FABPL_MOUSE
ID FABPL_MOUSE Reviewed; 127 AA.
AC P12710;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Fatty acid-binding protein, liver;
DE AltName: Full=14 kDa selenium-binding protein;
DE AltName: Full=Fatty acid-binding protein 1;
DE AltName: Full=Liver-type fatty acid-binding protein;
DE Short=L-FABP;
GN Name=Fabp1; Synonyms=Fabpl;
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 TISSUE=Liver;
RA Wolfrum C., Ellinghaus P., Kannenberg F., Seedorf U., Assmann G.,
RA Boerchers T., Spener F.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP PROTEIN SEQUENCE OF 21-113.
RX PubMed=2760043; DOI=10.1016/s0021-9258(18)80069-2;
RA Bansai M.P., Cook R.G., Danielson K.G., Medina D.;
RT "A 14-kilodalton selenium-binding protein in mouse liver is fatty acid-
RT binding protein.";
RL J. Biol. Chem. 264:13780-13784(1989).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-36; LYS-46; LYS-57;
RP LYS-78; LYS-84; LYS-90 AND LYS-121, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in
CC hepatocytes. Binds cholesterol. Binds free fatty acids and their
CC coenzyme A derivatives, bilirubin, and some other small molecules in
CC the cytoplasm. May be involved in intracellular lipid transport.
CC {ECO:0000250|UniProtKB:P07148, ECO:0000250|UniProtKB:P82289}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y14660; CAA74989.1; -; mRNA.
DR EMBL; BC009812; AAH09812.1; -; mRNA.
DR CCDS; CCDS20226.1; -.
DR PIR; A32640; A32640.
DR RefSeq; NP_059095.1; NM_017399.4.
DR AlphaFoldDB; P12710; -.
DR SMR; P12710; -.
DR BioGRID; 199584; 3.
DR IntAct; P12710; 2.
DR STRING; 10090.ENSMUSP00000064655; -.
DR BindingDB; P12710; -.
DR GuidetoPHARMACOLOGY; 2531; -.
DR CarbonylDB; P12710; -.
DR iPTMnet; P12710; -.
DR PhosphoSitePlus; P12710; -.
DR SWISS-2DPAGE; P12710; -.
DR jPOST; P12710; -.
DR PaxDb; P12710; -.
DR PeptideAtlas; P12710; -.
DR PRIDE; P12710; -.
DR ProteomicsDB; 267704; -.
DR Antibodypedia; 3707; 640 antibodies from 40 providers.
DR DNASU; 14080; -.
DR Ensembl; ENSMUST00000067492; ENSMUSP00000064655; ENSMUSG00000054422.
DR GeneID; 14080; -.
DR KEGG; mmu:14080; -.
DR UCSC; uc009cgh.1; mouse.
DR CTD; 2168; -.
DR MGI; MGI:95479; Fabp1.
DR VEuPathDB; HostDB:ENSMUSG00000054422; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; P12710; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 1440574at2759; -.
DR PhylomeDB; P12710; -.
DR TreeFam; TF330348; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 14080; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fabp1; mouse.
DR PRO; PR:P12710; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P12710; protein.
DR Bgee; ENSMUSG00000054422; Expressed in small intestine Peyer's patch and 106 other tissues.
DR ExpressionAtlas; P12710; baseline and differential.
DR Genevisible; P12710; MM.
DR GO; GO:0045179; C:apical cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0032052; F:bile acid binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound 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:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0050892; P:intestinal absorption; ISO:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:MGI.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR031276; Lb-FABP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF96; PTHR11955:SF96; 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; Selenium; Transport.
FT CHAIN 1..127
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067335"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80425"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02692"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 127 AA; 14246 MW; 2C787139174DD24D CRC64;
MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR
NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY
KRVSKRI
