ID A0A2G5U0K9_9PELO Unreviewed; 526 AA.
AC A0A2G5U0K9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=Cnig_chr_IV.g13190 {ECO:0000313|EMBL:PIC33079.1};
GN ORFNames=B9Z55_013190 {ECO:0000313|EMBL:PIC33079.1};
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:PIC33079.1, 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: 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:PIC33079.1}.
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DR EMBL; PDUG01000004; PIC33079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5U0K9; -.
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; 2.10.25.10; Laminin; 1.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR039178; Lag2.
DR InterPro; IPR006583; PAN-3_domain.
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 Pfam; PF08277; PAN_3; 1.
DR SMART; SM00605; CW; 1.
DR SMART; SM00051; DSL; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|RuleBase:RU280815};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00377}; EGF-like domain {ECO:0000256|RuleBase:RU280815};
KW 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, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU280815};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..526
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013869001"
FT DOMAIN 395..439
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DISULFID 397..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 410..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 430..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
SQ SEQUENCE 526 AA; 59837 MW; 8C88A0CBA5E364CA CRC64;
MKLALFLYCS IIFIESVKAD LIMVEVYGQP TTTKKVYSSN GKSWNECMAE CYYAQSCVAA
WKNGSTCYTF DYWLMGPITQ TKEINESIVA FKVENKGGEC PSGINPPTFG NKNATGSLYI
DSDPKIAPVW VHYNIYYTKG SWKLNYKVDR ICGEYEYDGF VSHADSTVTC SFVWYNENTG
GFTYSEMKET CDEYSYGMAG FKYKEDVAMF EAKKYLVKIK DTRAYVRVDG IRTAACQKTP
KTAYCMSEKD PTGRMTPSPF PGLFFYIRTP TMSPKLHISL LFLLLLIPNA QSSGYLEIRL
KSPFLLNATV TITEDIYFPT NKRVFNVPLV PDHTRILTNV PVKFHRPGTV LINSGPVDKF
GLHFATIRSD RWNTKQMIIA PDEMKLPFTG FRIDVKCDRN WHGPYCDKFC NDNHAKIINR
RCTHNATLGC PLMLSGPNCD VPLLQTESTC PCVNHGYCVS EFLNPLDTVD RSICECGVGF
EGEHCEEKEY DYADAIQFGM HGGPEKVFTE FFERSSVDNE LRYLYH
//
