosine; by Tyr-kinases.
{ECO:0000269|PubMed:8117746}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 30 30 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 64 64 S -> SN (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 70 70 E -> Q (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 71 71 F -> D (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 L -> LL (in Ref. 3; AAF19003).
{ECO:0000305}.
SEQUENCE 133 AA; 14775 MW; 31B49953B232234E CRC64;
MADAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDTI TIKTHSTFKN
TEISFQLGVE FDEVTADDRK VKSVVTLDGG KLVHVQKWDG QETTLTRELS DGKLILTLTH
GNVVSTRTYE KEA


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