DLL4_HUMAN » Delta-like protein 4

DLL4_HUMAN » Delta-like protein 4
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
DLL4_HUMAN » Delta-like protein 4 » Drosophila Delta homolog 4;Delta4;
Hydrophobic Thickness 34.4 ± 3.8 Å
Tilt Angle 31 ± 3°
ΔGtransfer -26.8 kcal/mol
ΔGfold -20.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, Reactome
Topology Out
TM Segments 529-555 (526-558)
Pathways

Notch signaling pathway (KEGG)

Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor (Reactome)

Signal Transduction (Reactome)

PDB none
OPM none
Complexes none
Interactions

NOTC1, Complex: DLL4:NOTC1, PubMed

NOTC4, Complex: DLL4:NOTC4, PubMed

Domains

AA: 27-89, PDBID: 4XL1, Subunit B, Seq Identity:84%, N terminus of Notch ligand

AA: 155-217, PDBID: 4XL1, Subunit B, Seq Identity:84%, Delta serrate ligand

AA: 281-320, PDBID: 4XBM, Subunit A, Seq Identity:51%, EGF-like domain

AA: 328-358, PDBID: 4XBM, Subunit B, Seq Identity:63%, EGF-like domain

AA: 366-398, PDBID: 4XBM, Subunit B, Seq Identity:50%, EGF-like domain

AA: 411-432, PDBID: 2YGQ, Subunit A, Seq Identity:47%, Human growth factor-like EGF

AA: 444-474, PDBID: 4XBM, Subunit B, Seq Identity:57%, EGF-like domain

UniProt annotation for DLL4_HUMAN » Delta-like protein 4
FUNCTION: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation is required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate.

SUBUNIT: Binds to Notch-1 and Notch-4.

TISSUE SPECIFICITY: Expressed in vascular endothelium.

DOMAIN: The Delta-Serrate-Lag2 (DSL) domain is required for binding to the Notch receptor.

UniProt features for DLL4_HUMAN » Delta-like protein 4
SIGNAL 1 26
CHAIN 27 685 Delta-like protein 4.
DOMAIN 173 217 DSL.
DOMAIN 218 251 EGF-like 1.
DOMAIN 252 282 EGF-like 2.
DOMAIN 284 322 EGF-like 3.
DOMAIN 324 360 EGF-like 4.
DOMAIN 362 400 EGF-like 5.
DOMAIN 402 438 EGF-like 6.
DOMAIN 440 476 EGF-like 7.
DOMAIN 480 518 EGF-like 8.
DISULFID 175 184 By similarity.
DISULFID 188 200 By similarity.
DISULFID 208 217 By similarity.
DISULFID 222 233 By similarity.
DISULFID 226 239 By similarity.
DISULFID 241 250 By similarity.
DISULFID 253 264 By similarity.
DISULFID 259 270 By similarity.
DISULFID 272 281 By similarity.
DISULFID 288 300 By similarity.
DISULFID 294 310 By similarity.
DISULFID 312 321 By similarity.
DISULFID 328 339 By similarity.
DISULFID 333 348 By similarity.
DISULFID 350 359 By similarity.
DISULFID 366 377 By similarity.
DISULFID 371 388 By similarity.
DISULFID 390 399 By similarity.
DISULFID 406 417 By similarity.
DISULFID 411 426 By similarity.
DISULFID 428 437 By similarity.
DISULFID 444 455 By similarity.
DISULFID 449 464 By similarity.
DISULFID 466 475 By similarity.
DISULFID 484 495 By similarity.
DISULFID 489 506 By similarity.
DISULFID 508 517 By similarity.
Amino Acid Sequence for DLL4_HUMAN » Delta-like protein 4
MAAASRSASG WALLLLVALW QQRAAGSGVF QLQLQEFINE RGVLASGRPC EPGCRTFFRV CLKHFQAVVS PGPCTFGTVS TPVLGTNSFA VRDDSSGGGR NPLQLPFNFT WPGTFSLIIE AWHAPGDDLR PEALPPDALI SKIAIQGSLA VGQNWLLDEQ TSTLTRLRYS YRVICSDNYY GDNCSRLCKK RNDHFGHYVC QPDGNLSCLP GWTGEYCQQP ICLSGCHEQN GYCSKPAECL CRPGWQGRLC NECIPHNGCR HGTCSTPWQC TCDEGWGGLF CDQDLNYCTH HSPCKNGATC SNSGQRSYTC TCRPGYTGVD CELELSECDS NPCRNGGSCK DQEDGYHCLC PPGYYGLHCE HSTLSCADSP CFNGGSCRER NQGANYACEC PPNFTGSNCE KKVDRCTSNP CANGGQCLNR GPSRMCRCRP GFTGTYCELH VSDCARNPCA HGGTCHDLEN GLMCTCPAGF SGRRCEVRTS IDACASSPCF NRATCYTDLS TDTFVCNCPY GFVGSRCEFP VGLPPSFPWV AVSLGVGLAV LLVLLGMVAV AVRQLRLRRP DDGSREAMNN LSDFQKDNLI PAAQLKNTNQ KKELEVDCGL DKSNCGKQQN HTLDYNLAPG PLGRGTMPGK FPHSDKSLGE KAPLRLHSEK PECRISAICS PRDSMYQSVC LISEERNECV IATEV