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Database: UniProt
Entry: A0A3Q1FD43_9TELE
LinkDB: A0A3Q1FD43_9TELE
Original site: A0A3Q1FD43_9TELE 
ID   A0A3Q1FD43_9TELE        Unreviewed;      1094 AA.
AC   A0A3Q1FD43;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000014953.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000014953.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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|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   AlphaFoldDB; A0A3Q1FD43; -.
DR   STRING; 80966.ENSAPOP00000014953; -.
DR   Ensembl; ENSAPOT00000023495.1; ENSAPOP00000014953.1; ENSAPOG00000017878.1.
DR   GeneTree; ENSGT00940000164854; -.
DR   InParanoid; A0A3Q1FD43; -.
DR   OrthoDB; 5475408at2759; -.
DR   Proteomes; UP000257200; Unplaced.
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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 13.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR026219; Jagged/Serrate.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR45836:SF13; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; 1.
DR   PANTHER; PTHR45836; SLIT 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   PRINTS; PR02059; JAGGEDFAMILY.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 16.
DR   SMART; SM00179; EGF_CA; 14.
DR   SMART; SM00215; VWC_out; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 11.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 7.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 15.
DR   PROSITE; PS01186; EGF_2; 10.
DR   PROSITE; PS50026; EGF_3; 14.
DR   PROSITE; PS01187; EGF_CA; 3.
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:UP000257200};
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        922..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..70
FT                   /note="DSL"
FT                   /evidence="ECO:0000259|PROSITE:PS51051"
FT   DOMAIN          137..175
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          177..213
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          215..251
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          253..289
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          291..326
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          328..364
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          370..406
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          431..471
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          473..509
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          511..547
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          549..585
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          588..624
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   REGION          980..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        28..37
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        41..53
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        61..70
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT   DISULFID        165..174
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        203..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        241..250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        279..288
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        295..305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        316..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        354..363
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        396..405
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        461..470
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        499..508
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        537..546
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        575..584
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        614..623
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"
SQ   SEQUENCE   1094 AA;  119842 MW;  9DC2174C3A3F06F8 CRC64;
     MINPGDHWQT ILHDGPVAHL MYRIRVRCDD NYYSNKCNKL CVPRDDYFGH YRCEPSGAQV
     CLDGWMGPDC RTAICKQGCN LLHGGCSVPG GCKCNYGWQG QFCDECVLYP GCVHGTCNLP
     WQCNCERNWG GLLCDKDLNY CGRHQPCING GTCMNTEPDE YYCACPQGYS GKTCQIAEHA
     CVSSPCANAG TCHEVPTGFE CQCPPGWEGP TCANNLDECA SSPCAQGGTC VDLEDGFECV
     CPPQWEGKTC QIDANECAEQ PCVNAYSCKN LIGGYHCDCF RGWSGLNCDI NVNGCHGQCL
     NGATCKEGPK GYHCQCTSGF VGTHCAIQRN QCDSRPCQNG GQCHAVLDSF VCECPAEFAG
     QLCEISTWSS SDACDPNPCE NEAQCHSMDQ DFYCACPEGY KGKTCERLKE NCQTTPCQVI
     DSCTVAEATN DSAEVRHISS NVCGPRGHCI SQPAGNFTCI CDAGFSGVYC HENINDCISN
     PCRNGGTCID GVNSFQCFCP DGWEGRLCDL NVNECRHNPC KNGGQCVDLV NDFYCECADN
     WKGKTCHSRE SQCDETTCSN GGTCYDHGDA FRCDCPPGWE GNTCNTAKKS TCTSSPCSNG
     GTCVGGGDTF TCICKEGWEG PSCGQNTNDC NPHPCYNGGI CVDGVNWFRC ECAPGFAGPD
     CRININECQS SPCAYGATCV DEINGFRCIC PLGRTGTRCQ EFIGIGKTCH YAGLQFPHGS
     HWEEECNTCH CINGKVDCTK VLCGRRPCRL QSAGQDQRQQ SCPAGRECLE HSYFTCFSPP
     CHQWGVCSMA GPPPPQATTK CQPNNGHLDN SCGRVTLVFN RDKVPPGTTV ENICFELRYL
     PDTQSLAKDH ALLLLCDLSH SNQDAVEVAI SFHPEDLPDH SLIQETASAI VGTLSKRHNS
     TIMLAVIEVK VETQVMPPSV DYLVPLLCVV FCLLCLFCII VCVWWTRKRR KERERTTHSA
     ADDNVNNQWE PLRLMVGRQQ QQQQQLKESN REAEQERKKL MGPSYRTCDE EEEEETDGEL
     ELEECGGAEA GKQLVYKYSK TAVQSSGGVI CTLHSSSSPL KAPHRTQGYS PKDNRWKNVS
     AVFNGQKDLR DHCV
//
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