ID A0A482WU96_LAOST Unreviewed; 799 AA.
AC A0A482WU96;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN ORFNames=LSTR_LSTR009704 {ECO:0000313|EMBL:RZF37179.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF37179.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF37179.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF37179.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF37179.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. {ECO:0000256|RuleBase:RU280815}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, 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:RZF37179.1}.
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DR EMBL; QKKF02025202; RZF37179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482WU96; -.
DR STRING; 195883.A0A482WU96; -.
DR InParanoid; A0A482WU96; -.
DR Proteomes; UP000291343; 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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 7.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011651; Notch_ligand_N.
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; 6.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 7.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW 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:UP000291343};
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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..799
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019734756"
FT TRANSMEM 581..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..218
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 285..323
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 325..361
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 363..399
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 401..437
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 439..475
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 477..513
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 515..551
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 612..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 176..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 189..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 209..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 313..322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 351..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 389..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 427..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 465..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 503..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 541..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 799 AA; 86562 MW; 8615F053206D2D40 CRC64;
MKWISSSLVF LLAILNQASS SGVFELRLKS FTNEHGRDSV GQCCSGERTE PCRGPCKTRF
RVCLKHYQVK IDTTSPCTFG DVITPVLGDN SVHLANANPH GFNNPIRFPF DFAWPGTFSL
IVEAWHDNNN TSTTAGSKTL ISRLTTQRWL DVSDDWTEDE HKSSHSDMRY EYRVTCDSHY
YGSGCANLCR PRDDSFGHYT CSPVGGRVCL DGWQGDYCTK PKCLPGCDEQ HGHCSQPNEC
TCHSGWKGRL CDQCERYPGC LHGSCQKPWE CLCDEGWGGL FCNQDLNYCT NHKPCRNGGT
CFNTGQGSYT CSCPPGFSGT DCEREVDDCA HHPCLNGGTC KDNGTSYICE CPKHWHGLHC
ENSAQTCGDL PCRNGGTCED TDHGYTCQCP PGYAGVDCAH QIDECSPNPC RNGGSCVDKI
GGYECHCPVG FQGPDCEINI DDCVDSPCLN GGTCIDMVNQ FRCQCIPGYV GNLCQSKVNY
CLAKPCANGG SCQDLVNDYK CSCRPGFTGK DCSVDIDECA SNPCANGGTC VNRVNGYRCD
CAHGWRGKNC RDEESSNVGN ISRHVSHQKA TADSGLTTEH VVVIATLSTA VPILVLVAAV
VVVCMKQRRK REQQRADDEA RMQNEQNAVH SSVSKRGDAH MIKNTWEPCV KDGGGGGELG
YTAKQCVASP NPTPGAGAGA AGPEAATGPV YSLHRSRSQK QLNTDISVQR QATRASCKDL
DRTPDNRISV LSVDSSLCNT SDTSLLKRSS TAQEKEGGVS SPLAGSASAS SSVYVIDEHY
NQRPAHAHSH TDTLLATEV
//
