ID G1PDP3_MYOLU Unreviewed; 1217 AA.
AC G1PDP3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=JAG1 {ECO:0000313|Ensembl:ENSMLUP00000008601.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008601.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000008601.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000008601.2}
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; AAPE02016065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02016066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PDP3; -.
DR STRING; 59463.ENSMLUP00000008601; -.
DR Ensembl; ENSMLUT00000009437.2; ENSMLUP00000008601.2; ENSMLUG00000009421.2.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160148; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR InParanoid; G1PDP3; -.
DR OMA; MAIGPCI; -.
DR TreeFam; TF351835; -.
DR Proteomes; UP000001074; 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; 9.
DR Pfam; PF12661; hEGF; 4.
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; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
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:UP000001074};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1217
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003418017"
FT TRANSMEM 1067..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..228
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 229..262
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 295..333
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 335..371
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 373..409
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 411..447
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 449..484
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 486..522
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 524..560
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 585..626
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 628..664
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 666..702
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 704..740
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 743..779
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 781..817
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 819..855
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1152..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 186..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 199..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 219..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 252..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 323..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 361..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 399..408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 437..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 453..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 474..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 512..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 550..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 616..625
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 654..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 692..701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 730..739
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 769..778
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 807..816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 845..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1217 AA; 133774 MW; 6867CD8E784B6CDB CRC64;
QREQRRRGGP GRTLNLLLAL SAPARQVCGA SGQFELEILS MQNVNGELQN GNCCGGARSP
GDRKCARDEC DTYFKVCLKE YQSRVTAEGP CSFGSGSTPV IGGNTFNLKT SRGNERNRIV
LPFSFAWPRS YTLLVEAWDS SNDTLQPDSI IEKASHSGMI NPSRQWQTLK QNTGVAHFEY
QIRVTCDDYY YGFGCNKFCR PRDDFFGHYA CDQNGNKTCM EGWMGPECNR AICRQGCSPK
HGSCKLPGDC RCQYGWQGLY CDKCIPHPGC VHGTCNEPWQ CLCETNWGGQ LCDKDLNYCG
THQPCLNRGT CSNTGPDKYQ CSCPEGYSGP NCEIAEHACL SDPCHNRGSC KETSLGFECE
CSPGWTGPTC STNIDDCSPN NCSHGGTCLD LVNGFKCVCP PQWTGKTCQL DANECEAKPC
VNAKSCKNLI ASYYCDCLPG WMGQNCEINI NDCLGQCQND ATCRDLVNGY RCICPPGYAG
DHCERDIDEC ASNPCLNGGH CQNEINRFQC LCPTGFSGNL CQLDIDYCEP NPCQNGAQCY
NRASDYFCKC TEDYEGKNCS HLKDHCRTTP CEVIDSCTVA MASNDTPEGV RYISSNVCGP
HGKCKSQSGG KFTCDCNKGF TGTYCHENIN DCESNPCKNG GTCIDGVNSY KCICSDGWEG
AYCEANINDC SQNPCHNGGS CRDLVNDFYC DCKNGWKGKT CHSRDSQCDE ATCNNGGTCY
DEGDAFKCMC PGGWEGTTCN IARNSSCLPS PCHNGGTCVV NGESFTCVCK EGWEGPICTQ
NTNDCSPHPC YNSGTCVDGD NWYRCECAPG FAGPDCRINI NECQSSPCAY GATCVDEING
YRCICPPGHS GAKCQEVSGR PCITMGGVIP DGAKWDDDCN TCQCLNGRIA CSKVWCGPRP
CLLHKGHSEC PSGQSCLPIL DDQCFVRPCT GVGECHSSSL QPVKTKCASD PYYQENCANI
TFTFNKEMMS PGLTTEHICS ELRNLNILKN VSAEYSIYIA CEPSPSANNE IHVAISAEDI
RDDGNPIKEI TDKIIDLVSK RDGNSSLIAA VAEVRVQRRP LKNRTDFLVP LLSSVLTVAW
ICCLVTAFYW CVRKRRKPSS HARSASEDNT TNNVREQLNQ IKNPIEKLGA NTVPIKDYEN
KNSKMSKIRT HNSEVEEDDM DKHQQKARFA KQPAYTLVDR EEKPPNGTPA KHPNWTNKQD
NRDLESAQSL NRMEYIV
//