JAG2_MOUSE
ID JAG2_MOUSE Reviewed; 1247 AA.
AC Q9QYE5; F8VPV5; O55139; O70219;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Protein jagged-2;
DE Short=Jagged2;
DE Flags: Precursor;
GN Name=Jag2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster / NIH;
RA Tsai S.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-819.
RC TISSUE=Brain;
RX PubMed=9341252; DOI=10.1007/s003359900642;
RA Lan Y., Jiang R., Shawber C., Weinmaster G., Gridley T.;
RT "The Jagged2 gene maps to chromosome 12 and is a candidate for the lgl and
RT sm mutations.";
RL Mamm. Genome 8:875-876(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-759.
RC TISSUE=Brain;
RX PubMed=9486542; DOI=10.1016/s0925-4773(97)00146-9;
RA Valsecchi C., Ghezzi C., Ballabio A., Rugarli E.I.;
RT "JAGGED2: a putative Notch ligand expressed in the apical ectodermal ridge
RT and in sites of epithelial-mesenchymal interactions.";
RL Mech. Dev. 69:203-207(1997).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9315665; DOI=10.1128/mcb.17.10.6057;
RA Luo B., Aster J.C., Hasserjian R.P., Kuo F., Sklar J.;
RT "Isolation and functional analysis of a cDNA for human Jagged2, a gene
RT encoding a ligand for the Notch1 receptor.";
RL Mol. Cell. Biol. 17:6057-6067(1997).
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. Plays an essential role during limb, craniofacial and thymic
CC development. May be involved in myogenesis and in the development of
CC peripheral and central nervous systems.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Found to be highest in fetal thymus, epidermis,
CC foregut dorsal root ganglia and inner ear. In 2-weeK-old mice, abundant
CC in heart, lung, thymus, skeletal muscle, brain and testis. Expression
CC overlaps partially with Notch1 expression.
CC {ECO:0000269|PubMed:9315665}.
CC -!- DEVELOPMENTAL STAGE: At 13 dpc, found in paravertebral vessels and
CC dorsal root ganglia. At 14 dpc, in oropharyngeal epithelium, developing
CC thymus and in the muscles of the tongue. By 15 dpc, in many tissues.
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DR EMBL; AF038572; AAF16411.1; -; mRNA.
DR EMBL; AC160929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF010137; AAC14010.1; -; mRNA.
DR EMBL; Y14495; CAA74835.1; -; mRNA.
DR CCDS; CCDS26200.1; -.
DR RefSeq; NP_034718.2; NM_010588.2.
DR AlphaFoldDB; Q9QYE5; -.
DR SMR; Q9QYE5; -.
DR BioGRID; 200855; 4.
DR STRING; 10090.ENSMUSP00000075224; -.
DR GlyGen; Q9QYE5; 5 sites.
DR iPTMnet; Q9QYE5; -.
DR PhosphoSitePlus; Q9QYE5; -.
DR MaxQB; Q9QYE5; -.
DR PaxDb; Q9QYE5; -.
DR PeptideAtlas; Q9QYE5; -.
DR PRIDE; Q9QYE5; -.
DR ProteomicsDB; 269113; -.
DR Antibodypedia; 14930; 455 antibodies from 38 providers.
DR DNASU; 16450; -.
DR Ensembl; ENSMUST00000075827; ENSMUSP00000075224; ENSMUSG00000002799.
DR GeneID; 16450; -.
DR KEGG; mmu:16450; -.
DR UCSC; uc007pfl.1; mouse.
DR CTD; 3714; -.
DR MGI; MGI:1098270; Jag2.
DR VEuPathDB; HostDB:ENSMUSG00000002799; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160944; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR InParanoid; Q9QYE5; -.
DR OMA; YGWQGKF; -.
DR OrthoDB; 72177at2759; -.
DR PhylomeDB; Q9QYE5; -.
DR TreeFam; TF351835; -.
DR Reactome; R-MMU-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR BioGRID-ORCS; 16450; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9QYE5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QYE5; protein.
DR Bgee; ENSMUSG00000002799; Expressed in lip and 257 other tissues.
DR ExpressionAtlas; Q9QYE5; baseline and differential.
