NLTP2_CAEEL
ID NLTP2_CAEEL Reviewed; 412 AA.
AC G5EDP2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Non-specific lipid-transfer protein-like 2 {ECO:0000250|UniProtKB:P22307};
DE Short=NSL-TP2 {ECO:0000250|UniProtKB:P22307};
DE EC=2.3.1.176 {ECO:0000269|PubMed:9151950};
DE AltName: Full=3-keto-acyl-CoA thiolase {ECO:0000303|PubMed:9151950};
DE AltName: Full=Abnormal dauer formation protein 22 {ECO:0000312|WormBase:Y57A10C.6};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000305};
DE AltName: Full=Protein P-44 {ECO:0000303|PubMed:9151950};
GN Name=daf-22 {ECO:0000312|WormBase:Y57A10C.6};
GN ORFNames=Y57A10C.6 {ECO:0000312|WormBase:Y57A10C.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|EMBL:BAA20377.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:BAA20377.1};
RX PubMed=9151950; DOI=10.1111/j.1432-1033.1997.t01-1-00252.x;
RA Bun-ya M., Maebuchi M., Hashimoto T., Yokota S., Kamiryo T.;
RT "A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis
RT elegans which is similar to sterol carrier protein x but lacks the sequence
RT of sterol carrier protein 2.";
RL Eur. J. Biochem. 245:252-259(1997).
RN [2] {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 [3] {ECO:0000305}
RP CHARACTERIZATION OF M130 MUTANT.
RX PubMed=3859733; DOI=10.1007/bf00332953;
RA Golden J.W., Riddle D.L.;
RT "A gene affecting production of the Caenorhabditis elegans dauer-inducing
RT pheromone.";
RL Mol. Gen. Genet. 198:534-536(1985).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19496754; DOI=10.1042/bj20090513;
RA Joo H.J., Yim Y.H., Jeong P.Y., Jin Y.X., Lee J.E., Kim H., Jeong S.K.,
RA Chitwood D.J., Paik Y.K.;
RT "Caenorhabditis elegans utilizes dauer pheromone biosynthesis to dispose of
RT toxic peroxisomal fatty acids for cellular homoeostasis.";
RL Biochem. J. 422:61-71(2009).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-351.
RX PubMed=19174521; DOI=10.1073/pnas.0810338106;
RA Butcher R.A., Ragains J.R., Li W., Ruvkun G., Clardy J., Mak H.Y.;
RT "Biosynthesis of the Caenorhabditis elegans dauer pheromone.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1875-1879(2009).
CC -!- FUNCTION: Catalyzes the thiolytic cleavage of 3-ketoacyl-CoA with 8-16
CC carbon residues in the acyl group using a ping-pong mechanism whereby
CC binding to 3-ketooctanoyl-CoA results in the release of acetyl-CoA and
CC the subsequent addition of CoA produces 3-ketohexanohyl-CoA
CC (PubMed:9151950). Involved in the biosynthesis of the dauer pheromone
CC by providing short chains of fatty acid that are attached to the
CC ascarylose sugars of the pheromone (PubMed:19496754, PubMed:19174521).
CC {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754,
CC ECO:0000269|PubMed:9151950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-
CC trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA;
CC Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176;
CC Evidence={ECO:0000269|PubMed:9151950};
CC -!- ACTIVITY REGULATION: Inhibited by acetyl-CoA.
CC {ECO:0000269|PubMed:9151950}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for 3-ketooctanoyl-CoA (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9151950};
CC KM=0.7 uM for CoA (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:9151950};
CC Vmax=0.1 mmol/min/mg enzyme {ECO:0000269|PubMed:9151950};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19174521,
CC ECO:0000269|PubMed:19496754}. Note=Punctate localization in the
CC cytoplasm. {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, hypodermis and body-wall
CC muscle. {ECO:0000269|PubMed:19174521}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all larval stages with levels peaking
CC at the L3 larval stage and decreasing in the adult.
CC {ECO:0000269|PubMed:19496754}.
