FABP4_RAT
ID FABP4_RAT Reviewed; 132 AA.
AC P70623;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Fatty acid-binding protein, adipocyte;
DE AltName: Full=Adipocyte lipid-binding protein;
DE Short=ALBP;
DE AltName: Full=Adipocyte-type fatty acid-binding protein;
DE Short=A-FABP;
DE Short=AFABP;
DE AltName: Full=Fatty acid-binding protein 4;
GN Name=Fabp4;
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].
RA Prinsen C., Veerkamp J.H.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP 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: Lipid transport protein in adipocytes. Binds both long chain
CC fatty acids and retinoic acid. Delivers long-chain fatty acids and
CC retinoic acid to their cognate receptors in the nucleus.
CC {ECO:0000250|UniProtKB:P04117}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer. Interacts with PPARG (By
CC similarity). {ECO:0000250|UniProtKB:P04117,
CC ECO:0000250|UniProtKB:P15090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus
CC {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the
CC ligand, a conformation change exposes a nuclear localization motif and
CC the protein is transported into the nucleus. Subject to constitutive
CC nuclear export. {ECO:0000250|UniProtKB:P04117}.
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; U75581; AAB18344.1; -; mRNA.
DR AlphaFoldDB; P70623; -.
DR SMR; P70623; -.
DR STRING; 10116.ENSRNOP00000014701; -.
DR BindingDB; P70623; -.
DR ChEMBL; CHEMBL2021755; -.
DR iPTMnet; P70623; -.
DR PhosphoSitePlus; P70623; -.
DR PaxDb; P70623; -.
DR PRIDE; P70623; -.
DR UCSC; RGD:69309; rat.
DR RGD; 69309; Fabp4.
DR eggNOG; KOG4015; Eukaryota.
DR InParanoid; P70623; -.
DR PhylomeDB; P70623; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR PRO; PR:P70623; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; ISO:RGD.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISS:UniProtKB.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR033073; FABP4.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF83; PTHR11955:SF83; 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; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15090"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, adipocyte"
FT /id="PRO_0000067369"
FT MOTIF 22..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 127..129
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P15090"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
SQ SEQUENCE 132 AA; 14708 MW; 5277E995DD99223B CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN LIISVEGDLV VIRSESTFKN
TEISFKLGVE FDEITPDDRK VKSIITLDGG VLVHVQKWDG KSTTIKKRRD GDKLVVECVM
KGVTSTRVYE RA
