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Database: UniProt
Entry: A0A2I2UBC8_FELCA
LinkDB: A0A2I2UBC8_FELCA
Original site: A0A2I2UBC8_FELCA 
ID   A0A2I2UBC8_FELCA        Unreviewed;      1180 AA.
AC   A0A2I2UBC8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN   Name=JAG1 {ECO:0000313|Ensembl:ENSFCAP00000029791.1,
GN   ECO:0000313|VGNC:VGNC:67874};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000029791.1, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000029791.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029791.1,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000029791.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029791.1,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000029791.1}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029791.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. {ECO:0000256|RuleBase:RU280815}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU280815}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU280815}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AANG04003379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC234833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2UBC8; -.
DR   Ensembl; ENSFCAT00000036393.2; ENSFCAP00000029791.1; ENSFCAG00000002195.6.
DR   VGNC; VGNC:67874; JAG1.
DR   GeneTree; ENSGT00940000160148; -.
DR   Proteomes; UP000011712; Chromosome A3.
DR   Bgee; ENSFCAG00000002195; Expressed in zone of skin and 10 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 12.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.60.40.3510; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 14.
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; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF21700; DL-JAG_EGF-like; 1.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 8.
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; 15.
DR   SMART; SM00179; EGF_CA; 13.
DR   SMART; SM00214; VWC; 1.
DR   SMART; SM00215; VWC_out; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 9.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 14.
DR   PROSITE; PS01186; EGF_2; 10.
DR   PROSITE; PS50026; EGF_3; 14.
DR   PROSITE; PS01187; EGF_CA; 4.
PE   4: Predicted;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW   ECO:0000256|RuleBase:RU280815};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW   Signal {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1180
FT                   /note="Delta-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014176817"
FT   TRANSMEM        1030..1055
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          185..229
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          230..263
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          296..334
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          336..372
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          374..410
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          412..448
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          450..485
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          487..523
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          525..561
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          586..627
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          629..665
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          667..703
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          706..742
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          744..780
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          782..818
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1114..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        187..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        200..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        220..229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        253..262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        324..333
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        362..371
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        400..409
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        438..447
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        454..464
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        475..484
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        513..522
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        551..560
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        617..626
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        655..664
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        693..702
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        732..741
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        770..779
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        808..817
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1180 AA;  129700 MW;  65CFB4590E60D181 CRC64;
     MRSPRTRGRP GRPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGVRN
     PGDRKCSHDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRGNERNRI
     VLPFSFAWPR SYTLLVEAWD SSNDTLQPDS IIEKASHSGM INPSRQWQTL KQNTGIAHFE
     YQIRVTCDDY YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC MEGWMGPECN KAICRQGCSP
     KHGSCKLPGD CRCQYGWQGL YCDKCIPHPG CVHGTCNEPW QCLCETNWGG QLCDKDLNYC
     GTHQPCLNGG TCSNTGPDKY QCSCPEGYSG PNCEIAEHAC LSDPCHNRGS CRETSLGFEC
     ECSPGWTGPT CSTNIDDCSP NNCSHGGTCQ DLVNGFKCVC PPQWTGKTCQ LDANECEAKP
     CVNAKSCKNL IASYYCDCLP GWTGQNCDIN INDCLGQCQN DASCRDLVNG YRCICPPGYA
     GDHCERDIDE CASNPCLNGG HCQNEINRFQ CLCPTGFSGN LCQLDIDYCE PNPCQHGAQC
     YNRASDYFCK CPEDYEGKNC SHLKDHCRTT PCEVIDSCTV AMASNDTPEG VRYISSNVCG
     PHGKCKSQSG GKFTCDCNKG FTGTYCHENI NDCSQNPCHN GGSCRDLVND FYCDCKNGWK
     GKTCHSRDSQ CDEATCNNGG TCYDEGDAFK CMCPGGWEGT TCNIARNSSC LPNPCHNGGT
     CVVNGDSFTC VCKEGWEGPI CTQNTNDCSP HPCYNSGTCV DGDNWYRCEC APGFAGPDCR
     ININECQSSP CAFGATCVDE INGYQCVCPP GHSGAKCQEV SGRPCITMGS VIPDGAKWDD
     DCNTCQCLNG RIACSKVWCG PRPCLLHKGH SECPSGQSCI PILDDQCFVR PCTGVGECRS
     SSLQPVKTKC TSDPYYQDNC ANITFTFNKE MMSPGLTTEH ICSELRNLNI LKNVSAEYSI
     YIACEPSPSA NNEIHVAISA EDIRDDGNPI KEITDKIIDL VSKRDGNSSL IAAVAEVRVQ
     RRPVKNRTDF LVPLLSSVLT VAWICCLVTA FYWCVRKRRK PSSHARAASE DNTTNNVREQ
     LNQIKNPIEK HGANTVPIKD YENKNSKMSK IRTHNSEVEE DDMDKHQQKA RFAKQPAYTL
     VDREEKPPNG TPAKHPNWTN KQDNRDLESA QSLNRMEYIV
//
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