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}.
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; 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
//