ID A0A3L8SVA7_CHLGU Unreviewed; 683 AA.
AC A0A3L8SVA7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN ORFNames=DV515_00002307 {ECO:0000313|EMBL:RLW09907.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW09907.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW09907.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW09907.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW09907.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW09907.1}.
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DR EMBL; QUSF01000004; RLW09907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SVA7; -.
DR STRING; 44316.ENSEGOP00005001490; -.
DR Ensembl; ENSEGOT00005001673; ENSEGOP00005001490; ENSEGOG00005001221.
DR OMA; ICLAGCT; -.
DR Proteomes; UP000276834; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 5.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
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; IPR011651; Notch_ligand_N.
DR PANTHER; PTHR24044:SF320; DELTA-LIKE PROTEIN 4-RELATED; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 1.
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 Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280815};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..683
FT /note="Delta-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017926277"
FT TRANSMEM 530..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 169..213
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 280..318
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 320..356
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 358..396
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 398..434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 436..472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 475..513
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 171..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 184..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 204..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 308..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 346..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 367..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 386..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 424..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 462..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 484..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 503..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 683 AA; 75894 MW; 92FF803D3A95BF6E CRC64;
MTALRIFGLT FLLTILQQRV SGSGVFQLEL HEFVNSHASL ASGKPCFPHC RTFFRVCLKH
FQTVVSPGSC TFGSIITPVL GINSFSIKDT ERFDSPIKLP FNFTWPGTFS LIIQAWHAPD
NYLPEGSRPP PQEWLISQMS IQRSLSVGED WLQDVHQGPL TKLRYSYRVV CSENYYGESC
SRLCKRRDDR FGHYVCAADG SLACLPGWAG EYCTDPICLA GCTEQNGYCN KPGECICRPG
WQGRYCDECI PHIGCRHGTC KTQWQCICDE GWGGLFCDQD LNYCTHHRPC KNGATCMNTG
QGSYTCACKP GFTGVDCEHE ISECDSNPCR NGGSCTDMEN GYHCLCPPGY YGTHCEHSAL
TCIDSPCFNG GTCLEKEQGA SYTCVCPFGF TGSNCEKKVD RCTSNPCAND GSCFYLGQIR
VCRCRAGFSG QKCEININDC ARNPCSNGGT CHDLINDYTC TCMPGYSGRN CDIKTRDECA
SGPCENGGTC YSGLYSANFV CYCPSGFMGN RCELPVYSVP ITLPPKPVPW IAISMGVGLV
ALLILFCMIA MVIRQMRMRP EQELETMNNL SDFQKDNLIP ASQLKNTNKN KDLEVDCGLE
KSNYKPKNHK LDYNLVKDLT SRGTAEDKYY KSEKCLGEKS PLRLHSEKPE CRISAICSPR
DSMYQSVFVI TEERNECIIA TEV
//