ID   FABP1_CAEEL             Reviewed;         159 AA.
AC   Q20223;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Fatty acid-binding protein homolog 1;
DE   AltName: Full=Lipid-binding protein 1;
DE   Flags: Precursor;
GN   Name=lbp-1; ORFNames=F40F4.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10693745; DOI=10.1016/s0166-6851(99)00179-6;
RA   Plenefisch J., Xiao H., Mei B., Geng J., Komuniecki P.R., Komuniecki R.;
RT   "Secretion of a novel class of iFABPs in nematodes: coordinate use of the
RT   Ascaris/Caenorhabditis model systems.";
RL   Mol. Biochem. Parasitol. 105:223-236(2000).
CC   -!- FUNCTION: May play a role in sequestering potentially toxic fatty acids
CC       and their peroxidation products, or it may be involved in the
CC       maintenance of the impermeable lipid layer of the eggshell.
CC       {ECO:0000269|PubMed:10693745}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10693745}. Note=From
CC       the hypodermis into the perivitelline fluid of the developing embryo
CC       prior to hatching.
CC   -!- TISSUE SPECIFICITY: First detected in hypodermal precursor cells at the
CC       time of gastrulation. From the two-fold stage through to three-fold
CC       stages, expression is localized exclusively to hyp-7 but disappears in
CC       newly hatched L1s and subsequent developmental stages. Expression from
CC       L1 to adult stages is found in a single neuron in the ventral cord with
CC       a process into the nerve ring. {ECO:0000269|PubMed:10693745}.
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; FO081243; CCD70142.1; -; Genomic_DNA.
DR   PIR; T16309; T16309.
DR   RefSeq; NP_508557.1; NM_076156.5.
DR   AlphaFoldDB; Q20223; -.
DR   SMR; Q20223; -.
DR   BioGRID; 45557; 17.
DR   DIP; DIP-24433N; -.
DR   IntAct; Q20223; 2.
DR   STRING; 6239.F40F4.3.1; -.
DR   World-2DPAGE; 0011:Q20223; -.
DR   EPD; Q20223; -.
DR   PaxDb; Q20223; -.
DR   PeptideAtlas; Q20223; -.
DR   EnsemblMetazoa; F40F4.3.1; F40F4.3.1; WBGene00002253.
DR   GeneID; 180616; -.
DR   KEGG; cel:CELE_F40F4.3; -.
DR   UCSC; F40F4.3.1; c. elegans.
DR   CTD; 180616; -.
DR   WormBase; F40F4.3; CE04533; WBGene00002253; lbp-1.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00390000007345; -.
DR   HOGENOM; CLU_113772_2_1_1; -.
DR   InParanoid; Q20223; -.
DR   OMA; KFYGKFD; -.
DR   OrthoDB; 1556612at2759; -.
DR   PhylomeDB; Q20223; -.
DR   PRO; PR:Q20223; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00002253; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR040094; Lbp1-4.
DR   PANTHER; PTHR22725; PTHR22725; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   2: Evidence at transcript level;
KW   Lipid-binding; Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..159
FT                   /note="Fatty acid-binding protein homolog 1"
FT                   /id="PRO_0000008737"
SQ   SEQUENCE   159 AA;  18284 MW;  6676E64C581458CF CRC64;
     MCAKIALLLV LVGAASAAVL PDKFYGTFDL DHSENFDEYL TAKGYGWFTR KLVTFATFKK
     VFTKTSNKNL FDYSNLTSKK DVHYKNVQLG KAFQGEGLDS TKHEITFTLK DGHLFEHHKP
     LEGGDAKEET YEYLFDKEFL LVRMSFNGVE GRRFYKRLP