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   01-OCT-2014, entry version 104.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 DSL domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00377}.
CC   -!- SIMILARITY: Contains 17 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
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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       {ECO:0000255}.
FT   CHAIN        29   1242       Protein jagged-1a.
FT                                /FTId=PRO_0000007628.
FT   TOPO_DOM     29   1070       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1071   1095       Helical. {ECO:0000255}.
FT   TOPO_DOM   1096   1242       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      186    230       DSL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00377}.
FT   DOMAIN      231    264       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      265    295       EGF-like 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      297    335       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      337    373       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      375    411       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      413    449       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      451    486       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      488    524       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      526    562       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      575    630       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      632    668       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      670    706       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      708    744       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      747    783       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      785    821       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      823    859       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      917    959       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    141    141       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    218    218       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    560    560       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    748    748       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    960    960       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    991    991       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1046   1046       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    188    197       {ECO:0000250}.
FT   DISULFID    201    213       {ECO:0000250}.
FT   DISULFID    221    230       {ECO:0000250}.
FT   DISULFID    235    246       {ECO:0000250}.
FT   DISULFID    239    252       {ECO:0000250}.
FT   DISULFID    254    263       {ECO:0000250}.
FT   DISULFID    266    277       {ECO:0000250}.
FT   DISULFID    272    283       {ECO:0000250}.
FT   DISULFID    285    294       {ECO:0000250}.
FT   DISULFID    301    313       {ECO:0000250}.
FT   DISULFID    307    323       {ECO:0000250}.
FT   DISULFID    325    334       {ECO:0000250}.
FT   DISULFID    341    352       {ECO:0000250}.
FT   DISULFID    346    361       {ECO:0000250}.
FT   DISULFID    363    372       {ECO:0000250}.
FT   DISULFID    379    390       {ECO:0000250}.
FT   DISULFID    384    399       {ECO:0000250}.
FT   DISULFID    401    410       {ECO:0000250}.
FT   DISULFID    417    428       {ECO:0000250}.
FT   DISULFID    422    437       {ECO:0000250}.
FT   DISULFID    439    448       {ECO:0000250}.
FT   DISULFID    455    465       {ECO:0000250}.
FT   DISULFID    459    474       {ECO:0000250}.
FT   DISULFID    476    485       {ECO:0000250}.
FT   DISULFID    492    503       {ECO:0000250}.
FT   DISULFID    497    512       {ECO:0000250}.
FT   DISULFID    514    523       {ECO:0000250}.
FT   DISULFID    530    541       {ECO:0000250}.
FT   DISULFID    535    550       {ECO:0000250}.
FT   DISULFID    552    561       {ECO:0000250}.
FT   DISULFID    600    618       {ECO:0000250}.
FT   DISULFID    620    629       {ECO:0000250}.
FT   DISULFID    636    647       {ECO:0000250}.
FT   DISULFID    641    656       {ECO:0000250}.
FT   DISULFID    658    667       {ECO:0000250}.
FT   DISULFID    674    685       {ECO:0000250}.
FT   DISULFID    679    694       {ECO:0000250}.
FT   DISULFID    696    705       {ECO:0000250}.
FT   DISULFID    712    723       {ECO:0000250}.
FT   DISULFID    717    732       {ECO:0000250}.
FT   DISULFID    734    743       {ECO:0000250}.
FT   DISULFID    751    762       {ECO:0000250}.
FT   DISULFID    756    771       {ECO:0000250}.
FT   DISULFID    773    782       {ECO:0000250}.
FT   DISULFID    789    800       {ECO:0000250}.
FT   DISULFID    794    809       {ECO:0000250}.
FT   DISULFID    811    820       {ECO:0000250}.
FT   DISULFID    827    838       {ECO:0000250}.
FT   DISULFID    832    847       {ECO:0000250}.
FT   DISULFID    849    858       {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
//
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