ID A0A0R3QV96_9BILA Unreviewed; 200 AA.
AC A0A0R3QV96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN ORFNames=BTMF_LOCUS9682 {ECO:0000313|EMBL:VDO32767.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001164801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001164801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO32767.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAG01017089; VDO32767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3QV96; -.
DR STRING; 42155.A0A0R3QV96; -.
DR WBParaSite; BTMF_0001164801-mRNA-1; BTMF_0001164801-mRNA-1; BTMF_0001164801.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR PANTHER; PTHR24044:SF420; NEUROGENIC LOCUS PROTEIN DELTA; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
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:UP000280834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280815};
KW Transmembrane {ECO:0000256|RuleBase:RU280815};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815}.
FT DOMAIN 36..80
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 76..111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 144..182
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 38..47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 51..63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 71..80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 101..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 172..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 200 AA; 21996 MW; 8BFB74B6A7009D0C CRC64;
MSHNGFQRES IPSGKTWIEE TLVGTNGFRM RIAYRITCAN DYYGPRCLTF CQPMSSTVGH
FQCTSNGSLA CSPGWEGSSC DIARCDNCIN GACDRPDSCR CKTGWTGPNC DQCVRYPGCK
HGTCKTPNQC ICDEGWGGHF CNEDLNYCTR HHPCRNNATC RNTGHGQYTC ECPDGYTGTD
CEIRVQNCSL QPCLNGATCS
//
