FABPL_BOVIN
ID FABPL_BOVIN Reviewed; 127 AA.
AC P80425; Q2M2U0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fatty acid-binding protein, liver;
DE AltName: Full=Fatty acid-binding protein 1;
DE AltName: Full=Liver-type fatty acid-binding protein;
DE Short=L-FABP;
GN Name=FABP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND DEAMIDATION AT ASN-105.
RC TISSUE=Liver;
RX PubMed=8344916; DOI=10.1016/s0021-9258(19)85418-2;
RA Doermann P., Boerchers T., Korf U., Hoejrup P., Roepstorff P., Spener F.;
RT "Amino acid exchange and covalent modification by cysteine and glutathione
RT explain isoforms of fatty acid-binding protein occurring in bovine liver.";
RL J. Biol. Chem. 268:16286-16292(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8541331; DOI=10.1016/0005-2760(95)00170-0;
RA Rolf B., Oudenampsen-Krueger E., Boerchers T., Faergeman N.J., Knudsen J.,
RA Lezius A., Spener F.;
RT "Analysis of the ligand binding properties of recombinant bovine liver-type
RT fatty acid binding protein.";
RL Biochim. Biophys. Acta 1259:245-253(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- PTM: Deamidation and transpeptidation at the beta carboxyl of Asn-105
CC forms an isoaspartyl residue and Edman degradation appears as though
CC blocked. This rearrangement gives rise to an extra negative charge
CC carried by the acid form. {ECO:0000269|PubMed:8344916}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; X86904; CAA60506.1; -; mRNA.
DR EMBL; BC111622; AAI11623.1; -; mRNA.
DR PIR; S54268; S54268.
DR RefSeq; NP_787011.1; NM_175817.3.
DR AlphaFoldDB; P80425; -.
DR SMR; P80425; -.
DR STRING; 9913.ENSBTAP00000054269; -.
DR iPTMnet; P80425; -.
DR PaxDb; P80425; -.
DR PeptideAtlas; P80425; -.
DR PRIDE; P80425; -.
DR Ensembl; ENSBTAT00000024032; ENSBTAP00000024032; ENSBTAG00000018054.
DR GeneID; 327700; -.
DR KEGG; bta:327700; -.
DR CTD; 2168; -.
DR VEuPathDB; HostDB:ENSBTAG00000018054; -.
DR VGNC; VGNC:28695; FABP1.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155135; -.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; P80425; -.
DR OMA; DTITNTM; -.
DR OrthoDB; 1440574at2759; -.
DR Reactome; R-BTA-163560; Triglyceride catabolism.
DR Reactome; R-BTA-189483; Heme degradation.
DR Reactome; R-BTA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000018054; Expressed in caecum and 57 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
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; Isopeptide bond;
KW Lipid-binding; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..127
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067333"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8344916"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02692"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 105
FT /note="Deamidated asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8344916"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT CROSSLNK 105..106
FT /note="Isoaspartyl glycine isopeptide (Asn-Gly); alternate"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14227 MW; 97785E0F58EA663A CRC64;
MNFSGKYQVQ TQENYEAFMK AVGMPDDIIQ KGKDIKGVSE IVQNGKHFKF IITAGSKVIQ
NEFTLGEECE MEFMTGEKIK AVVQQEGDNK LVTTFKGIKS VTEFNGDTVT STMTKGDVVF
KRVSKRI
