FABP3_CAEEL
ID FABP3_CAEEL Reviewed; 165 AA.
AC Q20222;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Fatty acid-binding protein homolog 3;
DE AltName: Full=Lipid-binding protein 3;
DE Flags: Precursor;
GN Name=lbp-3; ORFNames=F40F4.4;
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 muscle into the perienteric fluid.
CC -!- TISSUE SPECIFICITY: Expressed in presumptive hypodermal cells by the
CC comma stage and in posterior body wall muscle cells by the two-fold
CC stage. From L1 to adult stages, expression continues in body wall
CC muscle cells adjacent to the pseudocoelom, while hypodermal expression
CC is extinguished. {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; CCD70143.1; -; Genomic_DNA.
DR PIR; T16308; T16308.
DR RefSeq; NP_001041249.1; NM_001047784.4.
DR AlphaFoldDB; Q20222; -.
DR SMR; Q20222; -.
DR STRING; 6239.F40F4.4a; -.
DR EPD; Q20222; -.
DR PaxDb; Q20222; -.
DR PeptideAtlas; Q20222; -.
DR EnsemblMetazoa; F40F4.4a.1; F40F4.4a.1; WBGene00002255.
DR UCSC; F40F4.4a; c. elegans.
DR WormBase; F40F4.4a; CE30130; WBGene00002255; lbp-3.
DR eggNOG; KOG4015; Eukaryota.
DR InParanoid; Q20222; -.
DR OMA; TCRRWFK; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q20222; -.
DR PRO; PR:Q20222; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002255; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q20222; baseline and differential.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..165
FT /note="Fatty acid-binding protein homolog 3"
FT /id="PRO_0000008739"
SQ SEQUENCE 165 AA; 19099 MW; 73A845F85D0923D9 CRC64;
MNLYLTLFSF CFLAIMAEAA SEIPEKFFGK YDLDRSENFD EFLAAKGVSW FVRQMIKLAK
VSKVLAKNET PGKYNMENLT SKKNTLYHGW ELGKTFEAEG LDGVAHKITF SFKDGVLSEH
HIRLNDPEHS AETYYYTIEN DQLVMKMVNN GITCRRWFKR STGKK
