DSL1_CAEEL
ID DSL1_CAEEL Reviewed; 252 AA.
AC O45201;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Delta-like protein dsl-1 {ECO:0000305};
DE AltName: Full=DSL-domain containing protein dsl-1 {ECO:0000312|WormBase:W09G12.4};
DE Flags: Precursor;
GN Name=dsl-1 {ECO:0000312|WormBase:W09G12.4};
GN ORFNames=W09G12.4 {ECO:0000312|WormBase:W09G12.4};
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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14960273; DOI=10.1016/s1534-5807(04)00021-8;
RA Chen N., Greenwald I.;
RT "The lateral signal for LIN-12/Notch in C. elegans vulval development
RT comprises redundant secreted and transmembrane DSL proteins.";
RL Dev. Cell 6:183-192(2004).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LIN-12, AND DISRUPTION PHENOTYPE.
RX PubMed=18700817; DOI=10.1371/journal.pbio.0060196;
RA Komatsu H., Chao M.Y., Larkins-Ford J., Corkins M.E., Somers G.A.,
RA Tucey T., Dionne H.M., White J.Q., Wani K., Boxem M., Hart A.C.;
RT "OSM-11 facilitates LIN-12 Notch signaling during Caenorhabditis elegans
RT vulval development.";
RL PLoS Biol. 6:e196-e196(2008).
CC -!- FUNCTION: Probable secreted Notch ligand involved in the mediation of
CC Notch signaling (PubMed:14960273, PubMed:18700817). Involved in the
CC lin-12/Notch pathway-mediated signaling of cell fate in vulval
CC precursor cells (VPCs), acting redundantly with lag-2, apx-1 and osm-11
CC (PubMed:14960273, PubMed:18700817). May also be involved in glp-1/Notch
CC signaling (PubMed:14960273). {ECO:0000269|PubMed:14960273,
CC ECO:0000269|PubMed:18700817}.
CC -!- SUBUNIT: May interact with lin-12/Notch receptor.
CC {ECO:0000269|PubMed:18700817}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14960273}.
CC -!- DISRUPTION PHENOTYPE: Causes adjacent vulval precursor cells (VPCs) to
CC adopt altered cell fate; phenotype exacerbated when combined with
CC simultaneous RNAi-mediated knockdown of apx-1 and lag-2, and further
CC worsened on lin-15 mutant background (PubMed:14960273). Severe vulval
CC precursor cell (VPC) fate abnormalities, vulval defects and failure to
CC up-regulate lip-1 expression, on an osm-11 mutant background
CC (PubMed:18700817). {ECO:0000269|PubMed:14960273,
CC ECO:0000269|PubMed:18700817}.
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DR EMBL; BX284604; CCD74020.1; -; Genomic_DNA.
DR PIR; B88637; B88637.
DR RefSeq; NP_500054.1; NM_067653.1.
DR AlphaFoldDB; O45201; -.
DR DIP; DIP-46052N; -.
DR IntAct; O45201; 1.
DR STRING; 6239.W09G12.4; -.
DR PaxDb; O45201; -.
DR EnsemblMetazoa; W09G12.4.1; W09G12.4.1; WBGene00001103.
DR GeneID; 176939; -.
DR KEGG; cel:CELE_W09G12.4; -.
DR UCSC; W09G12.4; c. elegans.
DR CTD; 176939; -.
DR WormBase; W09G12.4; CE18343; WBGene00001103; dsl-1.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00970000195885; -.
DR HOGENOM; CLU_077229_0_0_1; -.
DR InParanoid; O45201; -.
DR OMA; RSERWNT; -.
DR OrthoDB; 1431525at2759; -.
DR PhylomeDB; O45201; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001103; Expressed in embryo and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005112; F:Notch binding; IPI:WormBase.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR039178; Lag2.
DR PANTHER; PTHR22669; PTHR22669; 1.
DR Pfam; PF01414; DSL; 1.
DR SMART; SM00051; DSL; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; EGF-like domain;
KW Notch signaling pathway; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..252
FT /note="Delta-like protein dsl-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004158656"
FT DOMAIN 120..164
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 169..210
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 122..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 135..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 155..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 173..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 175..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 199..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 252 AA; 28783 MW; 72F2276689A07008 CRC64;
MLKYLIFLAI LISVVHSNGY MTIRLKSAFP LNVTVEVAEE VYFPTNKRSF NLQLKPNRVG
FVSNIPVKFG RPGLVLVDCS PVEKFQIHRV TLRSIRWNTH VRSVASDNIF LPFTGFRYDI
KCNRYWHGLH CDHFCNDDFA RTINRRCTQN GTLGCLEGFH GPNCELPVPA DSCKCQNGGK
CVSSLENTWA QNGSLICECR LGHFEGKHCE KKSFNYFPKI EATTYATKDS HLARQFYNNS
RVPNELATLP RL
