ID A0A2G5UBX6_9PELO Unreviewed; 208 AA.
AC A0A2G5UBX6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=Cnig_chr_IV.g15829 {ECO:0000313|EMBL:PIC37058.1};
GN ORFNames=B9Z55_015829 {ECO:0000313|EMBL:PIC37058.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC37058.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. {ECO:0000256|RuleBase:RU280815}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU280815}; Single-
CC pass type I membrane protein {ECO:0000256|RuleBase:RU280815}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC37058.1}.
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DR EMBL; PDUG01000004; PIC37058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UBX6; -.
DR Proteomes; UP000230233; Chromosome iv.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005112; F:Notch binding; IEA:InterPro.
DR GO; GO:0001708; P:cell fate specification; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR039178; Lag2.
DR PANTHER; PTHR22669:SF1; DELTA-LIKE PROTEIN DSL-1; 1.
DR PANTHER; PTHR22669; DELTA/SERRATE/LAG-2 DOMAIN PROTEIN; 1.
DR Pfam; PF01414; DSL; 1.
DR SMART; SM00051; DSL; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|RuleBase:RU280815};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW ECO:0000256|RuleBase:RU280815}; Membrane {ECO:0000256|RuleBase:RU280815};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|RuleBase:RU280815};
KW Transmembrane {ECO:0000256|RuleBase:RU280815};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815}.
FT DOMAIN 69..113
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 120..160
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 71..80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 84..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 104..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 150..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 208 AA; 23855 MW; 2E28FF6C3D484F6C CRC64;
MPLVPDRTQI LTNLPAKFHR PGTVLINTGP FNKFGLDYAT FKFDRYNTMK KDTVPIYLVL
PFTGLKISFL CDRNWHGPYC DKFCNQDHAD IINRRCTHNG TLGCPKDFHG PNCDIPLDQS
SDQCQCSNGG YCISEFQNPE DTVDRLICEC PVGFEGDHCE TKQHDYELNM KKKRYGTPGK
QALLEQFERD SAVINELHPQ FDPHVHKN
//
