FABP4_PIG
ID FABP4_PIG Reviewed; 132 AA.
AC O97788; A0SXU3; A0SXU5; A0SXV1; A0SXV2; A0SXW5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Fatty acid-binding protein, adipocyte;
DE AltName: Full=AP2;
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Duroc; TISSUE=Liver;
RX PubMed=9880671; DOI=10.1007/s003359900918;
RA Gerbens F.N.A., Jansen A., van Erp A.J.M., Harders F., Meuwissen T.H.E.,
RA Rettenberger G.F.W., Veerkamp J.H., te Pas M.F.W.;
RT "The adipocyte fatty acid-binding protein locus: characterization and
RT association with intramuscular fat content in pigs.";
RL Mamm. Genome 9:1022-1026(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gerbens F.N.A.;
RT "Genetic control of intramuscular fat accretion in pigs. The role of heart
RT and adipocyte fatty acid-binding proteins.";
RL Thesis (2000), University of Nijmegen, Netherlands.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL373, DU271, IB113, IB114, IB415, IB521, LD400, LD518, LD519,
RC LD520, LW399, LW429, MS405, PN149, PN157, TW372, VT104, WB11, WB12, WB281,
RC and WB7;
RX PubMed=17057239; DOI=10.1534/genetics.106.063057;
RA Ojeda A., Rozas J., Folch J.M., Perez-Enciso M.;
RT "Unexpected high polymorphism at the FABP4 gene unveils a complex history
RT for pig populations.";
RL Genetics 174:2119-2127(2006).
RN [4]
RP PROTEIN SEQUENCE OF 37-48, AND TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=2334399; DOI=10.1042/bj2670373;
RA Armstrong M.K., Bernlohr D.A., Storch J., Clarke S.D.;
RT "The purification and characterization of a fatty acid binding protein
RT specific to pig (Sus domesticus) adipose tissue.";
RL Biochem. J. 267:373-378(1990).
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). Involved in the regulation of intramuscular fat accretion
CC (PubMed:9880671). {ECO:0000250|UniProtKB:P04117,
CC ECO:0000269|PubMed:9880671}.
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 -!- TISSUE SPECIFICITY: Adipose tissue. {ECO:0000269|PubMed:2334399}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; Y16039; CAA75995.1; -; Genomic_DNA.
DR EMBL; AJ416020; CAC95166.1; -; mRNA.
DR EMBL; EF061460; ABK58143.1; -; Genomic_DNA.
DR EMBL; EF061461; ABK58144.1; -; Genomic_DNA.
DR EMBL; EF061462; ABK58145.1; -; Genomic_DNA.
DR EMBL; EF061463; ABK58146.1; -; Genomic_DNA.
DR EMBL; EF061464; ABK58147.1; -; Genomic_DNA.
DR EMBL; EF061466; ABK58149.1; -; Genomic_DNA.
DR EMBL; EF061467; ABK58150.1; -; Genomic_DNA.
DR EMBL; EF061468; ABK58151.1; -; Genomic_DNA.
DR EMBL; EF061469; ABK58152.1; -; Genomic_DNA.
DR EMBL; EF061470; ABK58153.1; -; Genomic_DNA.
DR EMBL; EF061471; ABK58154.1; -; Genomic_DNA.
DR EMBL; EF061473; ABK58156.1; -; Genomic_DNA.
DR EMBL; EF061474; ABK58157.1; -; Genomic_DNA.
DR EMBL; EF061475; ABK58158.1; -; Genomic_DNA.
DR EMBL; EF061476; ABK58159.1; -; Genomic_DNA.
DR EMBL; EF061477; ABK58160.1; -; Genomic_DNA.
DR EMBL; EF061478; ABK58161.1; -; Genomic_DNA.
DR EMBL; EF061479; ABK58162.1; -; Genomic_DNA.
DR EMBL; EF061480; ABK58163.1; -; Genomic_DNA.
DR EMBL; EF061481; ABK58164.1; -; Genomic_DNA.
DR EMBL; EF061482; ABK58165.1; -; Genomic_DNA.
DR RefSeq; NP_001002817.1; NM_001002817.1.
DR AlphaFoldDB; O97788; -.
DR SMR; O97788; -.
DR PeptideAtlas; O97788; -.
DR PRIDE; O97788; -.
DR Ensembl; ENSSSCT00000064366; ENSSSCP00000036513; ENSSSCG00000040681.
DR Ensembl; ENSSSCT00005025544; ENSSSCP00005015468; ENSSSCG00005016220.
DR Ensembl; ENSSSCT00015103161; ENSSSCP00015042945; ENSSSCG00015076444.
DR Ensembl; ENSSSCT00025076427; ENSSSCP00025033140; ENSSSCG00025055830.
DR Ensembl; ENSSSCT00030059862; ENSSSCP00030027415; ENSSSCG00030042952.
DR Ensembl; ENSSSCT00035027047; ENSSSCP00035010335; ENSSSCG00035020786.
DR Ensembl; ENSSSCT00040079578; ENSSSCP00040034369; ENSSSCG00040058622.
DR Ensembl; ENSSSCT00045013136; ENSSSCP00045009060; ENSSSCG00045007828.
DR Ensembl; ENSSSCT00050055514; ENSSSCP00050023540; ENSSSCG00050040975.
DR Ensembl; ENSSSCT00055018700; ENSSSCP00055014736; ENSSSCG00055009580.
DR Ensembl; ENSSSCT00060068946; ENSSSCP00060029649; ENSSSCG00060050693.
DR Ensembl; ENSSSCT00065037806; ENSSSCP00065015928; ENSSSCG00065028040.
DR GeneID; 399533; -.
DR KEGG; ssc:399533; -.
DR CTD; 2167; -.
DR GeneTree; ENSGT00940000160340; -.
DR InParanoid; O97788; -.
DR OMA; LTAKCIM; -.
DR OrthoDB; 1417203at2759; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000040681; Expressed in subcutaneous adipose tissue and 39 other tissues.
DR ExpressionAtlas; O97788; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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: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; 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:0070346; P:positive regulation of fat cell proliferation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; 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_0000067368"
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; 14676 MW; 653389F3C1ABBAB2 CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN LIITVNGDMI TIRSESTFKN
TEIAFKLGQE FDEVTADDRK VKSTITLDGG ALVQVQKWDG KTTTINRKIV DDKLVVECIM
KGVTATRIYE RA
