ID E4XER7_OIKDI Unreviewed; 1207 AA.
AC E4XER7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN ORFNames=GSOID_T00008711001 {ECO:0000313|EMBL:CBY19564.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY19564.1};
RN [1] {ECO:0000313|EMBL:CBY19564.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC signaling. {ECO:0000256|RuleBase:RU280815}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU280815}; Single-
CC pass type I membrane protein {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; FN653042; CBY19564.1; -; Genomic_DNA.
DR AlphaFoldDB; E4XER7; -.
DR InParanoid; E4XER7; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 8.
DR Gene3D; 2.10.25.140; -; 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; IPR001007; VWF_dom.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF224; PROTEIN CBG18408; 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; 2.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00179; EGF_CA; 12.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 4.
PE 4: Predicted;
KW Developmental protein {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:UP000001307};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|RuleBase:RU280815};
KW Transmembrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280815,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 959..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..89
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 90..123
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 156..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 194..231
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 233..269
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 271..309
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 311..352
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 354..390
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 392..428
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 459..495
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 497..533
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 535..577
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 584..623
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 626..662
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 664..700
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 702..738
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 47..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 60..72
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 80..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 113..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 221..230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 259..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 299..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 342..351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 380..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 418..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 485..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 523..532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 594..611
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 613..622
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 630..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 652..661
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 690..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 728..737
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1207 AA; 132148 MW; 825DDB077BD17CCF CRC64;
MDYDEDSVPQ LIEATEESKT IRPTGEWVKE VHRGTVATIE YLLKVECDEN YYDMSCSTFC
EAKDDKEGHF LCSSFGEKIC RDGWDGDNCD QPICSEKCHE KHGYCNEAGE CKCRFGWTGP
LCSQCIPAEG CVNGTCENPF ECKCTPFWGG KFCDINLNSC ESNPCQSESK CENTYGNFTC
TCLPGYHGQR CEHQANACVS KPCGSHGVCS ATKEGSFTCA CKEGWTGPYC SVNVNECANA
PCKNGGTCID REGDFVCECP PGWIGKTCQL DVDECAAETN PCQNAKRCIN SAGTFFCHCK
AGFEGIFCEK KIDECLPEED GAPKCANGGT CIDAFGSFKC VCPNGFEGDR CEVDIDECAQ
TPCSNGGRCS DMIGDFKCLC PSGYSGRKCE IPMGFCSDNP CQNEGKCFNV AESYECQCKE
EFEGQNCERV KDYCAQTGAS CEVIDACETK LTELRTGTTR LLTTKVCGAH GHCIARSFED
FTCECEEGFT GDFCQEEVDN CASNPCQNHG VCLNGVNSFE CSCPVGFAGL KCEKEAQVCS
SSDNPCLNNG KCIPGNSGHP SDFTCSCSDG WERTHLPVYQ TYTAEEICKN SSPCNAGTCV
PDTRLSTGIS CECPRGTSGA LCQIDARSPC SANPCKNGVC VPNEGDDFEC RCKAGFTGAK
CEKKIDMCKP EPCFNGGACL SKVNHYECKC RAGFVGADCR KDVDDCANDR CAYGSTCVDK
VGGFECLCPP GRQGAYCEKL SSFPTKRSCA YKGKLFVHSY SWREQCNTCS CHDGDVSCSK
LDCGPVACSP HAPSSCLSDE SCQQETPSEY ENCVSSRCSR RYTCQKKFNH YGANKAPPAS
CKTPNCLELK IQFDVNRISS LERGVHAMDV CGALNFLPSL ARVAENKETS LNCESAQAGV
VVVVVKHQSS AELVVKEIRR SLFEESDLSS VLTYRDEVIL SAAYDVSTID TSNEIDNHWI
WYILAVMLGL LSLFAVILLA FMVKHKNGMK SSEHEGSSYT MGSGVTDQVL MAASPSSSAA
LEPREFVFID PKEHPYPNML PRRVPNHLLS HNLSQNCQFG CPCKGWCEEK LPSGVQQNIS
IETLRTLGYE PYYQELFGIS PSDEDMTPSS GDYLFIGCKE KTSDAFNTGI FGAKAFLLEI
QEFENSPSMI SKSTEHNEFY YYNTNSLNYC GPNKIFGFSP IENIYPYCAD YYDCKYEVGK
DWVPIQG
//
