ID A0A091SJX8_9GRUI Unreviewed; 1193 AA.
AC A0A091SJX8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
DE Flags: Fragment;
GN ORFNames=N332_11228 {ECO:0000313|EMBL:KFQ40590.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ40590.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ40590.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ40590.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK822344; KFQ40590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091SJX8; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; 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; 10.
DR Pfam; PF12661; hEGF; 2.
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; 6.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
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; 3.
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:UP000053369};
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 1043..1068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..203
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 204..237
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 270..308
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 310..346
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 348..384
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 386..422
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 424..459
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 461..497
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 499..535
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 564..601
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 603..639
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 641..677
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 679..715
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 718..754
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 756..792
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 794..830
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1126..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 161..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 174..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 194..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 227..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 298..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 336..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 374..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 412..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 428..438
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 449..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 487..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 525..534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 591..600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 629..638
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 667..676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 705..714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 744..753
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 782..791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 820..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ40590.1"
FT NON_TER 1193
FT /evidence="ECO:0000313|EMBL:KFQ40590.1"
SQ SEQUENCE 1193 AA; 131289 MW; F972AE4336E46000 CRC64;
QVTLASGQFE LEILSMQNVN GELQNGNCCD GTRNPGDRKC TRDECDTYFK VCLKEYQSRV
TAGGPCSFGS KSTPVIGGNT FNLKYSRNNE KNRIVIPFSF AWPRSYTLLV EAWDYNDNST
NPDRIIEKAS HSGMINPSRQ WQTLKHNAGV AHFEYQIRVT CAEHYYGFGC NKFCRPRDDF
FTHHTCDQNG NKTCLEGWMG PECNKAICRQ GCSPKHGSCT IPGECRCQYG WQGQYCDKCI
PHPGCVHGTC IEPWQCLCET NWGGQLCDKD LNYCGTHPPC LNGGTCSNTG PDKYQCSCPE
GYSGQNCEIA EHACLSDPCH NGGSCLETST GFECVCAPGW AGPTCTDNID DCSPNPCGHG
GTCQDLVDGF KCICPPQWTG KTCQLDANEC EGKPCVNANS CRNLIGSYYC DCITGWSGHN
CDININDCRG QCQNGGSCRD LVNGYRCICS PGYAGDHCEK DINECASNPC MNGGHCQDEI
NGFQCLCPAG FSGNLCQLDI DYCEPNPCQN GAQCFNLAMD YFCNCPEDYE GKNCSHLKDH
CRTTPCEVID SCTVAVASNS TPEGVRYISS NVCGPHGKCK SQAGGKFTCE CNKGFTGTYC
HENINDCESN PCKNGGTCID GINSYKCICS DGWEGTYCET NINDCSKNPC HNGGTCRDLV
NDFFCECKNG WKGKTCHSRD SQCDEATCNN GGTCYDEGDT FKCMCPAGWE GATCNIARNS
SCLPNPCHNG GTCVVSGDSF TCVCKEGWEG PTCTQNTNDC SPHPCYNSGT CVDGDNWYRC
ECAPGFAGPD CRININECQS SPCAFGATCV DEINGYRCIC PPGRSGPGCQ EVTGRPCITS
VRVMPDGAKW DDDCNTCRCS NGKITCSKVW CGPRPCVIHA KGHNECPAGH ACVPVKDDHC
FTHPCAAVGE CWPSNQQPVK TKCNSDSYYQ DNCANITFTF NKEMMAPGLT TEHICSELRN
LNILKNVSVE YSIYITCEPS RLANNEIHVA ISAEDTGEDE NPIRDITDKI IDLVSKRDGN
NTLIAAVAEV RVQRRPVKNK TDFLVPLLSS VLTVAWICCL VTVFYWCIRK RRKQSSHTHT
ASDDNTTNNV REQLNQIKNP IEKHGANTVP IKDYENKNSK IAKIRTHNSE VEEDDMDKHQ
QKARFTKQPA YTLVDRDEKP PNSTPTKHPN WTNKQDNRDL ESAQSLNRME YIV
//
