GenomeNet

Database: UniProt
Entry: Q9QXX0
LinkDB: Q9QXX0
Original site: Q9QXX0 
ID   JAG1_MOUSE              Reviewed;        1218 AA.
AC   Q9QXX0;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-FEB-2019, entry version 177.
DE   RecName: Full=Protein jagged-1;
DE            Short=Jagged1;
DE   AltName: CD_antigen=CD339;
DE   Flags: Precursor;
GN   Name=Jag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NOTHC1; NOTHC2 AND
RP   NOTCH3.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=10551863; DOI=10.1074/jbc.274.46.32961;
RA   Shimizu K., Chiba S., Kumano K., Hosoya N., Takahashi T., Kanda Y.,
RA   Hamada Y., Yazaki Y., Hirai H.;
RT   "Mouse Jagged1 physically interacts with Notch2 and other Notch
RT   receptors: assessment by quantitative methods.";
RL   J. Biol. Chem. 274:32961-32969(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=10556292; DOI=10.1093/hmg/8.13.2443;
RA   Loomes K.M., Underkoffler L.A., Morabito J., Gottlieb S.,
RA   Piccoli D.A., Spinner N.B., Baldwin H.S., Oakey R.J.;
RT   "The expression of Jagged1 in the developing mammalian heart
RT   correlates with cardiovascular disease in Alagille syndrome.";
RL   Hum. Mol. Genet. 8:2443-2449(1999).
CC   -!- FUNCTION: Ligand for multiple Notch receptors and involved in the
CC       mediation of Notch signaling. May be involved in cell-fate
CC       decisions during hematopoiesis. Seems to be involved in early and
CC       late stages of mammalian cardiovascular development. Inhibits
CC       myoblast differentiation (By similarity). May regulate fibroblast
CC       growth factor-induced angiogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NOTCH1, NOTCH2 and NOTCH3.
CC       {ECO:0000269|PubMed:10551863}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed in many tissues, with highest
CC       expression in brain, heart, muscle and thymus.
CC       {ECO:0000269|PubMed:10556292}.
CC   -!- DEVELOPMENTAL STAGE: At 8.75-9.75 dpc expression was detected in
CC       structures that include those destined to contribute to the
CC       cardiovascular system of the adult heart. Expression was also
CC       detected in the mesencephalon and rhombencephalon.
CC   -!- DOMAIN: The DSL domain is indispensable and sufficient for binding
CC       to NOTCH2.
DR   EMBL; AF171092; AAF15505.1; -; mRNA.
DR   EMBL; BC058675; AAH58675.1; -; mRNA.
DR   CCDS; CCDS16797.1; -.
DR   RefSeq; NP_038850.1; NM_013822.5.
DR   UniGene; Mm.22398; -.
DR   ProteinModelPortal; Q9QXX0; -.
DR   SMR; Q9QXX0; -.
DR   BioGrid; 200854; 1.
DR   STRING; 10090.ENSMUSP00000028735; -.
DR   iPTMnet; Q9QXX0; -.
DR   PhosphoSitePlus; Q9QXX0; -.
DR   SwissPalm; Q9QXX0; -.
DR   jPOST; Q9QXX0; -.
DR   MaxQB; Q9QXX0; -.
DR   PaxDb; Q9QXX0; -.
DR   PRIDE; Q9QXX0; -.
DR   Ensembl; ENSMUST00000028735; ENSMUSP00000028735; ENSMUSG00000027276.
DR   GeneID; 16449; -.
DR   KEGG; mmu:16449; -.
DR   UCSC; uc008moz.2; mouse.
DR   CTD; 182; -.
DR   MGI; MGI:1095416; Jag1.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00940000160148; -.
DR   HOGENOM; HOG000113124; -.
DR   HOVERGEN; HBG031645; -.
DR   InParanoid; Q9QXX0; -.
DR   KO; K06052; -.
DR   OMA; KRSINCK; -.
DR   OrthoDB; 72177at2759; -.
DR   PhylomeDB; Q9QXX0; -.
DR   TreeFam; TF351835; -.
DR   Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   ChiTaRS; Jag1; mouse.
DR   PRO; PR:Q9QXX0; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027276; Expressed in 384 organ(s), highest expression level in pineal body.
DR   ExpressionAtlas; Q9QXX0; baseline and differential.
DR   Genevisible; Q9QXX0; MM.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0035909; P:aorta morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060411; P:cardiac septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0061073; P:ciliary body morphogenesis; IMP:MGI.
DR   GO; GO:0072017; P:distal tubule development; IEP:UniProtKB.
DR   GO; GO:0061444; P:endocardial cushion cell development; IMP:BHF-UCL.
DR   GO; GO:0072015; P:glomerular visceral epithelial cell development; IMP:UniProtKB.
DR   GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
DR   GO; GO:0072070; P:loop of Henle development; IEP:UniProtKB.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:MGI.
DR   GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IDA:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
DR   GO; GO:0002456; P:T cell mediated immunity; ISO:MGI.
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   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; 15.
DR   PROSITE; PS01187; EGF_CA; 8.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34   1218       Protein jagged-1.
FT                                /FTId=PRO_0000007626.
