ID   FABP4_BOVIN             Reviewed;         132 AA.
AC   P48035;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 123.
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   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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=8702709; DOI=10.1074/jbc.271.33.19943;
RA   Specht B., Bartetzko N., Hohoff C., Kuhl H., Franke R., Boerchers T.,
RA   Spener F.;
RT   "Mammary derived growth inhibitor is not a distinct protein but a mix of
RT   heart-type and adipocyte-type fatty acid-binding protein.";
RL   J. Biol. Chem. 271:19943-19949(1996).
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; X89244; CAA61532.1; -; mRNA.
DR   PIR; S57744; S57744.
DR   RefSeq; NP_776739.1; NM_174314.2.
DR   AlphaFoldDB; P48035; -.
DR   SMR; P48035; -.
DR   STRING; 9913.ENSBTAP00000000079; -.
DR   PaxDb; P48035; -.
DR   PeptideAtlas; P48035; -.
DR   PRIDE; P48035; -.
DR   GeneID; 281759; -.
DR   KEGG; bta:281759; -.
DR   CTD; 2167; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   InParanoid; P48035; -.
DR   OrthoDB; 1417203at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:AgBase.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:AgBase.
DR   GO; GO:0071285; P:cellular response to lithium ion; ISS:AgBase.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISS:AgBase.
DR   GO; GO:0001816; P:cytokine production; ISS:AgBase.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:AgBase.
DR   GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:AgBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:AgBase.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:AgBase.
DR   GO; GO:0050872; P:white fat cell differentiation; ISS:AgBase.
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; 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_0000067365"
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;  14678 MW;  A787223AA5F1DD68 CRC64;
     MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPT LIISLNGGVV TIKSESTFKN
     TEISFKLGQE FDEITPDDRK VKSIVNLDEG ALVQVQNWDG KSTTIKRKLM DDKMVLECVM
     NGVTATRVYE RA