GenomeNet

Database: UniProt
Entry: Q90Y57
LinkDB: Q90Y57
Original site: Q90Y57 
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   19-FEB-2014, entry version 103.
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   Cyprinidae; 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
RT   Jagged 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
CC       in cell-fate decisions.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains 1 DSL domain.
CC   -!- SIMILARITY: Contains 17 EGF-like domains.
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DR   EMBL; AF229448; AAL08213.1; -; mRNA.
DR   RefSeq; NP_571936.1; NM_131861.1.
DR   UniGene; Dr.83677; -.
DR   ProteinModelPortal; Q90Y57; -.
DR   SMR; Q90Y57; 187-335.
DR   PRIDE; Q90Y57; -.
DR   GeneID; 140421; -.
DR   KEGG; dre:140421; -.
DR   CTD; 140421; -.
DR   ZFIN; ZDB-GENE-011128-2; jag1a.
DR   eggNOG; NOG12793; -.
DR   HOVERGEN; HBG031645; -.
DR   InParanoid; Q90Y57; -.
DR   KO; K06052; -.
DR   NextBio; 20796975; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_N_dom.
DR   InterPro; IPR026219; Jagged/Serrate.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   InterPro; IPR001007; VWF_C.
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; 7.
DR   SMART; SM00179; EGF_CA; 9.
DR   SMART; SM00214; VWC; 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; 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     28       Potential.
FT   CHAIN        29   1242       Protein jagged-1a.
FT                                /FTId=PRO_0000007628.
FT   TOPO_DOM     29   1070       Extracellular (Potential).
FT   TRANSMEM   1071   1095       Helical; (Potential).
FT   TOPO_DOM   1096   1242       Cytoplasmic (Potential).
FT   DOMAIN      186    230       DSL.
FT   DOMAIN      231    264       EGF-like 1.
FT   DOMAIN      265    295       EGF-like 2; atypical.
FT   DOMAIN      297    335       EGF-like 3.
FT   DOMAIN      337    373       EGF-like 4.
FT   DOMAIN      375    411       EGF-like 5; calcium-binding (Potential).
FT   DOMAIN      413    449       EGF-like 6; calcium-binding (Potential).
FT   DOMAIN      451    486       EGF-like 7; calcium-binding (Potential).
FT   DOMAIN      488    524       EGF-like 8; calcium-binding (Potential).
FT   DOMAIN      526    562       EGF-like 9.
FT   DOMAIN      575    630       EGF-like 10.
FT   DOMAIN      632    668       EGF-like 11; calcium-binding (Potential).
FT   DOMAIN      670    706       EGF-like 12; calcium-binding (Potential).
FT   DOMAIN      708    744       EGF-like 13.
FT   DOMAIN      747    783       EGF-like 14.
FT   DOMAIN      785    821       EGF-like 15; calcium-binding (Potential).
FT   DOMAIN      823    859       EGF-like 16; calcium-binding (Potential).
FT   DOMAIN      917    959       EGF-like 17.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    218    218       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    385    385       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    560    560       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    748    748       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    960    960       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    991    991       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1046   1046       N-linked (GlcNAc...) (Potential).
FT   DISULFID    188    197       By similarity.
FT   DISULFID    201    213       By similarity.
FT   DISULFID    221    230       By similarity.
FT   DISULFID    235    246       By similarity.
FT   DISULFID    239    252       By similarity.
FT   DISULFID    254    263       By similarity.
FT   DISULFID    266    277       By similarity.
FT   DISULFID    272    283       By similarity.
FT   DISULFID    285    294       By similarity.
FT   DISULFID    301    313       By similarity.
FT   DISULFID    307    323       By similarity.
FT   DISULFID    325    334       By similarity.
FT   DISULFID    341    352       By similarity.
FT   DISULFID    346    361       By similarity.
FT   DISULFID    363    372       By similarity.
FT   DISULFID    379    390       By similarity.
FT   DISULFID    384    399       By similarity.
FT   DISULFID    401    410       By similarity.
FT   DISULFID    417    428       By similarity.
FT   DISULFID    422    437       By similarity.
FT   DISULFID    439    448       By similarity.
FT   DISULFID    455    465       By similarity.
FT   DISULFID    459    474       By similarity.
FT   DISULFID    476    485       By similarity.
FT   DISULFID    492    503       By similarity.
FT   DISULFID    497    512       By similarity.
FT   DISULFID    514    523       By similarity.
FT   DISULFID    530    541       By similarity.
FT   DISULFID    535    550       By similarity.
FT   DISULFID    552    561       By similarity.
FT   DISULFID    600    618       By similarity.
FT   DISULFID    620    629       By similarity.
FT   DISULFID    636    647       By similarity.
FT   DISULFID    641    656       By similarity.
FT   DISULFID    658    667       By similarity.
FT   DISULFID    674    685       By similarity.
FT   DISULFID    679    694       By similarity.
FT   DISULFID    696    705       By similarity.
FT   DISULFID    712    723       By similarity.
FT   DISULFID    717    732       By similarity.
FT   DISULFID    734    743       By similarity.
FT   DISULFID    751    762       By similarity.
FT   DISULFID    756    771       By similarity.
FT   DISULFID    773    782       By similarity.
FT   DISULFID    789    800       By similarity.
FT   DISULFID    794    809       By similarity.
FT   DISULFID    811    820       By similarity.
FT   DISULFID    827    838       By similarity.
FT   DISULFID    832    847       By similarity.
FT   DISULFID    849    858       By similarity.
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
//
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