DLLC_DANRE
ID DLLC_DANRE Reviewed; 664 AA.
AC Q9IAT6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Delta-like protein C;
DE Short=DeltaC;
DE Short=delC;
DE Flags: Precursor;
GN Name=dlc;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10585570; DOI=10.1016/s0925-4773(99)00231-2;
RA Smithers L.E., Haddon C., Jiang Y.-J., Lewis J.;
RT "Sequence and embryonic expression of deltaC in the zebrafish.";
RL Mech. Dev. 90:119-123(2000).
RN [2]
RP FUNCTION.
RX PubMed=11100729; DOI=10.1038/35044091;
RA Jiang Y.-J., Aerne B.L., Smithers L., Haddon C., Ish-Horowicz D., Lewis J.;
RT "Notch signalling and the synchronization of the somite segmentation
RT clock.";
RL Nature 408:475-479(2000).
CC -!- FUNCTION: Acts as a ligand for Notch receptors and is involved in
CC somitogenesis. Can activate Notch receptors. Required in somite
CC segmentation to keep the oscillations of neighboring presomitic
CC mesoderm cells synchronized. {ECO:0000269|PubMed:11100729}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the early retina, where it
CC precedes other delta proteins. Also expressed in cranial ganglia, in
CC sensory epithelia including ear and lateral line and in scattered
CC epidermal cells. In the mesoderm, expression is visible by 50% epiboly;
CC it is expressed subsequently in the tail bud, in stripes in the
CC presomitic mesoderm and in the posterior half of each somite. Also
CC expressed in notochord, blood vessels and pronephros. In contrast to
CC other delta proteins, it is not expressed in the majority of nascent
CC primary neurons. In somites, it marks the posterior part of each formed
CC somite, while deltaD (dld) marks the anterior part.
CC {ECO:0000269|PubMed:10585570}.
CC -!- PTM: Ubiquitinated by mib, leading to its endocytosis and subsequent
CC degradation. {ECO:0000250}.
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DR EMBL; AF146429; AAF27299.1; -; mRNA.
DR RefSeq; NP_571019.1; NM_130944.1.
DR AlphaFoldDB; Q9IAT6; -.
DR SMR; Q9IAT6; -.
DR BioGRID; 78356; 3.
DR STRING; 7955.ENSDARP00000018643; -.
DR PaxDb; Q9IAT6; -.
DR PRIDE; Q9IAT6; -.
DR GeneID; 30120; -.
DR KEGG; dre:30120; -.
DR CTD; 30120; -.
DR ZFIN; ZDB-GENE-000125-4; dlc.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q9IAT6; -.
DR OrthoDB; 406049at2759; -.
DR PhylomeDB; Q9IAT6; -.
DR SignaLink; Q9IAT6; -.
DR PRO; PR:Q9IAT6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IGI:ZFIN.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:ZFIN.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IDA:ZFIN.
DR GO; GO:0060842; P:arterial endothelial cell differentiation; IMP:ZFIN.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:ZFIN.
DR GO; GO:0035907; P:dorsal aorta development; IGI:ZFIN.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:ZFIN.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IMP:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0061056; P:sclerotome development; IGI:ZFIN.
DR GO; GO:0001757; P:somite specification; IGI:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IGI:ZFIN.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF12661; hEGF; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
PE 2: Evidence at transcript level;
KW Calcium; Developmental protein; Differentiation; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..664
FT /note="Delta-like protein C"
FT /id="PRO_0000007516"
FT TOPO_DOM 21..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 154..198
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 199..232
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 233..263
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 265..303
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 305..341
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 343..380
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 382..418
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 420..456
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 458..494
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..165
FT /evidence="ECO:0000250"
FT DISULFID 169..181
FT /evidence="ECO:0000250"
FT DISULFID 189..198
FT /evidence="ECO:0000250"
FT DISULFID 203..214
FT /evidence="ECO:0000250"
FT DISULFID 207..220
FT /evidence="ECO:0000250"
FT DISULFID 222..231
FT /evidence="ECO:0000250"
FT DISULFID 234..245
FT /evidence="ECO:0000250"
FT DISULFID 240..251
FT /evidence="ECO:0000250"
FT DISULFID 253..262
FT /evidence="ECO:0000250"
FT DISULFID 269..281
FT /evidence="ECO:0000250"
FT DISULFID 275..291
FT /evidence="ECO:0000250"
FT DISULFID 293..302
FT /evidence="ECO:0000250"
FT DISULFID 309..320
FT /evidence="ECO:0000250"
FT DISULFID 314..329
FT /evidence="ECO:0000250"
FT DISULFID 331..340
FT /evidence="ECO:0000250"
FT DISULFID 347..358
FT /evidence="ECO:0000250"
FT DISULFID 352..368
FT /evidence="ECO:0000250"
FT DISULFID 370..379
FT /evidence="ECO:0000250"
FT DISULFID 386..397
FT /evidence="ECO:0000250"
FT DISULFID 391..406
FT /evidence="ECO:0000250"
FT DISULFID 408..417
FT /evidence="ECO:0000250"
FT DISULFID 424..435
FT /evidence="ECO:0000250"
FT DISULFID 429..444
FT /evidence="ECO:0000250"
FT DISULFID 446..455
FT /evidence="ECO:0000250"
FT DISULFID 462..473
FT /evidence="ECO:0000250"
FT DISULFID 467..482
FT /evidence="ECO:0000250"
FT DISULFID 484..493
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 72548 MW; 0AD6C34C8579116B CRC64;
MARVLLTCFF ILISSHLGKS SGVFELKVLS FTSTSSVCKG SSDCQIFFRV CLKHSQALIL
PEPPCTYGTG MSEILSADSI SSSAYISVPF NFKWPGIVSL IIETWNAETS DQSTENNNNM
ISRLATKRRL AISEDWSQDV HLGRQSQLRF SYRVVCDEFY HGEECSDFCR PRNDTFGHFN
CDAAGNRICL PGWKGDYCTE PICLSGCSEE NGYCEAPGEC KCRIGWEGPL CDECTRHPGC
LHGTCNQPFQ CTCKEGWGGL FCNEDLNFCT NHKPCRNDAT CTNTGQGSYT CICKPGFSGK
NCEIETNECD SNPCKNGGSC NDQENDYTCT CPQGFYGKNC EVSAMTCADG PCFNGGTCME
KGSGSYSCRC PPGYMGSNCE KKIDRCSSDP CANGGQCLDL GNKATCRCRP GFTGSRCETN
IDDCSSNPCQ NAGTCVDGIN GYTCTCTLGF SGKDCRVRSD ACSFMPCQNG GTCYTHFSGP
VCQCPAGFMG TQCEYKQKPT PVNSPALPAA LIVSFTLGLI TLTLVICAAI VVLRQMRQNH
KASSTTVRNN LDSVNNRISL SPTSPLGREK EAFLIPGGPF KVSNKDMALR STSVDTHSSD
KSNYKQKMVD YNLSIDEKHT NNKLEKNSES TLLVPPLNYP KEGVYHPVYI IPEHIEQRVF
ATEV
