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Database: UniProt
Entry: A0A096LPT7_POEFO
LinkDB: A0A096LPT7_POEFO
Original site: A0A096LPT7_POEFO 
ID   A0A096LPT7_POEFO        Unreviewed;       729 AA.
AC   A0A096LPT7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000021178.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000021178.1}
RP   IDENTIFICATION.
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; AYCK01017075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A096LPT7; -.
DR   STRING; 48698.ENSPFOP00000021178; -.
DR   Ensembl; ENSPFOT00000028998.1; ENSPFOP00000021178.1; ENSPFOG00000010460.2.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000159781; -.
DR   OMA; AACEDKY; -.
DR   Proteomes; UP000028760; 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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 6.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   PANTHER; PTHR24044:SF380; DELTA-LIKE PROTEIN 1; 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; 5.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 6.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
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};
KW   Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..729
FT                   /note="Delta-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001926983"
FT   TRANSMEM        531..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          179..223
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          286..324
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          326..362
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          364..401
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          403..439
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          441..477
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          479..515
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          602..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        181..190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        194..206
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        214..223
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        314..323
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        352..361
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        391..400
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        429..438
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        467..476
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        505..514
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   729 AA;  79622 MW;  103D9CA152C0A29E CRC64;
     MGRVILLTLT VMFMLLCQGF CSGVFELKLQ EFLNKKGAQG NKNCCKGGLT SSFQQQCECK
     TFFRICLKHY QPNASPEPPC TYGGAVTPVL GSNSFQVPEV IPESAFTNPV RINFGFTWPG
     TFSLIIEALH TDSKDDLSTE NPERVISTMT TQRHLTVGDD WSQDLHTAGR TELKYSYRFV
     CDEHYYGDGC SVFCRPRDDA FGHFTCGERG EIVCDAGWKG QYCTEPICLP GCDEEHGFCE
     KPGECKCRVG FKGRYCDECI RYPGCLHGTC QQPWQCNCQE GFCNQDLNYC THHKPCMNGA
     TCSNTGQGSY TCSCRPGFTG ASCEIKVNEC AGNPCRNGGS CTDSENTYKC NCPHGFYGNN
     CELSAMTCAD GPCSNGGRCA DNPDGGYFCQ CPTGYAGFNC EKKIDHCTSS PCSNGARCVD
     LVNSYLCQCP EGFAGMNCDQ TGDVCSAYPC QNGGTCQEGP TGYTCTCPPG YTGRNCSSPI
     SRCEHNPCHN GATCHERNNR YVCACVPGYG GRNCQFLLPE HAAIRGTEVP WMAIGSGVAM
     VLLLLAGCAV LVGFLRSKAQ HSVQAETAGE GETINNLTNN CHRSDRDLAI SVMPMPGVKN
     INKKMDFSSG DPDEDSSPGR SSCKSRHPPS DYNLVREVNY EQAAKEAMLE AACEDKYQSL
     DSLEFEEKHS KRLKWKLAVK MTPGSQNISS QSDASEKRAP ELSACADTKY KSVFVMSEEK
     DECIIATEV
//
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