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Database: UniProt
Entry: A0A3B3BFJ7_ORYME
LinkDB: A0A3B3BFJ7_ORYME
Original site: A0A3B3BFJ7_ORYME 
ID   A0A3B3BFJ7_ORYME        Unreviewed;       788 AA.
AC   A0A3B3BFJ7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000004250.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000004250.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A3B3BFJ7; -.
DR   STRING; 30732.ENSOMEP00000004250; -.
DR   PaxDb; 30732-ENSOMEP00000004250; -.
DR   Ensembl; ENSOMET00000009473.1; ENSOMEP00000004250.1; ENSOMEG00000005200.1.
DR   GeneTree; ENSGT00940000159781; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ 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; 6.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.60.40.3510; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   PANTHER; PTHR24044:SF380; DELTA-LIKE PROTEIN 1; 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; 5.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 6.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
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}; Membrane {ECO:0000256|RuleBase:RU280815};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
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          167..211
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          278..316
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          318..354
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          356..393
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          395..431
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          436..472
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          474..510
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          528..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        169..178
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        182..194
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        202..211
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        306..315
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        344..353
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        383..392
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        421..430
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        462..471
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        500..509
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   788 AA;  86339 MW;  C136175C0D4CB286 CRC64;
     MKFVFQVLCS GVFELKLQEF LNKKGISGNA NCCPGGSAHP QGHQQCECKT FFRVCLKHYQ
     ANVSPEPPCT YGGAVTPVLG SNSFQVPETN ADSFTNPIRF PFGFTWPGTF SLIIEALHTD
     SLDDLTTENP ERLISRITTQ RHLSVGEEWF KDMQTADRTE LRYSYRFLCD EHYYGDGCSV
     FCRPRDDAFG HFTCGERGEI ICNSGWKGQY CTDPICLPGC DEEHGFCDKP GECKCRVGFS
     GRYCDDCIRY PGCLHGTCQQ PWQCNCQEGW GGLFCNQDLN YCTHHKPCLN GATCTNTGQG
     SYTCTCLPGY TGASCEIQVS ECSGNPCRNG GSCSDNDNGY KCACPPGFYG NNCELSANTC
     ADGPCFNGGR CADNPEGGYF CQCPAGYAGF NCEKKIDHCS SNPCLNGAEC VDLVNSYLCR
     CPEGFIGSNC EVRSSISGHC QSFPCQNGGT CQDGGNDYSC TCPPGYTGKN CSSPVSRCHH
     NPCHNGATCH ERGGRYVCAC VPGYGGHNCQ FLLPEMSGGS QPVVDVADRR YSSSESENSE
     DSEDDESGFP WAAVCAGIFL VLVVLISCSV LVVYVRVKLQ DRLSHHSDSV HSDSQETMNN
     LTTTNNCLRS DKELGPMMTT SIKNTNKKAD YHSDLAGSLV GLSGINGSEK NGFKTRYPSV
     EYNLVHELRS EEPSLCKEDE PNEPEAKCEM LEEFNTEEGF RKTQNSNASE KQLTESTGCS
     EERYQSSTDL GCHSASDLKY HSTNDVKFQS GNDESPDDSQ YSCLPDTKYQ SVYVMSDQKD
     ECVIATEV
//
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