JAG2_RAT
ID JAG2_RAT Reviewed; 1202 AA.
AC P97607;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Protein jagged-2;
DE Short=Jagged2;
DE Flags: Fragment;
GN Name=Jag2;
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=Brain;
RX PubMed=8948600; DOI=10.1006/dbio.1996.0310;
RA Shawber C., Boulter J., Lindsell C.E., Weinmaster G.;
RT "Jagged2: a serrate-like gene expressed during rat embryogenesis.";
RL Dev. Biol. 180:370-376(1996).
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. May have a role in neurogenesis in the peripheral nervous
CC system, limb development and in the adult brain.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: At stage E12.5 it is detected in dorsal root
CC ganglia, AER, and surface ectoderm. At E14.5, found as well in cranial
CC ganglia, thymus and olfactory epithelia. At E16.5, found as well in
CC salivary gland, tooth buds and hair follicles.
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DR EMBL; U70050; AAC52946.1; -; mRNA.
DR AlphaFoldDB; P97607; -.
DR SMR; P97607; -.
DR STRING; 10116.ENSRNOP00000019213; -.
DR GlyGen; P97607; 5 sites.
DR jPOST; P97607; -.
DR PaxDb; P97607; -.
DR PRIDE; P97607; -.
DR UCSC; RGD:2938; rat.
DR RGD; 2938; Jag2.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P97607; -.
DR PhylomeDB; P97607; -.
DR Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0009912; P:auditory receptor cell fate commitment; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0030326; P:embryonic limb morphogenesis; NAS:UniProtKB.
DR GO; GO:1990134; P:epithelial cell apoptotic process involved in palatal shelf morphogenesis; ISO:RGD.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; TAS:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0003016; P:respiratory system process; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045061; P:thymic T cell selection; ISS:UniProtKB.
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; 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; 15.
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; Transmembrane; Transmembrane helix.
FT CHAIN <1..1202
FT /note="Protein jagged-2"
FT /id="PRO_0000055632"
FT TOPO_DOM <1..1037
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 150..194
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 195..228
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 229..259
FT /note="EGF-like 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 261..299
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 301..337
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 339..375
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 377..413
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 415..450
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 452..488
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 490..527
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 529..589
FT /note="EGF-like 10; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 591..627
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 629..665
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 667..703
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 706..742
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 744..780
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 782..818