DR Genevisible; Q9QYE5; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; ISO:MGI.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:1990134; P:epithelial cell apoptotic process involved in palatal shelf morphogenesis; IMP:MGI.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; NAS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; ISO:MGI.
DR GO; GO:0030217; P:T cell differentiation; ISO:MGI.
DR GO; GO:0045061; P:thymic T cell selection; ISS: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; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 3.
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; SM00215; VWC_out; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 16.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 7.
PE 2: Evidence at transcript level;
KW Calcium; Developmental protein; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Notch signaling pathway; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1247
FT /note="Protein jagged-2"
FT /id="PRO_0000007630"
FT TOPO_DOM 24..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 196..240
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 241..274
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 275..305
FT /note="EGF-like 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 307..345
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 347..383
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 385..421
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 423..459
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 461..496
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 498..534
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 536..572
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 574..634
FT /note="EGF-like 10; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 636..672
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 674..710
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 712..748
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 751..787
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 789..825
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 827..863
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1115..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y219"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1060
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 198..207
FT /evidence="ECO:0000250"
FT DISULFID 211..223
FT /evidence="ECO:0000250"
FT DISULFID 231..240
FT /evidence="ECO:0000250"
FT DISULFID 245..256
FT /evidence="ECO:0000250"
FT DISULFID 249..262
FT /evidence="ECO:0000250"
FT DISULFID 264..273
FT /evidence="ECO:0000250"
FT DISULFID 276..287
FT /evidence="ECO:0000250"
FT DISULFID 282..293
FT /evidence="ECO:0000250"
FT DISULFID 295..304
FT /evidence="ECO:0000250"
FT DISULFID 311..323
FT /evidence="ECO:0000250"
FT DISULFID 317..333
FT /evidence="ECO:0000250"
FT DISULFID 335..344
FT /evidence="ECO:0000250"
FT DISULFID 351..362
FT /evidence="ECO:0000250"
FT DISULFID 356..371
FT /evidence="ECO:0000250"
FT DISULFID 373..382
FT /evidence="ECO:0000250"
FT DISULFID 389..400
FT /evidence="ECO:0000250"
FT DISULFID 394..409
FT /evidence="ECO:0000250"
FT DISULFID 411..420
FT /evidence="ECO:0000250"
FT DISULFID 427..438
FT /evidence="ECO:0000250"
FT DISULFID 432..447
FT /evidence="ECO:0000250"
FT DISULFID 449..458
FT /evidence="ECO:0000250"
FT DISULFID 465..475
FT /evidence="ECO:0000250"
FT DISULFID 469..484
FT /evidence="ECO:0000250"
FT DISULFID 486..495
FT /evidence="ECO:0000250"
FT DISULFID 502..513
FT /evidence="ECO:0000250"
FT DISULFID 507..522
FT /evidence="ECO:0000250"
FT DISULFID 524..533
