JAG1A_DANRE
ID JAG1A_DANRE Reviewed; 1242 AA.
AC Q90Y57;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein jagged-1a;
DE Short=Jagged1;
DE Short=Jagged1a;
DE Flags: Precursor;
GN Name=jag1a; Synonyms=jag1;
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 multiple Notch receptors and involved in the
CC mediation of Notch signaling (By similarity). Seems to be involved in
CC cell-fate decisions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P78504}.
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DR EMBL; AF229448; AAL08213.1; -; mRNA.
DR RefSeq; NP_571936.1; NM_131861.1.
DR AlphaFoldDB; Q90Y57; -.
DR SMR; Q90Y57; -.
DR STRING; 7955.ENSDARP00000121170; -.
DR PaxDb; Q90Y57; -.
DR GeneID; 140421; -.
DR KEGG; dre:140421; -.
DR CTD; 140421; -.
DR ZFIN; ZDB-GENE-011128-2; jag1a.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q90Y57; -.
DR SignaLink; Q90Y57; -.
DR PRO; PR:Q90Y57; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; NAS:ZFIN.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030878; P:thyroid gland development; IMP:ZFIN.
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; 2.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 11.
DR Pfam; PF12661; hEGF; 2.
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; 9.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1242
FT /note="Protein jagged-1a"
FT /id="PRO_0000007628"
FT TOPO_DOM 29..1070
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 186..230
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 231..264
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 265..295
FT /note="EGF-like 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 297..335
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 337..373
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 375..411
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 413..449
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 451..486
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 488..524
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 526..562
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 575..630
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 632..668
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 670..706
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 708..744
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 747..783
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 785..821
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 823..859
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 917..959
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1191..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
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 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 188..197
FT /evidence="ECO:0000250"
FT DISULFID 201..213
FT /evidence="ECO:0000250"
FT DISULFID 221..230
FT /evidence="ECO:0000250"
FT DISULFID 235..246
FT /evidence="ECO:0000250"
FT DISULFID 239..252
FT /evidence="ECO:0000250"
FT DISULFID 254..263
FT /evidence="ECO:0000250"
FT DISULFID 266..277
FT /evidence="ECO:0000250"
FT DISULFID 272..283
FT /evidence="ECO:0000250"
FT DISULFID 285..294
FT /evidence="ECO:0000250"
FT DISULFID 301..313
FT /evidence="ECO:0000250"
FT DISULFID 307..323
FT /evidence="ECO:0000250"
