DAF1_CAEEL
ID DAF1_CAEEL Reviewed; 669 AA.
AC P20792;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cell surface receptor daf-1;
DE EC=2.7.11.30;
DE AltName: Full=Abnormal dauer formation protein 1;
DE Flags: Precursor;
GN Name=daf-1; ORFNames=F29C4.1;
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 [GENOMIC DNA] (ISOFORM A).
RX PubMed=2160853; DOI=10.1016/0092-8674(90)90475-t;
RA Georgi L.L., Albert P.S., Riddle D.L.;
RT "daf-1, a C. elegans gene controlling dauer larva development, encodes a
RT novel receptor protein kinase.";
RL Cell 61:635-645(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP OF GLY-70; CYS-90; GLU-105 AND GLY-110.
RX PubMed=10887089; DOI=10.1242/dev.127.15.3337;
RA Gunther C.V., Georgi L.L., Riddle D.L.;
RT "A Caenorhabditis elegans type I TGF beta receptor can function in the
RT absence of type II kinase to promote larval development.";
RL Development 127:3337-3347(2000).
RN [4]
RP FUNCTION.
RX PubMed=18316030; DOI=10.1016/j.cmet.2008.01.005;
RA You Y.J., Kim J., Raizen D.M., Avery L.;
RT "Insulin, cGMP, and TGF-beta signals regulate food intake and quiescence in
RT C. elegans: a model for satiety.";
RL Cell Metab. 7:249-257(2008).
RN [5]
RP FUNCTION.
RX PubMed=18524955; DOI=10.1073/pnas.0707469105;
RA Hallem E.A., Sternberg P.W.;
RT "Acute carbon dioxide avoidance in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8038-8043(2008).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-400.
RX PubMed=20713521; DOI=10.1101/gad.1932610;
RA Lesch B.J., Bargmann C.I.;
RT "The homeodomain protein hmbx-1 maintains asymmetric gene expression in
RT adult C. elegans olfactory neurons.";
RL Genes Dev. 24:1802-1815(2010).
CC -!- FUNCTION: Probably involved in a TGF-beta pathway (PubMed:10887089).
CC May be a receptor for TGF-beta-like ligand daf-7 (PubMed:10887089).
CC Controls the decision of whether or not larvae enter a developmentally
CC arrested state, known as dauer, in response to environmental conditions
CC (PubMed:10887089). Involved in regulating entry into quiescence
CC triggered by satiety (PubMed:18316030). Involved in sensitivity to CO2
CC levels (PubMed:18524955). In AWC neurons, acts to promote expression of
CC srsx-3, a member of the GPCR family (PubMed:20713521).
CC {ECO:0000269|PubMed:10887089, ECO:0000269|PubMed:18316030,
CC ECO:0000269|PubMed:18524955, ECO:0000269|PubMed:20713521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- SUBUNIT: May interact with daf-4 to regulate dauer larva development.
CC {ECO:0000269|PubMed:10887089}.
CC -!- INTERACTION:
CC P20792; Q18688: daf-21; NbExp=2; IntAct=EBI-360236, EBI-313329;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P20792-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P20792-2; Sequence=VSP_007948;
CC -!- TISSUE SPECIFICITY: Head and ventral nerve cord from embryos to adults.
CC Expressed in many sensory neurons. Subset of head neurons show
CC coexpression with daf-4 when dauer/nondauer decision is made. Also
CC expressed in non-neuronal cells: membraneous sheath surrounding the
CC distal end of the intestine and in the distal tip cell of the gonad.
CC {ECO:0000269|PubMed:10887089}.
CC -!- DEVELOPMENTAL STAGE: All stages. {ECO:0000269|PubMed:10887089}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; M32877; AAA28001.1; -; Genomic_DNA.
DR EMBL; FO080227; CCD62175.1; -; Genomic_DNA.
DR EMBL; FO080227; CCD62176.1; -; Genomic_DNA.
DR PIR; A35103; A35103.
DR RefSeq; NP_001023159.1; NM_001027988.4. [P20792-1]
DR RefSeq; NP_001023160.1; NM_001027989.3. [P20792-2]
DR AlphaFoldDB; P20792; -.
DR SMR; P20792; -.
DR BioGRID; 41992; 3.
DR IntAct; P20792; 1.
