ID JAG1B_DANRE Reviewed; 1213 AA. AC Q90Y54; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Protein jagged-1b; DE Short=Jagged1b; DE AltName: Full=Jagged3; DE Flags: Precursor; GN Name=jag1b; Synonyms=jag3; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Oda T., Chandrasekharappa S.C.; RT "Isolation, characterization and expression analysis of zebrafish Jagged RT genes."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Ligand for Notch receptors and involved in the mediation of CC Notch signaling (By similarity). Seems to be involved in cell-fate CC decisions. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Cell membrane CC {ECO:0000250|UniProtKB:P78504}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF229451; AAL08216.1; -; mRNA. DR AlphaFoldDB; Q90Y54; -. DR SMR; Q90Y54; -. DR STRING; 7955.ENSDARP00000008197; -. DR GlyCosmos; Q90Y54; 7 sites, No reported glycans. DR PaxDb; 7955-ENSDARP00000008197; -. DR AGR; ZFIN:ZDB-GENE-011128-4; -. DR ZFIN; ZDB-GENE-011128-4; jag1b. DR eggNOG; KOG1217; Eukaryota. DR InParanoid; Q90Y54; -. DR PhylomeDB; Q90Y54; -. DR Reactome; R-DRE-9013149; RAC1 GTPase cycle. DR Reactome; R-DRE-9013423; RAC3 GTPase cycle. DR SignaLink; Q90Y54; -. DR PRO; PR:Q90Y54; -. DR Proteomes; UP000000437; Genome assembly. DR GO; GO:0016020; C:membrane; NAS:ZFIN. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005112; F:Notch binding; IBA:GO_Central. DR GO; GO:0060117; P:auditory receptor cell development; IMP:ZFIN. DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:ZFIN. DR GO; GO:1904888; P:cranial skeletal system development; IMP:ZFIN. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN. DR GO; GO:0031017; P:exocrine pancreas development; IGI:ZFIN. DR GO; GO:0060325; P:face morphogenesis; IMP:ZFIN. DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:ZFIN. DR GO; GO:0035622; P:intrahepatic bile duct development; IGI:ZFIN. DR GO; GO:0001889; P:liver development; IGI:ZFIN. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0032474; P:otolith morphogenesis; IMP:ZFIN. DR GO; GO:0031016; P:pancreas development; IGI:ZFIN. DR GO; GO:0060872; P:semicircular canal development; IMP:ZFIN. DR GO; GO:0048752; P:semicircular canal morphogenesis; IMP:ZFIN. DR GO; GO:0030878; P:thyroid gland development; IMP:ZFIN. 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; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1. DR PANTHER; PTHR24044:SF448; PROTEIN JAGGED-1; 1. DR Pfam; PF21700; DL-JAG_EGF-like; 1. DR Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 8. DR Pfam; PF07645; EGF_CA; 1. 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; 7. DR SUPFAM; SSF57603; FnI-like domain; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 2. 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 2: Evidence at transcript level; KW Calcium; Cell membrane; Developmental protein; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..1213 FT /note="Protein jagged-1b" FT /id="PRO_0000007631" FT TOPO_DOM 27..1064 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1065..1087 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1088..1213 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 182..226 FT /note="DSL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377" FT DOMAIN 227..260 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 261..291 FT /note="EGF-like 2; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 293..331 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 333..369 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 371..407 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 409..445 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 447..482 FT /note="EGF-like 7; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 484..520 FT /note="EGF-like 8; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 522..558 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 592..624 FT /note="EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 626..662 FT /note="EGF-like 11; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 664..700 FT /note="EGF-like 12; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 702..738 FT /note="EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 746..777 FT /note="EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 779..815 FT /note="EGF-like 15; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 817..853 FT /note="EGF-like 16; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 860..914 FT /note="VWFC" FT DOMAIN 918..956 FT /note="EGF-like 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 1181..1202 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1188..1202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 214 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 556 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 742 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 957 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 988 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1042 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 184..193 FT /evidence="ECO:0000250" FT DISULFID 197..209 FT /evidence="ECO:0000250" FT DISULFID 217..226 FT /evidence="ECO:0000250" FT DISULFID 231..242 FT /evidence="ECO:0000250" FT DISULFID 235..248 FT /evidence="ECO:0000250" FT DISULFID 250..259 FT /evidence="ECO:0000250" FT DISULFID 262..273 FT /evidence="ECO:0000250" FT DISULFID 268..279 FT /evidence="ECO:0000250" FT DISULFID 281..290 FT /evidence="ECO:0000250" FT DISULFID 297..309 FT /evidence="ECO:0000250" FT DISULFID 303..319 FT /evidence="ECO:0000250" FT DISULFID 321..330 FT /evidence="ECO:0000250" FT DISULFID 337..348 FT /evidence="ECO:0000250" FT DISULFID 342..357 FT /evidence="ECO:0000250" FT DISULFID 359..368 FT /evidence="ECO:0000250" FT DISULFID 375..386 FT /evidence="ECO:0000250" FT DISULFID 380..395 FT /evidence="ECO:0000250" FT DISULFID 397..406 FT /evidence="ECO:0000250" FT DISULFID 413..424 FT /evidence="ECO:0000250" FT DISULFID 418..433 FT /evidence="ECO:0000250" FT DISULFID 435..444 FT /evidence="ECO:0000250" FT DISULFID 451..461 FT /evidence="ECO:0000250" FT DISULFID 455..470 FT /evidence="ECO:0000250" FT DISULFID 472..481 FT /evidence="ECO:0000250" FT DISULFID 488..499 FT /evidence="ECO:0000250" FT DISULFID 493..508 FT /evidence="ECO:0000250" FT DISULFID 510..519 FT /evidence="ECO:0000250" FT DISULFID 526..537 FT /evidence="ECO:0000250" FT DISULFID 531..546 FT /evidence="ECO:0000250" FT DISULFID 548..557 FT /evidence="ECO:0000250" FT DISULFID 596..612 FT /evidence="ECO:0000250" FT DISULFID 614..623 FT /evidence="ECO:0000250" FT DISULFID 630..641 FT /evidence="ECO:0000250" FT DISULFID 635..650 FT /evidence="ECO:0000250" FT DISULFID 652..661 FT /evidence="ECO:0000250" FT DISULFID 668..679 FT /evidence="ECO:0000250" FT DISULFID 673..688 FT /evidence="ECO:0000250" FT DISULFID 690..699 FT /evidence="ECO:0000250" FT DISULFID 706..717 FT /evidence="ECO:0000250" FT DISULFID 711..726 FT /evidence="ECO:0000250" FT DISULFID 728..737 FT /evidence="ECO:0000250" FT DISULFID 745..756 FT /evidence="ECO:0000250" FT DISULFID 750..765 FT /evidence="ECO:0000250" FT DISULFID 767..776 FT /evidence="ECO:0000250" FT DISULFID 783..794 FT /evidence="ECO:0000250" FT DISULFID 788..803 FT /evidence="ECO:0000250" FT DISULFID 805..814 FT /evidence="ECO:0000250" FT DISULFID 821..832 FT /evidence="ECO:0000250" FT DISULFID 826..841 FT /evidence="ECO:0000250" FT DISULFID 843..852 FT /evidence="ECO:0000250" SQ SEQUENCE 1213 AA; 133366 MW; 5C5F16A7E20D9534 CRC64; MILRRSSVFS AFYLHAFLLC LRTTVSDASG HFELEILSMQ NANGELQNGA CCDGARNPAD RKCTRDECDT YFKVCLKEYQ SRVSSAGACS FGTGSTPVLG GNKFSTKGTR SEKSRIVLPF SFAWPRSYTL IVEALDFNNE TASESGKLIE KAYHSGMINP NRQWQRLTHN GPVAQFEYQI RVTCLEHYYG FGCNKFCRPR DEFFGHYTCD QNGNKTCLEG WTGPDCNTAI CRQGCSTEHG SCKQPGGCKC LYGWQGPYCD KCIPHPGCVH GTCVEPWQCL CDTNWGGQLC DKDLNYCGTH QPCLNGGTCS NTGPDKYQCS CEDGYSGVNC ERAEHACLSN PCANGGTCKE TSQGYECHCA IGWSGTSCEI NVDDCTPNQC KHGGTCQDLV NGFKCACPPH WTGKTCQIDA NECEDKPCVN AKSCHNLIGA YFCECLPGWS GQNCDININD CKGQCLNGGT CKDLVNGYRC LCPPGYTGEQ CEKDVDECAS SPCLNGGRCQ DEVNGFQCLC PAGFSGQLCQ LDIDYCKPNP CQNGAQCFNL ASDYFCKCPD DYEGKNCSHL KDHCRTTSCQ VIDSCTVAVA SNSTPEGVRY ISSNVCGPHG RCRSQAGGQF TCECQEGFRG TYCHENINDC ESNPCRNGGT CIDKVNVYQC ICADGWEGVH CEINIDDCSL NPCLNKGACQ DLVNDFYCEC RNGWKGKTCH SRDSQCDEAT CNNGGTCHDE GDTFKCRCSP GWEGATCNIA KNSSCLPNPC ENGGTCVVNG DSFNCVCKEG WEGSTCTENT NDCNPHPCYN SGTCVDGENW YRCECAPGFA GPDCRININE CQSSPCAFGS TCVDEINGYR CLCPPGRIGP DCQEVVGRPC IANGQVTADG AKWEEDCNIC QCQNGRIHCT MMWCGPKSCR IGKARGGCPA SQSCVPIKEE QCFVKPCPSL GECWPSAPPP PSKCHASFSY QDDSCANITF TFNKENMPQG LSVEHVCNEL RHWYLLKNLS TEYAVSISCE PSSSASNEIH ISISTEEPRT DRSPIKDITV QIIDLVSKHN GNSTIIKAIT GVRVHQIPSP KTDYLVPLLS SIFIVLWIFA LASAFLWCIH RRRKQNTHSN TATSATEDNT TNNVREQLNQ IKNPIEKHAA HGVPIKDYEG KNSIIAKIRT HNSEVEEEDM DKHLQKARFT KQPAYTLVER EERAPNKNPN WTNKQDNRDL ETAQSLNRME YIV //