ID H0X4D3_OTOGA Unreviewed; 1218 AA.
AC H0X4D3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=JAG1 {ECO:0000313|Ensembl:ENSOGAP00000010051.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000010051.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000010051.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AAQR03053297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003788060.1; XM_003788012.2.
DR AlphaFoldDB; H0X4D3; -.
DR STRING; 30611.ENSOGAP00000010051; -.
DR Ensembl; ENSOGAT00000011228.2; ENSOGAP00000010051.2; ENSOGAG00000011220.2.
DR GeneID; 100950090; -.
DR KEGG; oga:100950090; -.
DR CTD; 182; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160148; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR InParanoid; H0X4D3; -.
DR OMA; MAIGPCI; -.
DR OrthoDB; 5475408at2759; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IEA:Ensembl.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IEA:Ensembl.
DR GO; GO:0061073; P:ciliary body morphogenesis; IEA:Ensembl.
DR GO; GO:0072017; P:distal tubule development; IEA:Ensembl.
DR GO; GO:0061444; P:endocardial cushion cell development; IEA:Ensembl.
DR GO; GO:0002085; P:inhibition of neuroepithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IEA:Ensembl.
DR GO; GO:0072070; P:loop of Henle development; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; IEA:Ensembl.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0072015; P:podocyte development; IEA:Ensembl.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IEA:Ensembl.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:2000241; P:regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0002456; P:T cell mediated immunity; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
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; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF225; NOTCH 2; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR02059; JAGGEDFAMILY.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00214; VWC; 1.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 4.
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:UP000005225};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1218
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003544393"
FT TRANSMEM 1068..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..229
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 230..263
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 296..334
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 336..372
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 374..410
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 412..448
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 450..485
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 487..523
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 525..561
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 586..627
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 629..665
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 667..703
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 705..741
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 744..780
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 782..818
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 820..856
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1142..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 187..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 200..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 220..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 253..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 324..333
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 362..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 400..409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 438..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 454..464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 475..484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 513..522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 551..560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 617..626
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 655..664
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 693..702
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 731..740
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 770..779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 808..817
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 846..855
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1218 AA; 133666 MW; FEC959362518BA3B CRC64;
MRSPRTRGRP GCPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGARN
PGDRKCTRDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRSNDRNRI
VLPFSFAWPR SYTLLVEAWD SSNDTAQPDN IIEKASHSGM INPSRQWQTL KQNTGVAHFE
YQIRVTCDDY YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC VEGWMGPECN KAICRQGCSL
KHGSCKLPGD CRCQYGWRGL YCDKCIPHPG CVHGTCNEPW QCLCETNWGG QLCDKDLNYC
GTHQPCLNGG TCSNTGPDKY QCSCPEGYSG PNCEIAEHAC LSDPCHNRGS CKETALGFEC
ECSPGWTGPT CSTNIDDCSP NNCSHGGTCQ DLVNGFKCVC PPQWTGKTCQ LDANECEAKP
CLNARGCKNL IASYYCDCLP GWMGQNCDIN INDCLGQCQN DASCRDLVNG YRCICPPGYA
GDHCERDIDE CASNPCLNGG HCQNEINRFQ CLCPTGFSGN LCQLDVDYCE PNPCQNGAQC
YNRASDYFCK CPEDYEGKNC SHLKDHCRTT PCEVIDSCTV AMASNDTPEG VRYISSNVCG
PHGKCKSQSG GKFTCDCNKG FTGTYCHENI NDCESSPCKN GGTCIDGVNS YKCICSDGWE
GAYCESNIND CSQNPCHNGG TCRDLVNDFY CDCKNGWKGK TCHSRDSQCD EATCNNGGTC
YDEGDAFKCM CPGGWEGTTC NIARNSSCLP SPCHNGGTCV VNGESFTCVC KEGWEGPICT
QNTNDCSPHP CYNSGTCVDG DNWYRCECAP GFAGPDCRIN INECQSSPCA FGATCVDEIN
GYRCVCPLGH SGAKCQEVSG RPCITMGSVI PDGAKWDEDC NTCQCVNGRI ACSKVWCGPR
PCLLRKGHSD CPSGQSCIPI LDDQCFVRPC TGVGECRSSS LQPVKTKCTS DSYYQDNCAN
ITFTFNKEMM SPGLTTEHIC SELRNLNILK NVSAEYSIYI ACEPSPSANN EIHVAISAED
IRDDGNPIKE ITDKIIDLVS KRDGNSSLIA AVAEVRVQRH PPKNRTDFLV PLLSSVLTVA
WICCLVTAFY WCVRKRRKPS SHTHSASEDN TTNNVREQLN QIKNPIEKHG ANTVPIKDYE
SKNSKMSKIR THNSEVEEDD MDKHQQKARF AKQPAYTLVD REEKPPNGTP TKHPNWTNKQ
DNRDLESAQS LNRMEYIV
//
