FABP5_RAT
ID FABP5_RAT Reviewed; 135 AA.
AC P55053; P97757;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000305};
DE AltName: Full=Cutaneous fatty acid-binding protein;
DE Short=C-FABP;
DE AltName: Full=DA11;
DE AltName: Full=Epidermal-type fatty acid-binding protein;
DE Short=E-FABP;
DE AltName: Full=Fatty acid-binding protein, epidermal;
GN Name=Fabp5 {ECO:0000312|RGD:70997};
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].
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RX PubMed=7607553; DOI=10.1016/0378-1119(95)00168-6;
RA Wen Y., Li G.W., Chen P., Wong E., Bekhor I.;
RT "Lens epithelial cell mRNA, II. Expression of a mRNA encoding a lipid-
RT binding protein in rat lens epithelial cells.";
RL Gene 158:269-274(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Skin;
RX PubMed=8166694; DOI=10.1006/bbrc.1994.1442;
RA Watanabe R., Fujii H., Odani S., Sakakibara J., Yamamoto A., Ito M.,
RA Ono T.;
RT "Molecular cloning of a cDNA encoding a novel fatty acid-binding protein
RT from rat skin.";
RL Biochem. Biophys. Res. Commun. 200:253-259(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Nerve;
RX PubMed=8723767;
RX DOI=10.1002/(sici)1097-4547(19960501)44:3<283::aid-jnr9>3.0.co;2-c;
RA de Leon M., Welcher A.A., Nahin R.H., Liu Y., Ruda M.A., Shooter E.M.,
RA Molina C.A.;
RT "Fatty acid binding protein is induced in neurons of the dorsal root
RT ganglia after peripheral nerve injury.";
RL J. Neurosci. Res. 44:283-292(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DISULFIDE BOND.
RX PubMed=10965032; DOI=10.1093/oxfordjournals.jbchem.a022761;
RA Odani S., Namba Y., Ishii A., Ono T., Fujii H.;
RT "Disulfide bonds in rat cutaneous fatty acid-binding protein.";
RL J. Biochem. 128:355-361(2000).
RN [5]
RP PROTEIN SEQUENCE OF 13-33 AND 73-99, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP 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: Intracellular carrier for long-chain fatty acids and related
CC active lipids, such as endocannabinoids, that regulate the metabolism
CC and actions of the ligands they bind. In addition to the cytosolic
CC transport, selectively delivers specific fatty acids from the cytosol
CC to the nucleus, wherein they activate nuclear receptors (By
CC similarity). Delivers retinoic acid to the nuclear receptor peroxisome
CC proliferator-activated receptor delta; which promotes proliferation and
CC survival. May also serve as a synaptic carrier of endocannabinoid at
CC central synapses and thus controls retrograde endocannabinoid
CC signaling. Modulates inflammation by regulating PTGES induction via NF-
CC kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during
CC inflammation (By similarity). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000250|UniProtKB:Q05816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q05816}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05816}. Nucleus
CC {ECO:0000250|UniProtKB:Q01469}. Synapse {ECO:0000250|UniProtKB:Q05816}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q05816}. Secreted
CC {ECO:0000250|UniProtKB:Q05816}. Note=Localizes primarily to the
CC cytoplasm. Upon certain ligand binding, a conformation change exposes a
CC nuclear localization motif and the protein is transported into nucleus
CC (By similarity). Secreted by astrocytes, but not by neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000250|UniProtKB:Q05816}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands 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; U13253; AAA86680.1; -; mRNA.
DR EMBL; S69874; AAB30574.1; -; mRNA.
DR EMBL; S83247; AAB46848.1; -; mRNA.
DR PIR; JC2201; JC2201.
DR RefSeq; NP_665885.1; NM_145878.1.
DR AlphaFoldDB; P55053; -.
DR SMR; P55053; -.
DR STRING; 10116.ENSRNOP00000064809; -.
DR iPTMnet; P55053; -.
DR PhosphoSitePlus; P55053; -.
DR jPOST; P55053; -.
DR PaxDb; P55053; -.
DR PRIDE; P55053; -.
DR GeneID; 140868; -.
DR KEGG; rno:140868; -.
DR CTD; 2171; -.
DR RGD; 70997; Fabp5.
DR VEuPathDB; HostDB:ENSRNOG00000049075; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P55053; -.
DR OMA; MGGMAKP; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P55053; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P55053; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000049075; Expressed in esophagus and 20 other tissues.
DR Genevisible; P55053; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:RGD.
DR GO; GO:0001972; F:retinoic acid binding; ISO:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:RGD.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISO:RGD.
DR GO; GO:0031392; P:regulation of prostaglandin biosynthetic process; ISO:RGD.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 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; Disulfide bond;
KW Lipid transport; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT CHAIN 2..135
FT /note="Fatty acid-binding protein 5"
FT /id="PRO_0000067379"
FT MOTIF 24..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 43
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 109
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 129..131
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 131
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 131
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT DISULFID 120..127
FT /evidence="ECO:0000269|PubMed:10965032"
FT CONFLICT 49
FT /note="G -> N (in Ref. 1; AAA86680)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> N (in Ref. 3; AAB46848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 135 AA; 15059 MW; 978392433DF54358 CRC64;
MASLKDLEGK WRLVESHGFE DYMKELGVGL ALRKMGAMAK PDCIITLDGN NLTVKTESTV
KTTVFSCTLG EKFDETTADG RKTETVCTFT DGALVQHQKW EGKESTITRK LKDGKMVVEC
VMNNAICTRV YEKVQ