FT /evidence="ECO:0000250"
FT DISULFID 540..551
FT /evidence="ECO:0000250"
FT DISULFID 545..560
FT /evidence="ECO:0000250"
FT DISULFID 562..571
FT /evidence="ECO:0000250"
FT DISULFID 589..612
FT /evidence="ECO:0000255"
FT DISULFID 606..622
FT /evidence="ECO:0000255"
FT DISULFID 624..633
FT /evidence="ECO:0000250"
FT DISULFID 640..651
FT /evidence="ECO:0000250"
FT DISULFID 645..660
FT /evidence="ECO:0000250"
FT DISULFID 662..671
FT /evidence="ECO:0000250"
FT DISULFID 678..689
FT /evidence="ECO:0000250"
FT DISULFID 683..698
FT /evidence="ECO:0000250"
FT DISULFID 700..709
FT /evidence="ECO:0000250"
FT DISULFID 716..727
FT /evidence="ECO:0000250"
FT DISULFID 721..736
FT /evidence="ECO:0000250"
FT DISULFID 738..747
FT /evidence="ECO:0000250"
FT DISULFID 755..766
FT /evidence="ECO:0000250"
FT DISULFID 760..775
FT /evidence="ECO:0000250"
FT DISULFID 777..786
FT /evidence="ECO:0000250"
FT DISULFID 793..804
FT /evidence="ECO:0000250"
FT DISULFID 798..813
FT /evidence="ECO:0000250"
FT DISULFID 815..824
FT /evidence="ECO:0000250"
FT DISULFID 831..842
FT /evidence="ECO:0000250"
FT DISULFID 836..851
FT /evidence="ECO:0000250"
FT DISULFID 853..862
FT /evidence="ECO:0000250"
FT CONFLICT 302
FT /note="L -> M (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="N -> S (in Ref. 1; AAF16411, 3; AAC14010 and 4;
FT CAA74835)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="N -> T (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..478
FT /note="CQHGGTCKDL -> VSAWGHLQGP (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="G -> V (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="L -> F (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="A -> V (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..738
FT /note="RCAC -> PAR (in Ref. 4; CAA74835)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="N -> H (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="R -> A (in Ref. 3; AAC14010)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="V -> M (in Ref. 1; AAF16411)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="A -> T (in Ref. 1; AAF16411)"
FT /evidence="ECO:0000305"
FT CONFLICT 1223
FT /note="R -> C (in Ref. 1; AAF16411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1247 AA; 134745 MW; E1352B1856946EA6 CRC64;
MRARGWGRLP RRLLLLLVLC VQATRPMGYF ELQLSALRNV NGELLSGACC DGDGRTTRAG
GCGRDECDTY VRVCLKEYQA KVTPTGPCSY GYGATPVLGG NSFYLPPAGA AGDRARARSR
TGGHQDPGLV VIPFQFAWPR SFTLIVEAWD WDNDTTPDEE LLIERVSHAG MINPEDRWKS
LHFSGHVAHL ELQIRVRCDE NYYSATCNKF CRPRNDFFGH YTCDQYGNKA CMDGWMGKEC
KEAVCKQGCN LLHGGCTVPG ECRCSYGWQG KFCDECVPYP GCVHGSCVEP WHCDCETNWG
GLLCDKDLNY CGSHHPCVNG GTCINAEPDQ YLCACPDGYL GKNCERAEHA CASNPCANGG
SCHEVPSGFE CHCPSGWNGP TCALDIDECA SNPCAAGGTC VDQVDGFECI CPEQWVGATC
QLDANECEGK PCLNAFSCKN LIGGYYCDCL PGWKGINCQI NINDCHGQCQ HGGTCKDLVN
GYQCVCPRGF GGRHCELEYD KCASSPCRRG GICEDLVDGF RCHCPRGLSG LHCEVDMDLC
EPSPCLNGAR CYNLEGDYYC ACPEDFGGKN CSVPRDTCPG GACRVIDGCG FEAGSRARGV
APSGICGPHG HCVSLPGGNF SCICDSGFTG TYCHENIDDC MGQPCRNGGT CIDEVDSFRC
FCPSGWEGEL CDINPNDCLP DPCHSRGRCY DLVNDFYCAC DDGWKGKTCH SREFQCDAYT
CSNGGTCYDS GDTFRCACPP GWKGSTCTIA KNSSCVPNPC VNGGTCVGSG DSFSCICRDG
WEGRTCTHNT NDCNPLPCYN GGICVDGVNW FRCECAPGFA GPDCRINIDE CQSSPCAYGA
TCVDEINGYR CSCPPGRSGP RCQEVVIFTR PCWSRGMSFP HGSSWMEDCN SCRCLDGHRD
CSKVWCGWKP CLLSGQPSDP SAQCPPGQQC QEKAVGQCLQ PPCENWGECT AEEPLPPSTP
CQPRSSHLDN NCARLTLRFN RDQVPQGTTV GAICSGIRAL PATRAAAHDR LLLLLCDRAS
SGASAVEVAV SFSPARDLPD SSLIQSTAHA IVAAITQRGN SSLLLAVTEV KVETVVMGGS
STGLLVPVLC SVFSVLWLAC VVICVWWTRK RRKERERSRL PRDESANNQW APLNPIRNPI
ERPGGSGLGT GGHKDILYQC KNFTPPPRRA GEALPGPAGH GAGGEDEEDE ELSRGDGDSP
EAEKFISHKF TKDPSCSLGR PARWAPGPKV DNRAVRSTKD VRRAGRE
