FABP2_CAEEL
ID FABP2_CAEEL Reviewed; 161 AA.
AC Q20224;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fatty acid-binding protein homolog 2;
DE AltName: Full=Lipid-binding protein 2;
DE Flags: Precursor;
GN Name=lbp-2; ORFNames=F40F4.2;
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 PROTEIN SEQUENCE OF 20-37.
RC STRAIN=Bristol N2;
RX PubMed=9150941; DOI=10.1002/elps.1150180337;
RA Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT and identification of protein spots by microsequencing.";
RL Electrophoresis 18:557-562(1997).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 -!- 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; CCD70141.1; -; Genomic_DNA.
DR PIR; T16310; T16310.
DR RefSeq; NP_508558.1; NM_076157.7.
DR AlphaFoldDB; Q20224; -.
DR SMR; Q20224; -.
DR BioGRID; 45558; 42.
DR IntAct; Q20224; 1.
DR STRING; 6239.F40F4.2.2; -.
DR EPD; Q20224; -.
DR PaxDb; Q20224; -.
DR PeptideAtlas; Q20224; -.
DR EnsemblMetazoa; F40F4.2.1; F40F4.2.1; WBGene00002254.
DR EnsemblMetazoa; F40F4.2.2; F40F4.2.2; WBGene00002254.
DR GeneID; 180617; -.
DR KEGG; cel:CELE_F40F4.2; -.
DR UCSC; F40F4.2.1; c. elegans.
DR CTD; 180617; -.
DR WormBase; F40F4.2; CE04532; WBGene00002254; lbp-2.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00390000007345; -.
DR HOGENOM; CLU_113772_2_1_1; -.
DR InParanoid; Q20224; -.
DR OMA; RFHMEED; -.
DR OrthoDB; 1520038at2759; -.
DR PhylomeDB; Q20224; -.
DR PRO; PR:Q20224; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002254; Expressed in adult organism and 4 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 1: Evidence at protein level;
KW Direct protein sequencing; Lipid-binding; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:9150941"
FT CHAIN 20..161
FT /note="Fatty acid-binding protein homolog 2"
FT /id="PRO_0000008738"
SQ SEQUENCE 161 AA; 18843 MW; 0A00AAD416C69879 CRC64;
MSSKFLILLA FCGATLVAAE QLPEKFYGTF DLDHSENFDE YLTAKGYGWF TRKLVTFATF
KKVFAKNANK NLFDYSNLTS KKDVFYKNVQ IGSKFEGEGL DNTKHEVTFT LKDGHLFEHH
KPLEEGESKE ETYEYYFDGD FLIQKMSFNN IEGRRFYKRL P