CC -!- DISRUPTION PHENOTYPE: In short-term culture, loss of the capacity to
CC enter the dauer stage which is associated with a loss in the production
CC of the dauer pheromone. In long-term culture, the capacity to induce
CC the dauer stage is restored and is associated with the accumulation of
CC long fatty acid chain ascarosides (PubMed:19174521). Intestinal
CC expression of daf-22 restores the production of the pheromone
CC (PubMed:19174521). Partial dauer phenotype in only half of mutants when
CC the dauer pheromone is added exogenously (PubMed:19496754). In
CC addition, mutants accumulate large fat granules in the intestine, have
CC a decreased growth rate resulting in smaller adults and have a
CC substantial reduction in brood size (PubMed:19496754).
CC {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; D86473; BAA20377.1; -; mRNA.
DR EMBL; AL023847; CAA19548.1; -; Genomic_DNA.
DR PIR; T27202; T27202.
DR RefSeq; NP_496639.1; NM_064238.3.
DR AlphaFoldDB; G5EDP2; -.
DR SMR; G5EDP2; -.
DR IntAct; G5EDP2; 1.
DR STRING; 6239.Y57A10C.6; -.
DR EPD; G5EDP2; -.
DR PaxDb; G5EDP2; -.
DR PeptideAtlas; G5EDP2; -.
DR EnsemblMetazoa; Y57A10C.6.1; Y57A10C.6.1; WBGene00013284.
DR GeneID; 174881; -.
DR KEGG; cel:CELE_Y57A10C.6; -.
DR CTD; 174881; -.
DR WormBase; Y57A10C.6; CE18418; WBGene00013284; daf-22.
DR eggNOG; KOG1406; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_035425_0_0_1; -.
DR InParanoid; G5EDP2; -.
DR OMA; PSLYAMM; -.
DR OrthoDB; 661265at2759; -.
DR PhylomeDB; G5EDP2; -.
DR Reactome; R-CEL-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-CEL-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-CEL-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR SABIO-RK; G5EDP2; -.
DR PRO; PR:G5EDP2; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013284; Expressed in larva and 3 other tissues.
DR GO; GO:0005777; C:peroxisome; IDA:WormBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IMP:UniProtKB.
DR GO; GO:1904070; P:ascaroside biosynthetic process; IMP:UniProtKB.
DR GO; GO:0043053; P:dauer entry; IMP:UniProtKB.
DR GO; GO:0043054; P:dauer exit; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; IMP:UniProtKB.
DR GO; GO:0042811; P:pheromone biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; IBA:GO_Central.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IMP:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 1: Evidence at protein level;
KW Lipid transport; Lipid-binding; Peroxisome; Reference proteome;
KW Transferase; Transport.
FT CHAIN 1..412
FT /note="Non-specific lipid-transfer protein-like 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431921"
FT MOTIF 410..412
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MUTAGEN 351
FT /note="G->R: In m130; loss of dauer larvae formation and
FT dauer pheromone production."
FT /evidence="ECO:0000269|PubMed:19174521,
FT ECO:0000269|PubMed:3859733"
SQ SEQUENCE 412 AA; 44386 MW; 6B9DA9BA18ABF446 CRC64;
MTPTKPKVYI VGVGMTKFCK PGSVPGWDYP DMVKEAVTTA LDDCKMKYSD IQQATVGYLF
GGTCCGQRAL YEVGLTGIPI FNVNNACASG SSGLFLGKQI IESGNSDVVL CAGFERMAPG
SLENLAAPID DRALSVDKHI SVMSETYGLE PAPMTAQMFG NAAKEHMEKY GSKREHYAKI
AYKNHLHSVH NPKSQFTKEF SLDQVINARK IYDFMGLLEC SPTSDGAAAA VLVSEKFLEK
NPRLKAQAVE IVGLKLGTDE PSVFAENSNI KMIGFDMIQK LAKQLWAETK LTPNDVQVIE
LHDCFAPNEL ITYEAIGLCP VGQGHHIVDR NDNTYGGKWV INPSGGLISK GHPIGATGVA
QAVELSNQLR GKCGKRQVPN CKVAMQHNIG IGGAGVVGLY RLGFPGAAQS KI
