ID M3VY27_FELCA Unreviewed; 1234 AA.
AC M3VY27;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=JAG1 {ECO:0000313|Ensembl:ENSFCAP00000002028.5,
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:ENSFCAP00000002028.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000002028.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002028.5,
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:ENSFCAP00000002028.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002028.5,
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:ENSFCAP00000002028.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002028.5};
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; M3VY27; -.
DR PaxDb; 9685-ENSFCAP00000002028; -.
DR Ensembl; ENSFCAT00000002198.6; ENSFCAP00000002028.5; ENSFCAG00000002195.6.
DR VGNC; VGNC:67874; JAG1.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160148; -.
DR HOGENOM; CLU_004732_0_0_1; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
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; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF228; JAGGED CANONICAL NOTCH LIGAND 2; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
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; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
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..1234
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023937712"
FT TRANSMEM 1084..1109
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 705..741
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 DOMAIN 836..872
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1168..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1225
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 731..740
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"
FT DISULFID 862..871
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1234 AA; 135540 MW; 37452760376BC7A3 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 NDCESNPCKN GGTCIDGVNS YKCICSDGWE
GAYCETNIND CSQNPCHNGG SCRDLVNDFY CDCKNGWKGK TCHSRDSQCD EATCNNGGTC
YDEGDAFKCM CPGGWEGTTC NIARNSSCLP NPCHNGGTCV VNGDSFTCVC KEGWEGPICT
QNTNDCSPHP CYNSGTCVDG DNWYRCECAP GFAGPDCRIM LEITKSGTDW SSLNKDINEC
QSSPCAFGAT CVDEINGYQC VCPPGHSGAK CQEVSGRPCI TMGSVIPDGA KWDDDCNTCQ
CLNGRIACSK VWCGPRPCLL HKGHSECPSG QSCIPILDDQ CFVRPCTGVG ECRSSSLQPV
KTKCTSDPYY QDNCANITFT FNKEMMSPGL TTEHICSELR NLNILKNVSA EYSIYIACEP
SPSANNEIHV AISAEDIRDD GNPIKEITDK IIDLVSKRDG NSSLIAAVAE VRVQRRPVKN
RTDFLVPLLS SVLTVAWICC LVTAFYWCVR KRRKPSSHAR AASEDNTTNN VREQLNQIKN
PIEKHGANTV PIKDYENKNS KMSKIRTHNS EVEEDDMDKH QQKARFAKQP AYTLVDREEK
PPNGTPAKHP NWTNKQDNRD LESAQSLNRM EYIV
//
