JAG1_RAT
ID JAG1_RAT Reviewed; 1219 AA.
AC Q63722; P70640;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein jagged-1;
DE Short=Jagged1;
DE AltName: CD_antigen=CD339;
DE Flags: Precursor;
GN Name=Jag1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Sciatic nerve;
RX PubMed=7697721; DOI=10.1016/0092-8674(95)90294-5;
RA Lindsell C.E., Shawber C.J., Boulter J., Weinmaster G.;
RT "Jagged: a mammalian ligand that activates Notch1.";
RL Cell 80:909-917(1995).
RN [2]
RP INTERACTION WITH NOTCH1.
RX PubMed=28089369; DOI=10.1016/j.devcel.2016.12.013;
RA Kakuda S., Haltiwanger R.S.;
RT "Deciphering the fringe-mediated notch code: identification of activating
RT and inhibiting sites allowing discrimination between ligands.";
RL Dev. Cell 40:193-201(2017).
CC -!- FUNCTION: Ligand for multiple Notch receptors and involved in the
CC mediation of Notch signaling. May be involved in cell-fate decisions
CC during hematopoiesis. Enhances fibroblast growth factor-induced
CC angiogenesis (in vitro). Seems to be involved in early and late stages
CC of mammalian cardiovascular development. Inhibits myoblast
CC differentiation. May regulate fibroblast growth factor-induced
CC angiogenesis.
CC -!- SUBUNIT: Interacts with NOTCH1 (PubMed:28089369). Interacts with NOTCH2
CC and NOTCH3 (By similarity). {ECO:0000250|UniProtKB:Q9QXX0,
CC ECO:0000269|PubMed:28089369}.
CC -!- INTERACTION:
CC Q63722; Q07954: LRP1; Xeno; NbExp=4; IntAct=EBI-4567800, EBI-1046087;
CC Q63722; Q03350: Thbs2; Xeno; NbExp=2; IntAct=EBI-4567800, EBI-4567830;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000250|UniProtKB:P78504}.
CC -!- TISSUE SPECIFICITY: Widely expressed in a variety of tissues.
CC -!- DEVELOPMENTAL STAGE: Expression is seen in E11.5-E14.5 embryos in four
CC distinct regions of the ventricular zone in the developing spinal cord.
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DR EMBL; L38483; AAB06509.1; -; mRNA.
DR PIR; A56136; A56136.
DR RefSeq; NP_062020.1; NM_019147.1.
DR PDB; 5UK5; X-ray; 2.51 A; B=32-334.
DR PDBsum; 5UK5; -.
DR AlphaFoldDB; Q63722; -.
DR BMRB; Q63722; -.
DR SMR; Q63722; -.
DR BioGRID; 247829; 3.
DR IntAct; Q63722; 5.
DR MINT; Q63722; -.
DR STRING; 10116.ENSRNOP00000010638; -.
DR GlyGen; Q63722; 9 sites.
DR PhosphoSitePlus; Q63722; -.
DR PaxDb; Q63722; -.
DR PRIDE; Q63722; -.
DR GeneID; 29146; -.
DR KEGG; rno:29146; -.
DR UCSC; RGD:2937; rat.
DR CTD; 182; -.
DR RGD; 2937; Jag1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q63722; -.
DR OrthoDB; 72177at2759; -.
DR PhylomeDB; Q63722; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR PRO; PR:Q63722; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; IDA:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISO:RGD.
DR GO; GO:0060411; P:cardiac septum morphogenesis; ISO:RGD.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0061073; P:ciliary body morphogenesis; ISO:RGD.
DR GO; GO:0072017; P:distal tubule development; ISO:RGD.
DR GO; GO:0061444; P:endocardial cushion cell development; ISO:RGD.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0072070; P:loop of Henle development; ISO:RGD.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; ISO:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:RGD.
