ID A1L1P2_DANRE Unreviewed; 717 AA. AC A1L1P2; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-DEC-2022, entry version 105. DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815}; GN Name=sc:d0402 {ECO:0000313|RefSeq:NP_571030.2}; GN OrderedLocusNames=dld {ECO:0000313|EMBL:AAI29160.1, GN ECO:0000313|RefSeq:NP_571030.2, ECO:0000313|ZFIN:ZDB-GENE-990415-47}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI29160.1}; RN [1] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=9007237; RA van Eeden F.J., Granato M., Schach U., Brand M., Furutani-Seiki M., RA Haffter P., Hammerschmidt M., Heisenberg C.P., Jiang Y.J., Kane D.A., RA Kelsh R.N., Mullins M.C., Odenthal J., Warga R.M., Allende M.L., RA Weinberg E.S., Nusslein-Volhard C.; RT "Mutations affecting somite formation and patterning in the zebrafish, RT Danio rerio."; RL Development 123:153-164(1996). RN [2] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=9706695; RA van Eeden F.J., Holley S.A., Haffter P., Nusslein-Volhard C.; RT "Zebrafish segmentation and pair-rule patterning."; RL Dev. Genet. 23:65-76(1998). RN [3] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=9765210; RA Durbin L., Brennan C., Shiomi K., Cooke J., Barrios A., Shanmugalingam S., RA Guthrie B., Lindberg R., Holder N.; RT "Eph signaling is required for segmentation and differentiation of the RT somites."; RL Genes Dev. 12:3096-3109(1998). RN [4] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=10101116; RA Takke C., Dornseifer P., v Weizsacker E., Campos-Ortega J.A.; RT "her4, a zebrafish homologue of the Drosophila neurogenic gene E(spl), is a RT target of NOTCH signalling."; RL Development 126:1811-1821(1999). RN [5] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=10191075; RA Lissemore J.L., Starmer W.T.; RT "Phylogenetic analysis of vertebrate and invertebrate Delta/Serrate/LAG-2 RT (DSL) proteins."; RL Mol. Phylogenet. Evol. 11:308-319(1999). RN [6] {ECO:0000313|EMBL:AAI29160.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000313|EMBL:AAI29160.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=30244429; RA Yang Z., Chen S., Xue S., Li X., Sun Z., Yang Y., Hu X., Geng T., Cui H.; RT "Generation of Cas9 transgenic zebrafish and their application in RT establishing an ERV-deficient animal model."; RL Biotechnol. Lett. 40:1507-1518(2018). RN [8] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=30267687; RA Mitra S., Sharma P., Kaur S., Khursheed M.A., Gupta S., Ahuja R., RA Kurup A.J., Chaudhary M., Ramachandran R.; RT "Histone Deacetylase-Mediated Muller Glia Reprogramming through Her4.1- RT Lin28a Axis Is Essential for Retina Regeneration in Zebrafish."; RL iScience 7:68-84(2018). RN [9] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=30208064; RA Bickers C., Espanola S.D., Grainger S., Pouget C., Traver D.; RT "Zebrafish snai2 mutants fail to phenocopy morphant phenotypes."; RL PLoS ONE 13:e0202747-e0202747(2018). RN [10] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=30681411; RA Lush M.E., Diaz D.C., Koenecke N., Baek S., Boldt H., St Peter M.K., RA Gaitan-Escudero T., Romero-Carvajal A., Busch-Nentwich E.M., Perera A.G., RA Hall K.E., Peak A., Haug J.S., Piotrowski T.; RT "scRNA-Seq reveals distinct stem cell populations that drive hair cell RT regeneration after loss of Fgf and Notch signaling."; RL Elife 8:e44431-e44431(2019). RN [11] {ECO:0000313|RefSeq:NP_571030.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=30606747; RA Mitra S., Sharma P., Kaur S., Khursheed M.A., Gupta S., Chaudhary M., RA Kurup A.J., Ramachandran R.; RT "Dual regulation of lin28a by Myc is necessary during zebrafish retina RT regeneration."; RL J. Cell Biol. 218:489-507(2019). RN [12] {ECO:0000313|RefSeq:NP_571030.2} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC129159; AAI29160.1; -; mRNA. DR RefSeq; NP_571030.2; NM_130955.2. DR AlphaFoldDB; A1L1P2; -. DR DNASU; 30138; -. DR GeneID; 30138; -. DR KEGG; dre:30138; -. DR CTD; 1738; -. DR ZFIN; ZDB-GENE-990415-47; dld. DR OrthoDB; 406049at2759; -. DR Proteomes; UP000000437; Chromosome 13. 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: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 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 Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 5. DR Pfam; PF12661; hEGF; 1. DR Pfam; PF07657; MNNL; 1. DR SMART; SM00051; DSL; 1. DR SMART; SM00181; EGF; 8. DR SMART; SM00179; EGF_CA; 6. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. 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. DR PROSITE; PS01187; EGF_CA; 2. PE 2: Evidence at transcript level; 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}; KW Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; 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..19 FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_571030.2" FT CHAIN 20..717 FT /note="Delta-like protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035105290" FT CHAIN 20..717 FT /note="Delta-like protein D" FT /evidence="ECO:0000313|RefSeq:NP_571030.2" FT /id="PRO_5002635839" FT TRANSMEM 544..570 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 175..219 FT /note="DSL" FT /evidence="ECO:0000259|PROSITE:PS51051" FT DOMAIN 286..324 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 326..362 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 364..401 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 403..439 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 441..477 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 479..515 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT REGION 649..693 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 177..186 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377" FT DISULFID 190..202 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377" FT DISULFID 210..219 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377" FT DISULFID 314..323 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 352..361 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 391..400 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 429..438 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 467..476 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 505..514 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" SQ SEQUENCE 717 AA; 78971 MW; D599476052EFE60F CRC64; MGRLMIAVLL CVMISQGFCS GVFELKLQEF LNKKGVTGNA NCCKGSAAEG LQCECKTFFR ICLKHYQANV SPDPPCTYGG AVTPVLGSNS FQVPESFPDS SFTNPIPFAF GFTWPGTFSL IIEALHTDST DDLSTENPDR LISRMTTQRH LTVGEEWSQD LQVGGRTELK YSYRFVCDEH YYGEGCSVFC RPRDDTFGHF TCGERGEIIC NSGWKGQYCT EPICLPGCDE DHGFCDKPGE CKCRVGFSGK YCDDCIRYPG CLHGTCQQPW QCNCQEGWGG LFCNQDLNYC THHKPCQNGA TCTNTGQGSY TCSCRPGFTG DSCEIEVNEC SGSPCRNGGS CTDLENTYSC TCPPGFYGRN CELSAMTCAD GPCFNGGQCA DNPEGGYFCQ CPMGYAGFNC EKKIDHCSSN PCSNDAQCLD LVDSYLCQCP EGFTGTHCED NIDECATYPC QNGGTCQDGL SDYTCTCPPG YTGKNCTSAV NKCLHNPCHN GATCHEMDGR YVCACIPGYG GRNCQFLLPE NPQGQAIVEG ADKRYSYEED DGGFPWTAVC AGIILVLLVL IGGSVFVIYI RLKLQQRSQQ IDSHSEIETM NNLTNNRSRE KDLSVSIIGA TQVKNINKKV DFQSDGDKNG FKSRYSLVDY NLVHELKQED LGKEDSERSE ATKCEPLDSD SEEKHRNHLK SDSSERKRTE SLCKDTKYQS VFVLSEEKDE CIIATEV //