FABPH_MOUSE
ID FABPH_MOUSE Reviewed; 133 AA.
AC P11404; Q91W23;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 188.
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;
DE AltName: Full=Mammary-derived growth inhibitor;
DE Short=MDGI;
GN Name=Fabp3; Synonyms=Fabph1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA;
RX PubMed=2740224; DOI=10.1093/nar/17.11.4374;
RA Tweedie S., Edwards Y.;
RT "cDNA sequence for mouse heart fatty acid binding protein, H-FABP.";
RL Nucleic Acids Res. 17:4374-4374(1989).
RN [2]
RP SEQUENCE REVISION TO 3-4.
RA Tweedie S.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ICR X Swiss Webster; TISSUE=Liver;
RX PubMed=7926807; DOI=10.1016/0378-1119(94)90073-6;
RA Treuner M., Kozak C.A., Gallahan D., Grosse R., Mueller T.;
RT "Cloning and characterization of the mouse gene encoding mammary-derived
RT growth inhibitor/heart-fatty acid-binding protein.";
RL Gene 147:237-242(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Mammary gland;
RX PubMed=1429365; DOI=10.1007/bf02631038;
RA Binas B., Spitzer E., Zschiesche W., Erdmann B., Kurtz A., Mueller T.,
RA Niemann C., Blenau W., Grosse R.;
RT "Hormonal induction of functional differentiation and mammary-derived
RT growth inhibitor expression in cultured mouse mammary gland explants.";
RL In Vitro Cell. Dev. Biol. 28A:625-634(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 60-79 AND 114-127, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; X14961; CAA33084.1; -; mRNA.
DR EMBL; U02884; AAA61933.1; -; Genomic_DNA.
DR EMBL; U02883; AAA03445.1; -; mRNA.
DR EMBL; BC002082; AAH02082.1; -; mRNA.
DR CCDS; CCDS18709.1; -.
DR PIR; PC4011; PC4011.
DR RefSeq; NP_034304.1; NM_010174.1.
DR AlphaFoldDB; P11404; -.
DR SMR; P11404; -.
DR BioGRID; 199582; 3.
DR IntAct; P11404; 6.
DR STRING; 10090.ENSMUSP00000070709; -.
DR iPTMnet; P11404; -.
DR PhosphoSitePlus; P11404; -.
DR REPRODUCTION-2DPAGE; IPI00230124; -.
DR REPRODUCTION-2DPAGE; P11404; -.
DR SWISS-2DPAGE; P11404; -.
DR UCD-2DPAGE; P11404; -.
DR CPTAC; non-CPTAC-3706; -.
DR jPOST; P11404; -.
DR PaxDb; P11404; -.
DR PeptideAtlas; P11404; -.
DR PRIDE; P11404; -.
DR ProteomicsDB; 275846; -.
DR Antibodypedia; 4505; 1156 antibodies from 41 providers.
DR DNASU; 14077; -.
DR Ensembl; ENSMUST00000070532; ENSMUSP00000070709; ENSMUSG00000028773.
DR GeneID; 14077; -.
DR KEGG; mmu:14077; -.
DR UCSC; uc008uzd.1; mouse.
DR CTD; 2170; -.
DR MGI; MGI:95476; Fabp3.
DR VEuPathDB; HostDB:ENSMUSG00000028773; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155104; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P11404; -.
DR OMA; TRQVACM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P11404; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 14077; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Fabp3; mouse.
DR PRO; PR:P11404; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P11404; protein.
DR Bgee; ENSMUSG00000028773; Expressed in heart and 117 other tissues.
DR ExpressionAtlas; P11404; baseline and differential.
DR Genevisible; P11404; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016528; C:sarcoplasm; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0050543; F:icosatetraenoic acid binding; ISO:MGI.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISO:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0070538; F:oleic acid binding; ISO:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0032365; P:intracellular lipid transport; IMP:BHF-UCL.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:ARUK-UCL.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
DR GO; GO:0140214; P:positive regulation of long-chain fatty acid import into cell; IDA:ARUK-UCL.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IC:BHF-UCL.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; IMP:BHF-UCL.
DR GO; GO:2001245; P:regulation of phosphatidylcholine biosynthetic process; IGI:MGI.
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:0000250|UniProtKB:P07483"
FT CHAIN 2..133
FT /note="Fatty acid-binding protein, heart"
FT /id="PRO_0000067322"
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:0000250|UniProtKB:P07483"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT CONFLICT 34
FT /note="A -> G (in Ref. 1; CAA33084)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> D (in Ref. 1; CAA33084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 133 AA; 14819 MW; F78BFF5A7533DD9A CRC64;
MADAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDTI TIKTQSTFKN
TEINFQLGIE FDEVTADDRK VKSLVTLDGG KLIHVQKWNG QETTLTRELV DGKLILTLTH
GSVVSTRTYE KEA