FT DISULFID 325..334
FT /evidence="ECO:0000250"
FT DISULFID 341..352
FT /evidence="ECO:0000250"
FT DISULFID 346..361
FT /evidence="ECO:0000250"
FT DISULFID 363..372
FT /evidence="ECO:0000250"
FT DISULFID 379..390
FT /evidence="ECO:0000250"
FT DISULFID 384..399
FT /evidence="ECO:0000250"
FT DISULFID 401..410
FT /evidence="ECO:0000250"
FT DISULFID 417..428
FT /evidence="ECO:0000250"
FT DISULFID 422..437
FT /evidence="ECO:0000250"
FT DISULFID 439..448
FT /evidence="ECO:0000250"
FT DISULFID 455..465
FT /evidence="ECO:0000250"
FT DISULFID 459..474
FT /evidence="ECO:0000250"
FT DISULFID 476..485
FT /evidence="ECO:0000250"
FT DISULFID 492..503
FT /evidence="ECO:0000250"
FT DISULFID 497..512
FT /evidence="ECO:0000250"
FT DISULFID 514..523
FT /evidence="ECO:0000250"
FT DISULFID 530..541
FT /evidence="ECO:0000250"
FT DISULFID 535..550
FT /evidence="ECO:0000250"
FT DISULFID 552..561
FT /evidence="ECO:0000250"
FT DISULFID 600..618
FT /evidence="ECO:0000250"
FT DISULFID 620..629
FT /evidence="ECO:0000250"
FT DISULFID 636..647
FT /evidence="ECO:0000250"
FT DISULFID 641..656
FT /evidence="ECO:0000250"
FT DISULFID 658..667
FT /evidence="ECO:0000250"
FT DISULFID 674..685
FT /evidence="ECO:0000250"
FT DISULFID 679..694
FT /evidence="ECO:0000250"
FT DISULFID 696..705
FT /evidence="ECO:0000250"
FT DISULFID 712..723
FT /evidence="ECO:0000250"
FT DISULFID 717..732
FT /evidence="ECO:0000250"
FT DISULFID 734..743
FT /evidence="ECO:0000250"
FT DISULFID 751..762
FT /evidence="ECO:0000250"
FT DISULFID 756..771
FT /evidence="ECO:0000250"
FT DISULFID 773..782
FT /evidence="ECO:0000250"
FT DISULFID 789..800
FT /evidence="ECO:0000250"
FT DISULFID 794..809
FT /evidence="ECO:0000250"
FT DISULFID 811..820
FT /evidence="ECO:0000250"
FT DISULFID 827..838
FT /evidence="ECO:0000250"
FT DISULFID 832..847
FT /evidence="ECO:0000250"
FT DISULFID 849..858
FT /evidence="ECO:0000250"
SQ SEQUENCE 1242 AA; 135343 MW; 59557A4B7F052860 CRC64;
MILRPSATFA ALSAHVLLRC LWMRVCEASG HFEMQVLSMQ NVNGELQSGA CCDGARDPAE
RSCAADQCDT FFRVCLKEYQ SRVSSGGPCS YGSGSTPVIG GNTFSVKPLD QTNDKTRIVL
PFSFAWPRSY TLIVEALDFN NDSSTGSING QVIEKAVQSG MINPNRQWQV LKHNGPVAQF
QYQIRVTCDE HYFGFGCNKF CRPRDDFFGH YTCDHNGNKT CLEGWAGPEC NTAICKQGCS
IEHGSCKVPG NCRCLYGWQG EYCDQCIPHP GCVHGTCIEP WQCLCDTNWG GQLCDKDLNT
CGTLQPCLNG GTCSNTGPDK YHCACPDGYS GQNCERADNA CLSEPCLNGG LCVESSLGFE
CQCAAGWTGP SCNINEDDCS PNPCNHSGVC VDLVDGFKCI CPVQWTGKTC LIDANECEES
PCVNAHSCRN LIGGYFCECL PGWTGQNCDI NVNDCHGQCL NGGLCKDLVN GYRCVCAAGF
AGDRCERDVD ECASRPCLNG GRCQDTLNGF QCLCPPGFSG ATCQLDLDYC ESGPCQNGAQ
CFSLASDYYC KCPEDYEGKN CSQLKDHCLI TPCQVIDSCT VAVVSNSTPG GLRLISSSVC
GPHGRCRSHS HAGGHFSCDC QDGFTGTYCH ENINDCESSP CLSGGTCIDK INAYQCICAD
GWEGPNCETN IDDCRTNPCR DRGVCRDLVN DFYCECENGW KGKTCHSRES QCDEDTCNNG
GTCSDEGDSF KCLCSPGWEG ATCNIAKNSS CLPNPCENGA TCVVTGDGFT CVCKEGWEGP
TCSQNSNDCN PQPCYNSGTC VDGDNWYRCE CASGFAGPDC RININECQSS PCAFGSTCVD
EINGYRCLCP PGRTGPRCQE VTGRPCVIGG RIAVDGAKWA EDCNTCYCHK GIVTCTKLFC
GPKACRMLGS GRGDCPTGQL CVPVRDEQCF VKPCSSQGEC WSAHRPAVRT HCQPDSHCAN
VTFTFNKDTM PQGVTVEQVC RELRHLYVTK NVTSEFSISV SCELSSAASN EIHVAIHVTE
NGIHGRVPVK EITDNIIDLV SKHSANSSVI GSIAEVRVQR KQPQNPNVDY MVPLLVSVVT
AIWVLALASV FLWCIRHHRK QSSSATAINP TSPFSTPEEN TANNAREHLN QIKNHIEKNA
SNGSLPGKEL HCDDKNTVNA KIRTQFPESD ASRRLQKTRF PHQPAYMLVD RDDRLSSNGT
DIKKHPQWTN KRDNRDLESQ HRVPDSQHRD SQHSLQKMEY IV
