FABP4_ICTTR
ID FABP4_ICTTR Reviewed; 132 AA.
AC Q99P60;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
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 Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX PubMed=11779641; DOI=10.1016/s0167-4781(01)00338-4;
RA Hittel D., Storey K.B.;
RT "Differential expression of adipose- and heart-type fatty acid binding
RT proteins in hibernating ground squirrels.";
RL Biochim. Biophys. Acta 1522:238-243(2001).
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 (By
CC similarity). FABPs are important elements related to the hibernating
CC state in mammals (PubMed:11779641). {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 -!- INDUCTION: Up-regulated during hibernation in brown adipose tissue.
CC {ECO:0000269|PubMed:11779641}.
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}.
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; AF327855; AAK08084.1; -; mRNA.
DR RefSeq; NP_001269191.1; NM_001282262.1.
DR AlphaFoldDB; Q99P60; -.
DR SMR; Q99P60; -.
DR STRING; 43179.ENSSTOP00000007662; -.
DR Ensembl; ENSSTOT00000008548; ENSSTOP00000007662; ENSSTOG00000008554.
DR GeneID; 101975999; -.
DR CTD; 2167; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160340; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; Q99P60; -.
DR OMA; LTAKCIM; -.
DR OrthoDB; 1417203at2759; -.
DR TreeFam; TF316894; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051427; F:hormone receptor binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hibernation; Lipid-binding; Nucleus;
KW Phosphoprotein; 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_0000067370"
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:0000250|UniProtKB:P04117"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
SQ SEQUENCE 132 AA; 14765 MW; FCB14230E34C0708 CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIRSESTFKN
TEISFKLGQE FDEVTADDRK VKSIITLDGG VLVQVQKWDG KSTTIKRKRE DDKLVVECVM
KGVTSTRVYE RA