DR STRING; 6239.F29C4.1a; -.
DR EPD; P20792; -.
DR PaxDb; P20792; -.
DR PeptideAtlas; P20792; -.
DR EnsemblMetazoa; F29C4.1a.1; F29C4.1a.1; WBGene00000897. [P20792-1]
DR EnsemblMetazoa; F29C4.1b.1; F29C4.1b.1; WBGene00000897. [P20792-2]
DR GeneID; 176829; -.
DR KEGG; cel:CELE_F29C4.1; -.
DR UCSC; F29C4.1a; c. elegans. [P20792-1]
DR CTD; 176829; -.
DR WormBase; F29C4.1a; CE17719; WBGene00000897; daf-1. [P20792-1]
DR WormBase; F29C4.1b; CE31492; WBGene00000897; daf-1. [P20792-2]
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000168401; -.
DR InParanoid; P20792; -.
DR OMA; MWETLCR; -.
DR OrthoDB; 1100558at2759; -.
DR PhylomeDB; P20792; -.
DR BRENDA; 2.7.10.2; 1045.
DR Reactome; R-CEL-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-CEL-2173789; TGF-beta receptor signaling activates SMADs.
DR SignaLink; P20792; -.
DR PRO; PR:P20792; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000897; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0016361; F:activin receptor activity, type I; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISS:WormBase.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0043053; P:dauer entry; IGI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR GO; GO:0061067; P:negative regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0061065; P:regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:WormBase.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..669
FT /note="Cell surface receptor daf-1"
FT /id="PRO_0000024430"
FT TOPO_DOM 20..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 262..292
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 293..593
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 611..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 299..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 467
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007948"
FT MUTAGEN 70
FT /note="G->R: In allele p168; forms many dauer larvae."
FT /evidence="ECO:0000269|PubMed:10887089"
FT MUTAGEN 90
FT /note="C->Y: In allele m138; forms many dauer larvae."
FT /evidence="ECO:0000269|PubMed:10887089"
FT MUTAGEN 105
FT /note="E->A: In allele m122; forms many dauer larvae; when
FT associated with E-110."
FT /evidence="ECO:0000269|PubMed:10887089"
FT MUTAGEN 110
FT /note="G->E: In allele m122; forms many dauer larvae; when
FT associated with A-105."
FT /evidence="ECO:0000269|PubMed:10887089"
FT MUTAGEN 400
FT /note="G->E: In ky803; reduces expression of the G protein-
FT coupled receptor (GPCR) srsx-3 in the AWC neuron."
FT /evidence="ECO:0000269|PubMed:20713521"
SQ SEQUENCE 669 AA; 75006 MW; 8BDD86C67C8F2A6A CRC64;
MRIRHVVFCL LALVYGAETS DDDLDERTNI FIRDKLIPAL KLAEVTKVNF TRLHLCHCSR
EVGCNARTTG WVPGIEFLNE TDRSFYENTC YTDGSCYQSA RPSPEISHFG CMDEKSVTDE
TEFHDTAAKV CTNNTKDPHA TVWICCDKGN FCANETIIHL APGPQQSSTW LILTILALLT
FIVLLGIAIF LTRKSWEAKF DWYIRFKPKP GDPLRETENN VPMVTMGDGA GSSVPEVAPI
EQQGSTMSTS AGNSFPPGIM PNNMKDMLDV LEETSGSGMG PTTLHKLTIG GQIRLTGRVG
SGRFGNVSRG DYRGEAVAVK VFNALDEPAF HKETEIFETR MLRHPNVLRY IGSDRVDTGF
VTELWLVTEY HPSGSLHDFL LENTVNIETY YNLMRSTASG LAFLHNQIGG SKESNKPAMA
HRDIKSKNIM VKNDLTCAIG DLGLSLSKPE DAASDIIANE NYKCGTVRYL APEILNSTMQ
FTVFESYQCA DVYSFSLVMW ETLCRCEDGD VLPREAATVI PYIEWTDRDP QDAQMFDVVC
TRRLRPTENP LWKDHPEMKH IMEIIKTCWN GNPSARFTSY ICRKRMDERQ QLLLDKKAKA
VAQTAGVTVQ DRKILGPQKP KDESPANGAP RIVQKEIDRE DEQENWRETA KTPNGHISSN
DDSSRPLLG
