GenomeNet

Database: UniProt
Entry: A0A016WCG4_9BILA
LinkDB: A0A016WCG4_9BILA
Original site: A0A016WCG4_9BILA 
ID   A0A016WCG4_9BILA        Unreviewed;       519 AA.
AC   A0A016WCG4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN   Name=Acey_s0807.g2448 {ECO:0000313|EMBL:EYC37301.1};
GN   Synonyms=Acey-apx-1 {ECO:0000313|EMBL:EYC37301.1};
GN   ORFNames=Y032_0807g2448 {ECO:0000313|EMBL:EYC37301.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC37301.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYC37301.1}.
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DR   EMBL; JARK01000407; EYC37301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016WCG4; -.
DR   STRING; 53326.A0A016WCG4; -.
DR   Proteomes; UP000024635; 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; 2.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 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; 6.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
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|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..519
FT                   /note="Delta-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001490505"
FT   TRANSMEM        382..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..167
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          203..232
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          234..273
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          276..314
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        129..138
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        158..167
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        222..231
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        244..261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        263..272
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        304..313
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   519 AA;  57483 MW;  C4A2F25FFE02CA6D CRC64;
     MCIYSSIFFA ALLATLTDLV AASGSLEVRL ISSRACSVKL CVKKPRAKPL DSCLLESQLI
     FLQSQQQRLV STPFHFPFPE SFILVVELYD AQGGQLSQNT SKERFTVGTE FKPAAGSSEF
     LDIAFRASCH SSYFGAGCQR YCKSSFSYTC DSEGRKICAE GWQGEQCDQP ICPDGCKHGR
     CVEPGRCECD HGFFGSTCAE CRRSENCRHG TCRDDQPFTC ACEPGWGGIF CERDLEYCTR
     HQPCKNDGVC TNGGVRTDFT CQCPEGFVGA TCDIELPSIC EHLGICRNGG VCTDADTRLG
     RCICADGFEG RYCERRVVRS LCTATTCKNG GSCLDGSKCV CPQCLSGADC STIDEQCLWQ
     RANATLTPTV TDHQSDVTEA RILMLMAFAS IMMLATCVVI FFLKYKKMKR ILRDPVTQNT
     LNEHRQIHEL PNRSIDNRSP DEVYKVFVIP SKKSKDVDGP ASIEYETRYI SQPRGRYRTL
     PCVDVSAAAE PEHHYAEIEY RPTTVSLDDK QLADNACSV
//
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