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Database: UniProt
Entry: A0A3L8SVA7_CHLGU
LinkDB: A0A3L8SVA7_CHLGU
Original site: A0A3L8SVA7_CHLGU 
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
//
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