DRL1_CAEEL
ID DRL1_CAEEL Reviewed; 589 AA.
AC Q86ME2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein drl-1 {ECO:0000305};
DE AltName: Full=Dietary restriction-like protein 1 {ECO:0000312|WormBase:F18F11.5};
GN Name=drl-1 {ECO:0000312|WormBase:F18F11.5};
GN Synonyms=mekk-3 {ECO:0000312|WormBase:F18F11.5};
GN ORFNames=F18F11.5 {ECO:0000312|WormBase:F18F11.5};
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24655420; DOI=10.1111/acel.12218;
RA Chamoli M., Singh A., Malik Y., Mukhopadhyay A.;
RT "A novel kinase regulates dietary restriction-mediated longevity in
RT Caenorhabditis elegans.";
RL Aging Cell 13:641-655(2014).
CC -!- FUNCTION: Negatively regulates lifespan and health span probably by
CC participating in nutrient sensing. {ECO:0000269|PubMed:24655420}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval and body wall muscles,
CC hypodermis, seam cells and tissues next to pharynx and anus.
CC {ECO:0000269|PubMed:24655420}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase in
CC lifespan of about 60 percent compared to wild type but only when done
CC at an early larval stage. Lifespan increase is associated with a
CC decrease in the accumulation of the age pigment lipofuscin, a delayed
CC age-onset nuclear membrane disintegration in muscles and loss of
CC mobility. In addition, causes an increase in lipid catabolism resulting
CC in fewer fat droplets in intestinal cells and hypodermis and lower
CC triglycerides levels. Transcriptional up-regulation of genes involved
CC in fatty acid degradation and in xenobiotic detoxification and decrease
CC in cellular oxygen reactive species (ROS) production. Low brood size,
CC longer reproductive span, increased autophagosome formation in seam
CC cells and smaller body size. Normal pharyngeal pumping and feeding
CC rate. RNAi-mediated knockdown in muscles or hypodermis causes a
CC moderate increase in lifespan. {ECO:0000269|PubMed:24655420}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Although the residues involved in the catalytic activity are
CC absent, suggesting that the kinase is inactive, some kinase activity
CC has been detected. {ECO:0000305|PubMed:24655420}.
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DR EMBL; BX284604; CCD69674.2; -; Genomic_DNA.
DR RefSeq; NP_001023134.2; NM_001027963.3.
DR AlphaFoldDB; Q86ME2; -.
DR SMR; Q86ME2; -.
DR STRING; 6239.F18F11.5; -.
DR PaxDb; Q86ME2; -.
DR EnsemblMetazoa; F18F11.5.1; F18F11.5.1; WBGene00017578.
DR GeneID; 3565236; -.
DR KEGG; cel:CELE_F18F11.5; -.
DR UCSC; F18F11.5; c. elegans.
DR CTD; 3565236; -.
DR WormBase; F18F11.5; CE48587; WBGene00017578; drl-1.
DR eggNOG; KOG0198; Eukaryota.
DR GeneTree; ENSGT00940000160383; -.
DR HOGENOM; CLU_032945_0_0_1; -.
DR InParanoid; Q86ME2; -.
DR OMA; NGIQIAC; -.
DR OrthoDB; 789401at2759; -.
DR PRO; PR:Q86ME2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017578; Expressed in adult organism and 2 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="Protein drl-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435334"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 97..373
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 66851 MW; 035CB51F454CACC8 CRC64;
MHSEEKYLHI PNNTKYPEII VEEEEEDPSE EERSELSETD DVATPLRPSD TFPFKRRNSP
CSIKMSEEHL KRLREIACPS PTPTQCSTVS KHEFQNWRIN EDVMKDMMHI GTICERENVC
KTSKYVYTAT MASYTVTEWK LKEGNTPDEI EKISRTIEDL CQLRHKRLAP MYGYHWRLET
ELMVFRAHVP SGTVADLVKV SAIPQETAVR YIVHVIDALA YLHERKHVHG KLNASNLLLT
ISNDILLADP FIEGLPSAQK RRALLASPPE AFRSLESYPC LTPSSDIWSV GCVLVTMLTR
YPPFLEHYMH FHGESLHREL VSEWCTRRQL IYSSQTLIPS ASKEICELID QIFNVDPENR
PSAQNLLESH GSKSRKASLR NSLASLTTAK EPDPPKPIDD FYVEREDDEE HRKIEELREL
AERGNNEGGF IPFIRWYMSR ILIFSVLLVK WIGMVLCAAL SLAAVAGGVF FAIFLIYNGI
QIACQCSLNE GFVVLIALIL LPIIILLTTL CCNNSLDRYH ADVESGKVEK SRFVMKTPEK
DVIVGGYILV EGSPDHDKPA EVPRKLGISE GLQSTMGNTF LGYGVDKIA
