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   27-MAR-2024, entry version 187.
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.1; -.
DR   GlyCosmos; P20792; 4 sites, No reported glycans.
DR   EPD; P20792; -.
DR   PaxDb; 6239-F29C4-1a; -.
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   AGR; WB:WBGene00000897; -.
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; 3900892at2759; -.
DR   PhylomeDB; P20792; -.
DR   BRENDA; 2.7.10.2; 1045.
DR   Reactome; R-CEL-1502540; Signaling by Activin.
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 cell types or tissues.
DR   GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:WormBase.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
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 nematode pharyngeal pumping; IMP:WormBase.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:WormBase.
DR   CDD; cd14056; STKc_TGFbR_I; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF71; RECEPTOR PROTEIN SERINE_THREONINE KINASE; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
FT                   protein-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
//