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1070..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y219"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..161
FT /evidence="ECO:0000250"
FT DISULFID 165..177
FT /evidence="ECO:0000250"
FT DISULFID 185..194
FT /evidence="ECO:0000250"
FT DISULFID 199..210
FT /evidence="ECO:0000250"
FT DISULFID 203..216
FT /evidence="ECO:0000250"
FT DISULFID 218..227
FT /evidence="ECO:0000250"
FT DISULFID 230..241
FT /evidence="ECO:0000250"
FT DISULFID 236..247
FT /evidence="ECO:0000250"
FT DISULFID 249..258
FT /evidence="ECO:0000250"
FT DISULFID 265..277
FT /evidence="ECO:0000250"
FT DISULFID 271..287
FT /evidence="ECO:0000250"
FT DISULFID 289..298
FT /evidence="ECO:0000250"
FT DISULFID 305..316
FT /evidence="ECO:0000250"
FT DISULFID 310..325
FT /evidence="ECO:0000250"
FT DISULFID 327..336
FT /evidence="ECO:0000250"
FT DISULFID 343..354
FT /evidence="ECO:0000250"
FT DISULFID 348..363
FT /evidence="ECO:0000250"
FT DISULFID 365..374
FT /evidence="ECO:0000250"
FT DISULFID 381..392
FT /evidence="ECO:0000250"
FT DISULFID 386..401
FT /evidence="ECO:0000250"
FT DISULFID 403..412
FT /evidence="ECO:0000250"
FT DISULFID 419..429
FT /evidence="ECO:0000250"
FT DISULFID 423..438
FT /evidence="ECO:0000250"
FT DISULFID 440..449
FT /evidence="ECO:0000250"
FT DISULFID 456..467
FT /evidence="ECO:0000250"
FT DISULFID 461..476
FT /evidence="ECO:0000250"
FT DISULFID 478..487
FT /evidence="ECO:0000250"
FT DISULFID 495..506
FT /evidence="ECO:0000250"
FT DISULFID 500..515
FT /evidence="ECO:0000250"
FT DISULFID 517..526
FT /evidence="ECO:0000250"
FT DISULFID 544..567
FT /evidence="ECO:0000255"
FT DISULFID 561..577
FT /evidence="ECO:0000255"
FT DISULFID 579..588
FT /evidence="ECO:0000250"
FT DISULFID 595..606
FT /evidence="ECO:0000250"
FT DISULFID 600..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 710..721
FT /evidence="ECO:0000250"
FT DISULFID 715..730
FT /evidence="ECO:0000250"
FT DISULFID 732..741
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 NON_TER 1
SQ SEQUENCE 1202 AA; 129705 MW; 08CB44E5271FF8BE CRC64;
GACCDGDGRT TRAGGCGRDE CDTYVRVCLK EYQAKVTPTG PCSYGYGATP VLGSNSFYLP
PAGAAGDRAR ARSRTGGHQD PGLVVIPFQF AWPRSFTLIV EAWDWDNDTT PDEELLIERV
SHAGMINPED RWKSLHFSGH VAHLELQIRV RCDENYYSAT CNKFCRPRND FFGHYTCDQY
GNKACMDGWM GKECKEAVCK QGCNLLHGGC TVPGECRCSY GWQGKFCDEC VPYPGCVHGS
CVEPWHCDCE TNWGGLLCDK DLNYCGSHHP CVNGGTCINA EPDQYLCACP DGYLGKNCER
AEHACASNPC ANGGSCHEVL SGFECHCPSG WSGPTCALDI DECASNPCAA GGTCVDQVDG
FECICPEQWV GATCQLDANE CEGKPCLNAF SCKNLIGGYY CDCLPGWKGA NCHININDCH
GQCQHGGTCK DLVNGYQCVC PRGFGGRHCE LEYYKCASSP CRRGGICEDL VDGFRCHCPR
GLSGPLCEVD VDLWCEPNPC LNGARCYNLE DDYYCACPED FGGKNCSVPR ETCPGGACRV
IDGCGFEAGS RAHGAAPSGV CGPHGHCVSL PGGNFSCICD SGFTGTYCHE NIDDCMGQPC
RNGGTCIDEV DSFACFCPSG WEGELCDINP NDCLPDPCHS RGRCYDLVND FYCVCDDGWK
DKTCHSREFQ CDAYTCSNGG TCYDSGDTFR CACPPGWKGS TCTIAKNSSC VPNPCVNGGT
CVGSGDSFSC ICRDGWEGRT CTHNTNDCNP LPCYNGGICV DGVNWFRCEC APGFAGPDCR
INIDECQSSP CAYGATCVDE INGYRCSCPP GRSGPRCQEV VIFTRPCWSR GVSFPHGSSW
VEDCNSCRCL DGHRDCSKVW CGWKPCLLSP QPSALSAQCP PGQQCREKAM GQCLQPPCEN
WGECTAEDPL PPSTPCLPRT THLDNNCARL TLHFNRDQVP QGTTVGAICS GIRALPATRA
AARDRLLLLL CDRASSGASA VEVAVSFSPA RDLPDSSLIQ STAHAIVAAI TQRGNSSLLL
AVTEVKVETV VMGGSSTGLL VPVLCSVFSV LWLACMVICV WWTRKRRKER ERSRLPRDES
ANNQWAPLNP IRNPIERPGS SGLGTGGHKD VLYQCKNFTP PPRRAGEALP GPASHGAGGE
DEEDEELSRG DGRLSRSREV PLTQIHQRPQ LLPGKASLLA PGPKVDNRAV RSTKDVRCAG
RE