DR GO; GO:0061314; P:Notch signaling involved in heart development; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:BHF-UCL.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISO:RGD.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0032495; P:response to muramyl dipeptide; ISO:RGD.
DR GO; GO:0002456; P:T cell mediated immunity; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:UniProtKB.
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; IPR033108; Jag1.
DR InterPro; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24049:SF18; PTHR24049:SF18; 3.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 11.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF07657; MNNL; 1.
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; SSF57184; SSF57184; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 16.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 16.
DR PROSITE; PS01187; EGF_CA; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Developmental protein;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Notch signaling pathway; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1219
FT /note="Protein jagged-1"
FT /id="PRO_0000007627"
FT TOPO_DOM 34..1067
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1068..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1094..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..229
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 230..263
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 264..294
FT /note="EGF-like 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 296..334
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 336..372
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 374..410
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 412..448
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 450..485
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 487..523
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 525..561
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 586..627
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 629..665
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 667..703
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 705..741
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 744..780
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 782..818
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 820..856
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 199..207
FT /note="Important for interaction with NOTCH1"
FT /evidence="ECO:0000250"
FT REGION 1182..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 187..196
FT /evidence="ECO:0000250"
FT DISULFID 200..212
FT /evidence="ECO:0000250"
FT DISULFID 220..229
FT /evidence="ECO:0000250"
FT DISULFID 234..245
FT /evidence="ECO:0000250"
FT DISULFID 238..251
FT /evidence="ECO:0000250"
FT DISULFID 253..262
FT /evidence="ECO:0000250"
FT DISULFID 265..276
FT /evidence="ECO:0000250"
FT DISULFID 271..282
FT /evidence="ECO:0000250"
FT DISULFID 284..293
FT /evidence="ECO:0000250"
FT DISULFID 300..312
FT /evidence="ECO:0000250"
FT DISULFID 306..322
FT /evidence="ECO:0000250"
FT DISULFID 324..333
FT /evidence="ECO:0000250"
FT DISULFID 340..351
FT /evidence="ECO:0000250"
FT DISULFID 345..360
FT /evidence="ECO:0000250"
FT DISULFID 362..371
FT /evidence="ECO:0000250"
FT DISULFID 378..389
FT /evidence="ECO:0000250"
FT DISULFID 383..398
FT /evidence="ECO:0000250"
FT DISULFID 400..409
FT /evidence="ECO:0000250"
FT DISULFID 416..427
