FABPH_RAT
ID FABPH_RAT Reviewed; 133 AA.
AC P07483; Q9QY04;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Fatty acid-binding protein, heart;
DE AltName: Full=Fatty acid-binding protein 3;
DE AltName: Full=Heart-type fatty acid-binding protein;
DE Short=H-FABP;
GN Name=Fabp3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3427112; DOI=10.1021/bi00398a054;
RA Claffey K.P., Herrera V.L., Brecher P., Ruiz-Opazo N.;
RT "Cloning and tissue distribution of rat heart fatty acid binding protein
RT mRNA: identical forms in heart and skeletal muscle.";
RL Biochemistry 26:7900-7904(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3036869; DOI=10.1016/s0021-9258(18)47992-6;
RA Heuckeroth R.O., Birkenmeier E.H., Levin M.S., Gordon J.I.;
RT "Analysis of the tissue-specific expression, developmental regulation, and
RT linkage relationships of a rodent gene encoding heart fatty acid binding
RT protein.";
RL J. Biol. Chem. 262:9709-9717(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Heart;
RX PubMed=10561574; DOI=10.1046/j.1432-1327.1999.00860.x;
RA Zhang J., Rickers-Haunerland J., Dawe I., Haunerland N.H.;
RT "Structure and chromosomal location of the rat gene encoding the heart
RT fatty acid-binding protein.";
RL Eur. J. Biochem. 266:347-351(1999).
RN [4]
RP PROTEIN SEQUENCE OF 2-133.
RX PubMed=3162235; DOI=10.1016/s0021-9258(18)68906-9;
RA Gibson B.W., Yu Z., Aberth W., Burlingame A.L., Bass N.M.;
RT "Revision of the blocked N-terminus of rat heart fatty acid-binding protein
RT by liquid secondary ion mass spectrometry.";
RL J. Biol. Chem. 263:4182-4185(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-133, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RC TISSUE=Kidney;
RX PubMed=2005132; DOI=10.1016/s0021-9258(19)67692-1;
RA Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.;
RT "Primary structure and cellular distribution of two fatty acid-binding
RT proteins in adult rat kidneys.";
RL J. Biol. Chem. 266:5963-5972(1991).
RN [6]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-133.
RX PubMed=2424895; DOI=10.1016/s0021-9258(19)83898-x;
RA Sacchettini J.C., Said B., Schulz H., Gordon J.I.;
RT "Rat heart fatty acid-binding protein is highly homologous to the murine
RT adipocyte 422 protein and the P2 protein of peripheral nerve myelin.";
RL J. Biol. Chem. 261:8218-8223(1986).
RN [7]
RP PROTEIN SEQUENCE OF 59-87.
RX PubMed=2775193; DOI=10.1042/bj2600303;
RA Kimura H., Hitomi M., Odani S., Koide T., Arakawa M., Ono T.;
RT "Rat heart fatty acid-binding protein. Evidence that supports the amino
RT acid sequence predicted from the cDNA.";
RL Biochem. J. 260:303-306(1989).
RN [8]
RP PROTEIN SEQUENCE OF 60-80 AND 114-127, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (NOV-2006) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Stomach;
RX PubMed=2806260; DOI=10.1111/j.1432-1033.1989.tb15076.x;
RA Kanda T., Iseki S., Hitomi M., Kimura H., Odani S., Kondo H., Matsubara Y.,
RA Muto T., Ono T.;
RT "Purification and characterization of a fatty-acid-binding protein from the
RT gastric mucosa of rats. Possible identity with heart fatty-acid-binding
RT protein and its parietal cell localization.";
RL Eur. J. Biochem. 185:27-33(1989).
RN [10]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Mammary gland;
RX PubMed=3415652; DOI=10.1042/bj2510919;
RA Jones P.D., Carne A., Bass N.M., Grigor M.R.;
RT "Isolation and characterization of fatty acid binding proteins from mammary
RT tissue of lactating rats.";
RL Biochem. J. 251:919-925(1988).
RN [11]
RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-20.
RC TISSUE=Mammary gland;
RX PubMed=8117746; DOI=10.1016/0005-2760(94)90268-2;
RA Nielsen S.U., Rump R., Hoejrup P., Roepstorff P., Spener F.;
RT "Differentiational regulation and phosphorylation of the fatty acid-binding
RT protein from rat mammary epithelial cells.";
RL Biochim. Biophys. Acta 1211:189-197(1994).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-23; THR-30 AND SER-83,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: FABP are thought to play a role in the intracellular
CC transport of long-chain fatty acids and their acyl-CoA esters.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Heart, but also skeletal muscle, kidney, brain and
CC mammary gland.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=14683.9; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8117746};
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M18034; AAA41137.1; -; mRNA.
DR EMBL; J02773; AAA41136.1; -; mRNA.
DR EMBL; AF144090; AAF19003.1; -; Genomic_DNA.
DR PIR; A28458; A27452.
DR RefSeq; NP_077076.1; NM_024162.1.
DR AlphaFoldDB; P07483; -.
DR SMR; P07483; -.
DR BioGRID; 249415; 1.
DR STRING; 10116.ENSRNOP00000017325; -.
DR iPTMnet; P07483; -.
DR PhosphoSitePlus; P07483; -.
DR PaxDb; P07483; -.
DR PRIDE; P07483; -.
DR Ensembl; ENSRNOT00000017325; ENSRNOP00000017325; ENSRNOG00000012879.
DR GeneID; 79131; -.
DR KEGG; rno:79131; -.
DR UCSC; RGD:69048; rat.
DR CTD; 2170; -.
DR RGD; 69048; Fabp3.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155104; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P07483; -.
DR OMA; TRQVACM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P07483; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR PRO; PR:P07483; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012879; Expressed in heart and 20 other tissues.
DR Genevisible; P07483; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016528; C:sarcoplasm; IDA:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; IPI:RGD.
DR GO; GO:0050543; F:icosatetraenoic acid binding; IPI:RGD.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IPI:RGD.
DR GO; GO:0070538; F:oleic acid binding; ISO:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; NAS:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEP:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0032365; P:intracellular lipid transport; ISO:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:RGD.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0140214; P:positive regulation of long-chain fatty acid import into cell; ISO:RGD.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; ISO:RGD.
DR GO; GO:2001245; P:regulation of phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2005132,
FT ECO:0000269|PubMed:3162235"
FT CHAIN 2..133
FT /note="Fatty acid-binding protein, heart"
FT /id="PRO_0000067325"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000250|UniProtKB:P05413"
FT BINDING 127..129
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:P05413"
FT BINDING 127..129
FT /ligand="octadecanoate"
FT /ligand_id="ChEBI:CHEBI:25629"
FT /evidence="ECO:0000250|UniProtKB:P05413"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2005132"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:8117746"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 64
FT /note="S -> SN (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="F -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> LL (in Ref. 3; AAF19003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 133 AA; 14775 MW; 31B49953B232234E CRC64;
MADAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDTI TIKTHSTFKN
TEISFQLGVE FDEVTADDRK VKSVVTLDGG KLVHVQKWDG QETTLTRELS DGKLILTLTH
GNVVSTRTYE KEA
