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Database: UniProt
Entry: A0A0N4X7G6_HAEPC
LinkDB: A0A0N4X7G6_HAEPC
Original site: A0A0N4X7G6_HAEPC 
ID   A0A0N4X7G6_HAEPC        Unreviewed;       335 AA.
AC   A0A0N4X7G6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN   ORFNames=HPLM_LOCUS20299 {ECO:0000313|EMBL:VDO82827.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0002030801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0002030801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO82827.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO82827.1,
RC   ECO:0000313|Proteomes:UP000268014};
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:PRU00377}.
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DR   EMBL; UZAF01022060; VDO82827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4X7G6; -.
DR   STRING; 6290.A0A0N4X7G6; -.
DR   WBParaSite; HPLM_0002030801-mRNA-1; HPLM_0002030801-mRNA-1; HPLM_0002030801.
DR   OMA; LENWINQ; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   Gene3D; 2.10.25.140; -; 1.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR000742; EGF-like_dom.
DR   Pfam; PF01414; DSL; 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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW   Signal {ECO:0000256|RuleBase:RU280815};
KW   Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          85..127
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   REGION          216..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        87..96
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        118..127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
SQ   SEQUENCE   335 AA;  36429 MW;  9ECEB12C79A30BA4 CRC64;
     MLPYPIKDPD RKCLKSGQLE IVGGTETVLD LIITNITVEY ITVEFEIVGN TERPIQRISK
     RIAVDGGLPA ERVAVAKGIL IDFVTKCTRP FYGIMCARQC FEEDGAKYVC DPHGEKVCLV
     GWTGKDCNTG KCRLSLAFDV ICLCLVGWTG KDCNTAMTGV STEKLSSHAP ILTSTSTSHK
     VDLSSHAPIL TTTSSGRLLT KDIETTTRPK VLLVDPDVQK PSTPSPVATK QLPEKPVSAG
     PLSTGSTPVA HMTAVPTSTS RVTALPANSL IDHVLVLFFV AMLIGVIKYA TWKMTRSVLL
     ENWINQKRAK VFTTESSSHS LRKDVTEKVR AGYHS
//
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