ID K7FNC7_PELSI Unreviewed; 1184 AA.
AC K7FNC7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=JAG1 {ECO:0000313|Ensembl:ENSPSIP00000009537.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000009537.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000009537.1}
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; AGCU01171898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01171900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FNC7; -.
DR STRING; 13735.ENSPSIP00000009537; -.
DR Ensembl; ENSPSIT00000009584.1; ENSPSIP00000009537.1; ENSPSIG00000008520.1.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160148; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR OMA; MAIGPCI; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000007267; 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:SF228; JAGGED CANONICAL NOTCH LIGAND 2; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF12661; hEGF; 2.
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; SSF57603; FnI-like domain; 1.
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; 3.
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:UP000007267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {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 TRANSMEM 1034..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..195
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 196..229
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 262..300
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 302..338
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 340..376
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 378..414
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 416..451
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 453..489
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 491..527
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 556..593
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 595..631
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 633..669
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 671..707
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 710..746
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 748..784
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 786..822
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1117..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 153..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 166..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 186..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 219..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 290..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 328..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 366..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 404..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 420..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 441..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 479..488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 517..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 583..592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 621..630
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 659..668
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 697..706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 736..745
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 774..783
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 812..821
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1184 AA; 130237 MW; F101CC637FC070CC CRC64;
FELEILSVQN VNGELQNGNC CDGTRNPGDR KCTKDECDTY FKACLKEYQS RVSAGGPCSF
GSGATPVIGG NTFNLKYTRN NERNRIVLPF SFAWPRSYTL LVEAWDYSND TANPDSIIEK
ASHSGMINPS RQWQTLKHNA GIAHFEYQIR VTCDEHYYGF GCNKFCRPRD DFFGHHTCDQ
NGNKTCLEGW MGPECSKAIC RQGCSPKHGS CKIPGECRCQ YGWQGQYCDK CIPHPGCVHG
TCIEPWQCLC ETNWGGQLCD KDLNYCGTHP PCLNGGTCSN TGPDKYQCSC PEGYSGQNCE
IAEHACLSDP CHNGGSCLET STGFECVCMP GWAGPTCTLN IDDCSPNPCG HGGTCQDLVD
GFKCICPPQW TGKTCQLDAN ECEGKPCVNA NSCRNLIGSY YCDCIAGWSG QNCDININDC
LGQCQNGGSC RDLVNGYRCI CPPGYAGDHC EKDINECASN PCLNGGHCQD EINGFHCLCP
AGFSGNLCQL DIDYCEPNPC QNGAQCFNLN TDYFCTCPED YEGKNCSHLK DHCRTTPCEV
IDSCTVAVAS NSTPEGVRYI SSNVCGPHGK CKSQAGGKFT CECNKGFTGT YCHENINDCE
SNPCKNGGTC IDGINSYKCI CSDGWEGIYC ETNINDCSKN PCHNGGTCRD LVNDFFCECK
NGWKGKTCHS RDSQCDEATC NNGGTCYDEG DTFKCMCPAG WEGATCNIAR NSSCLPNPCH
NGGTCVVSGD SFTCVCKEGW EGPTCTQNTN DCSPHPCYNS GTCVDGDNWY RCECAPGFAG
PDCRININEC QSSPCAFGAT CVDEINGYRC ICPPGRSGPR CQEVTGRPCI SNGRVMPDGA
KWDDDCNTCQ CWNGKVACSK VWCGPRPCLI HGKGHECPAG HTCVPIKDDH CFTRPCSGVG
VCWPSNQQPI KTKCNLDSYY QDNCANITFT FNKELMASGL TTEHICSDLR NLNILKNVSV
EYSIYITCEP SHLAHNEIHV AISAEDIGKD ENPVKEITDK IIDLVSKRDG NNTLIAAVAE
VRVQRRPIKN KTDFLVPLLS SVLTVAWICC LVTAFYWCIR KRRKQSSHSH TASDDNTTNN
VREQLNQIKN PIEKHGANTV PIKDYENKNS KIAKIRTHNS EVEEDDMDKH QQKSRFVKQP
AYTLVDRDEK PPNSTPTKHP NWTNKQDNRD LESAQSLNRM EYIV
//