FT   TOPO_DOM     34   1067       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1068   1093       Helical. {ECO:0000255}.
FT   TOPO_DOM   1094   1218       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      185    229       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      230    263       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      264    294       EGF-like 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      296    334       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      336    372       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      374    410       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      412    448       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      450    485       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      487    523       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      525    561       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      586    627       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      629    665       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      667    703       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      705    741       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      744    780       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      782    818       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      820    856       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION      199    207       Important for interaction with NOTCH1.
FT                                {ECO:0000250}.
FT   CARBOHYD    143    143       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    382    382       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    559    559       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    745    745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    960    960       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    991    991       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1045   1045       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1064   1064       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    187    196       {ECO:0000250}.
FT   DISULFID    200    212       {ECO:0000250}.
FT   DISULFID    220    229       {ECO:0000250}.
FT   DISULFID    234    245       {ECO:0000250}.
FT   DISULFID    238    251       {ECO:0000250}.
FT   DISULFID    253    262       {ECO:0000250}.
FT   DISULFID    265    276       {ECO:0000250}.
FT   DISULFID    271    282       {ECO:0000250}.
FT   DISULFID    284    293       {ECO:0000250}.
FT   DISULFID    300    312       {ECO:0000250}.
FT   DISULFID    306    322       {ECO:0000250}.
FT   DISULFID    324    333       {ECO:0000250}.
FT   DISULFID    340    351       {ECO:0000250}.
FT   DISULFID    345    360       {ECO:0000250}.
FT   DISULFID    362    371       {ECO:0000250}.
FT   DISULFID    378    389       {ECO:0000250}.
FT   DISULFID    383    398       {ECO:0000250}.
FT   DISULFID    400    409       {ECO:0000250}.
FT   DISULFID    416    427       {ECO:0000250}.
FT   DISULFID    421    436       {ECO:0000250}.
FT   DISULFID    438    447       {ECO:0000250}.
FT   DISULFID    454    464       {ECO:0000250}.
FT   DISULFID    458    473       {ECO:0000250}.
FT   DISULFID    475    484       {ECO:0000250}.
FT   DISULFID    491    502       {ECO:0000250}.
FT   DISULFID    496    511       {ECO:0000250}.
FT   DISULFID    513    522       {ECO:0000250}.
FT   DISULFID    529    540       {ECO:0000250}.
FT   DISULFID    534    549       {ECO:0000250}.
FT   DISULFID    551    560       {ECO:0000250}.
FT   DISULFID    578    605       {ECO:0000250}.
FT   DISULFID    599    615       {ECO:0000250}.
FT   DISULFID    617    626       {ECO:0000250}.
FT   DISULFID    633    644       {ECO:0000250}.
FT   DISULFID    638    653       {ECO:0000250}.
FT   DISULFID    655    664       {ECO:0000250}.
FT   DISULFID    671    682       {ECO:0000250}.
FT   DISULFID    676    691       {ECO:0000250}.
FT   DISULFID    693    702       {ECO:0000250}.
FT   DISULFID    709    720       {ECO:0000250}.
FT   DISULFID    714    729       {ECO:0000250}.
FT   DISULFID    731    740       {ECO:0000250}.
FT   DISULFID    748    759       {ECO:0000250}.
FT   DISULFID    753    768       {ECO:0000250}.
FT   DISULFID    770    779       {ECO:0000250}.
FT   DISULFID    786    797       {ECO:0000250}.
FT   DISULFID    791    806       {ECO:0000250}.
FT   DISULFID    808    817       {ECO:0000250}.
FT   DISULFID    824    835       {ECO:0000250}.
FT   DISULFID    829    844       {ECO:0000250}.
FT   DISULFID    846    855       {ECO:0000250}.
SQ   SEQUENCE   1218 AA;  134164 MW;  77739F8928BB793C CRC64;
     MRSPRTRGRP GRPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGVRN
     PGDRKCTRDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRGNDRNRI
     VLPFSFAWPR SYTLLVEAWD SSNDTIQPDS IIEKASHSGM INPSRQWQTL KQNTGIAHFE
     YQIRVTCDDH YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC MEGWMGPDCN 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 TCEVIDSCTV AMASNDTPEG VRYISSNVCG
     PHGKCKSQSG GKFTCDCNKG FTGTYCHENI NDCESNPCKN 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
     PCRLHKSHNE CPSGQSCIPV LDDQCFVRPC TGVGECRSSS LQPVKTKCTS DSYYQDNCAN
     ITFTFNKEMM SPGLTTEHIC SELRNLNILK NVSAEYSIYI ACEPSLSANN EIHVAISAED
     IRDDGNPVKE ITDKIIDLVS KRDGNSSLIA AVAEVRVQRR PLKNRTDFLV PLLSSVLTVA
     WVCCLVTAFY WCVRKRRKPS SHTHSAPEDN TTNNVREQLN QIKNPIEKHG ANTVPIKDYE
     NKNSKMSKIR THNSEVEEDD MDKHQQKVRF AKQPVYTLVD REEKAPSGTP TKHPNWTNKQ
     DNRDLESAQS LNRMEYIV
//
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