FT /evidence="ECO:0000250"
FT DISULFID 421..436
FT /evidence="ECO:0000250"
FT DISULFID 438..447
FT /evidence="ECO:0000250"
FT DISULFID 454..464
FT /evidence="ECO:0000250"
FT DISULFID 458..473
FT /evidence="ECO:0000250"
FT DISULFID 475..484
FT /evidence="ECO:0000250"
FT DISULFID 491..502
FT /evidence="ECO:0000250"
FT DISULFID 496..511
FT /evidence="ECO:0000250"
FT DISULFID 513..522
FT /evidence="ECO:0000250"
FT DISULFID 529..540
FT /evidence="ECO:0000250"
FT DISULFID 534..549
FT /evidence="ECO:0000250"
FT DISULFID 551..560
FT /evidence="ECO:0000250"
FT DISULFID 578..605
FT /evidence="ECO:0000250"
FT DISULFID 599..615
FT /evidence="ECO:0000250"
FT DISULFID 617..626
FT /evidence="ECO:0000250"
FT DISULFID 633..644
FT /evidence="ECO:0000250"
FT DISULFID 638..653
FT /evidence="ECO:0000250"
FT DISULFID 655..664
FT /evidence="ECO:0000250"
FT DISULFID 671..682
FT /evidence="ECO:0000250"
FT DISULFID 676..691
FT /evidence="ECO:0000250"
FT DISULFID 693..702
FT /evidence="ECO:0000250"
FT DISULFID 709..720
FT /evidence="ECO:0000250"
FT DISULFID 714..729
FT /evidence="ECO:0000250"
FT DISULFID 731..740
FT /evidence="ECO:0000250"
FT DISULFID 748..759
FT /evidence="ECO:0000250"
FT DISULFID 753..768
FT /evidence="ECO:0000250"
FT DISULFID 770..779
FT /evidence="ECO:0000250"
FT DISULFID 786..797
FT /evidence="ECO:0000250"
FT DISULFID 791..806
FT /evidence="ECO:0000250"
FT DISULFID 808..817
FT /evidence="ECO:0000250"
FT DISULFID 824..835
FT /evidence="ECO:0000250"
FT DISULFID 829..844
FT /evidence="ECO:0000250"
FT DISULFID 846..855
FT /evidence="ECO:0000250"
FT DISULFID 925..936
FT /evidence="ECO:0000250"
FT DISULFID 948..958
FT /evidence="ECO:0000250"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5UK5"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:5UK5"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5UK5"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5UK5"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5UK5"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5UK5"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:5UK5"
SQ SEQUENCE 1219 AA; 134326 MW; 65D4CFC238A0E204 CRC64;
MRSPRTRGRP GRPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGARN
PGDRKCTRDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRGNDRNRI
VLPFSFAWPR SYTLLVEAWD SSNDTIQPDS IIEKASHSGM INPSRQWQTL KQNTGIAHFE
YQIRVTCDDH YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC MEGWMGPECN KAICRQGCSP
KHGSCKLPGD CRCQYGWQGL YCDKCIPHPG CVHGTCNEPW QCLCETNWGG QLCDKDLNYC
GTHQPCLNRG TCSNTGPDKY QCSCPEGYSG PNCEIAEHAC LSDPCHNRGS CKETSSGFEC
ECSPGWTGPT CSTNIDDCSP NNCSHGGTCQ DLVNGFKCVC PPQWTGKTCQ LDANECEAKP
CVNARSCKNL IASYYCDCLP GWMGQNCDIN INDCLGQCQN DASCRDLVNG YRCICPPGYA
GDHCERDIDE CASNPCLNGG HCQNEINRFQ CLCPTGFSGN LCQLDIDYCE PNPCQNGAQC
YNRASDYFCK CPEDYEGKNC SHLKDHCRTT PCEVIDSCTV AMASNDTPEG VRYISSNVCG
PHGKCKSESG GKFTCDCNKG FTGTYCHENI NDCEGNPCTN GGTCIDGVNS YKCICSDGWE
GAHCENNIND CSQNPCHYGG TCRDLVNDFY CDCKNGWKGK TCHSRDSQCD EATCNNGGTC
YDEVDTFKCM CPGGWEGTTC NIARNSSCLP NPCHNGGTCV VNGDSFTCVC KEGWEGPICT
QNTNDCSPHP CYNSGTCVDG DNWYRCECAP GFAGPDCRIN INECQSSPCA FGATCVDEIN
GYQCICPPGH SGAKCHEVSG RSCITMGRVI LDGAKWDDDC NTCQCLNGRV ACSKVWCGPR
PCRLHKGHGE CPNGQSCIPV LDDQCFVRPC TGAGECRSSS LQPVKTKCTS DSYYQDNCAN
ITFTFNKEMM SPGLTTEHIC SELRNLNILK NVSAEYSIYI ACEPSLSANN EIHVAISAED
IRDDGNPVKE ITDKIIDLVS KRDGNSSLIA AVAEVRVQRR PLKNRTDFLV PLLSSVLTVA
WVCCLVTAFY WCVRKRRRKP SSHTHSAPED NTTNNVREQL NQIKNPIEKH GANTVPIKDY
ENKNSKMSKI RTHNSEVEED DMDKHQQKVR FAKQPVYTLV DREEKVPQRT PTKHPNWTNK
QDNRDLESAQ SLNRMEYIV
