ID A0A0V1DHB9_TRIBR Unreviewed; 886 AA.
AC A0A0V1DHB9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Delta-like protein {ECO:0000256|RuleBase:RU280815};
GN Name=CDK16 {ECO:0000313|EMBL:KRY60726.1};
GN ORFNames=T03_1381 {ECO:0000313|EMBL:KRY60726.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY60726.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY60726.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY60726.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRY60726.1}.
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DR EMBL; JYDI01000004; KRY60726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DHB9; -.
DR STRING; 45882.A0A0V1DHB9; -.
DR Proteomes; UP000054653; 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:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24044:SF501; EGF-LIKE DOMAIN-CONTAINING PROTEIN C02B10.3; 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; 1.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
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|PROSITE-ProRule:PRU00076,
KW ECO:0000256|RuleBase:RU280815};
KW Membrane {ECO:0000256|RuleBase:RU280815, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 735..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..364
FT /note="DSL"
FT /evidence="ECO:0000259|PROSITE:PS51051"
FT DOMAIN 429..467
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 325..334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 355..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00377"
FT DISULFID 457..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 886 AA; 98893 MW; AFF907F3361159FE CRC64;
MLYIGSDHTI VLNSTINIIV IIICCFCSFF ADIRWQQRIF KRRSSMASFC EMASVLLKVY
SCETIYFSEL CFGKRKHPKP SQQLAALCYK GGPCGDQSAS TSRPLSNRFS LSSKRIDLVE
KRASILHSVP GSVRMLSSVR QISLIALLLL ACSGSTYAVG RIEMALDAVY NPKGQLSNGA
HCRDRYMINE SVAVPGLCHT IAMICYRTYD DQERLGTVEV GKCHYGQWSS HGELGLNSFG
DPDDLLKPLI SNRQDFTYKW PGSLTIVVKL IHGGPTVDRQ QLIFESVKPM LLVASSDQGW
TRVDDYGQVG VDGSVGLTYR IRVVCADHHY GPDCAKRCSP KEGYYNCSAE GERICMPGWL
PPKCQMPICL PGCTSTCRRP GTCDLCPQGW TGPTCGQCEV RQGCVNGYCN KPNECICHER
WGGVHCDIDL DLCFHRNPCQ NGATCLGRTQ GNFTCLCASG FTGTYCNITK VNSSNEANSC
KYNGIVYQAQ QRWLVDDCAI CECSNGTVHC NRELCNPNDC LTVTHSNGQH SACPAGQLCK
AIYPSPSSCL KAPCSLLPFG QCWPVELIER QQSIEDRRKL CDFDHRGLKT SQQFCSRIFL
RLNISTLDKN TYVEQLCSTF WLQLSKLGFA RFHTQCKVYN TQSFPVVSVD LVSLTATPAF
ELKSHLLLLI GKRPLLFTAM NHTDGEMEVD EHNDINNKEN NHNYKRAPQQ TTTFLGSKQA
VTDKQDVYSE AVHNFLSVVL PAATVLLFVF LLISWTVWRK LKKLNQLHKR SSGPANTTKC
TIVGSMPITK SAGSQLDVLY NELRPQPSWT RQKRPFNDNS RHCWTMASRS SSPRIGRLYS
KGCTTGVYSD PVVQEELESP PHYDEVVGNG KDGRRTRPIF QFDVGI
//
