FABP8_CAEEL
ID FABP8_CAEEL Reviewed; 137 AA.
AC O02324;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fatty acid-binding protein homolog 8 {ECO:0000305};
GN Name=lbp-8 {ECO:0000312|WormBase:T22G5.6};
GN ORFNames=T22G5.6 {ECO:0000312|WormBase:T22G5.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25554789; DOI=10.1126/science.1258857;
RA Folick A., Oakley H.D., Yu Y., Armstrong E.H., Kumari M., Sanor L.,
RA Moore D.D., Ortlund E.A., Zechner R., Wang M.C.;
RT "Aging. Lysosomal signaling molecules regulate longevity in Caenorhabditis
RT elegans.";
RL Science 347:83-86(2015).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=30713071; DOI=10.1016/j.devcel.2018.12.022;
RA Ramachandran P.V., Savini M., Folick A.K., Hu K., Masand R., Graham B.H.,
RA Wang M.C.;
RT "Lysosomal Signaling Promotes Longevity by Adjusting Mitochondrial
RT Activity.";
RL Dev. Cell 48:685-696(2019).
RN [4] {ECO:0007744|PDB:6C1Z}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=31292465; DOI=10.1038/s41598-019-46230-8;
RA Tillman M.C., Khadka M., Duffy J., Wang M.C., Ortlund E.A.;
RT "Structural characterization of life-extending Caenorhabditis elegans Lipid
RT Binding Protein 8.";
RL Sci. Rep. 9:9966-9966(2019).
CC -!- FUNCTION: Lysosomal lipid chaperone which binds to a wide range of
CC unsaturated fatty acids, including high affinity binding to oleic acid
CC and oleoylethanolamide, to transport them into the nucleus
CC (PubMed:31292465, PubMed:25554789). As part of a lysosome-to-nucleus
CC retrograde lipid signaling pathway, translocates into the nucleus where
CC it activates the transcription of genes promoting longevity and
CC activation of mitochondrial beta oxidation (PubMed:30713071,
CC PubMed:25554789). {ECO:0000269|PubMed:25554789,
CC ECO:0000269|PubMed:30713071, ECO:0000269|PubMed:31292465}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31292465}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:25554789}. Nucleus
CC {ECO:0000269|PubMed:25554789}.
CC -!- TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:25554789}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000255|RuleBase:RU003696}.
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DR EMBL; BX284605; CAB03391.2; -; Genomic_DNA.
DR PIR; T25127; T25127.
DR RefSeq; NP_506444.2; NM_074043.4.
DR PDB; 6C1Z; X-ray; 1.30 A; A=1-137.
DR PDBsum; 6C1Z; -.
DR AlphaFoldDB; O02324; -.
DR SMR; O02324; -.
DR STRING; 6239.T22G5.6; -.
DR PaxDb; O02324; -.
DR PeptideAtlas; O02324; -.
DR EnsemblMetazoa; T22G5.6.1; T22G5.6.1; WBGene00002260.
DR GeneID; 188761; -.
DR KEGG; cel:CELE_T22G5.6; -.
DR UCSC; T22G5.6; c. elegans.
DR CTD; 188761; -.
DR WormBase; T22G5.6; CE41159; WBGene00002260; lbp-8.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00970000196311; -.
DR HOGENOM; CLU_113772_0_1_1; -.
DR InParanoid; O02324; -.
DR OMA; ICRREFV; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; O02324; -.
DR Reactome; R-CEL-159418; Recycling of bile acids and salts.
DR Reactome; R-CEL-163560; Triglyceride catabolism.
DR Reactome; R-CEL-189483; Heme degradation.
DR Reactome; R-CEL-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR Reactome; R-CEL-5365859; RA biosynthesis pathway.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-975634; Retinoid metabolism and transport.
DR PRO; PR:O02324; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002260; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; TAS:WormBase.
DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:UniProtKB.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:UniProtKB.
DR GO; GO:0070538; F:oleic acid binding; IDA:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; TAS:WormBase.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:UniProtKB.
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 3D-structure; Lipid-binding; Lysosome; Nucleus; Reference proteome;
KW Transport.
FT CHAIN 1..137
FT /note="Fatty acid-binding protein homolog 8"
FT /id="PRO_0000450342"
FT MOTIF 24..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:6C1Z"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:6C1Z"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6C1Z"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6C1Z"
SQ SEQUENCE 137 AA; 16092 MW; EFF96E41019F5551 CRC64;
MVSMKEFIGR WKLVHSENFE EYLKEIGVGL LIRKAASLTS PTLEIKLDGD TWHFNQYSTF
KNNKLAFKIR EKFVEIAPDE RSYNTLVTFE NGKFISHQDK IKENHHSSVF TTWLENGKLL
QTYQSGSVIC RREFVKE
