ID A0A3Q3BPV0_KRYMA Unreviewed; 644 AA.
AC A0A3Q3BPV0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028249.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000028249.1}
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|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 AlphaFoldDB; A0A3Q3BPV0; -.
DR Ensembl; ENSKMAT00000028603.1; ENSKMAP00000028249.1; ENSKMAG00000020885.1.
DR GeneTree; ENSGT00940000166445; -.
DR Proteomes; UP000264800; Unplaced.
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; 2.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011651; Notch_ligand_N.
DR PANTHER; PTHR24044:SF508; DELTA-LIKE PROTEIN; 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; 2.
DR Pfam; PF07657; MNNL; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
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};
KW Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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 TRANSMEM 510..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..271
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 272..305
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 338..376
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 378..414
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 415..461
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 463..501
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 575..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 229..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 242..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 262..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 295..304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 366..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 404..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 419..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 451..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 472..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 491..500
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 644 AA; 70441 MW; B176D00396B3FC98 CRC64;
MFFWQTEARK QSHNVVALFL CLCLKQAKKS PNTHFLAHTY LTLLLLDSQE VLLTLICVCV
CDVGAAGVFE LQIRHFQNPH GHLQSGKCCD LRAGGGQRCS ARDQCDTFFH ACLKEYQARV
IPTGACTFGS DSTGVLGGNS QSLRNRGNDG GGGGEDGTNG HIAIPFKFAW PKSFSLVLEA
LDYDNDTSEP GQLIERVLLS SMLNPGEQWQ KFHHHGRVLT LEYRLRFRCD ANYYGPFCNK
FCRARDDFFG HFSCDPSGFK VCMEGWTGPE CKEAVCRQGC HQAHGSCTVP GECKCHYGWT
GPFCDQCETF PGCVYGSCTE PWQCVCDVNW GGLLCNKDLN YCGTHQPCKN GGTCTNTEPN
EYQCECQEGF RGRNCDIDAN ECEASVCIHA RSCRNLIGGY LCDCLPGWTG PNCDISTSCQ
GLCLNGGRCE VRHVKLEKKN TLLLSGSRCS CPPGFSGKFC QSGPGPCDSA PCLHGGQCTV
EQDGRTAACN CPTGRSGLLC AVSDTTHGGL SFYMILVGVL ALVMVCGCAA CAFTFSHLHR
KRRKQQSVPP EEGINNQREF VTLIRNVDRA VPLVPPAAPA AQPPAPAPAP RCYEEIELTL
PPSPAPSHPS PALKPAHAPK LDISNREREK LNRFHYTDNQ ELEV
//
