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5F84

Crystal structure of Drosophila Poglut1 (Rumi) complexed with its glycoprotein product (glucosylated EGF repeat) and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0007219biological_processNotch signaling pathway
A0012505cellular_componentendomembrane system
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processprotein O-linked glycosylation via serine
A0035251molecular_functionUDP-glucosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
A0042052biological_processrhabdomere development
A0045165biological_processcell fate commitment
A0045746biological_processnegative regulation of Notch signaling pathway
A0045747biological_processpositive regulation of Notch signaling pathway
A0046527molecular_functionglucosyltransferase activity
A0060537biological_processmuscle tissue development
A0140561molecular_functionEGF-domain serine glucosyltransferase activity
A0140562molecular_functionEGF-domain serine xylosyltransferase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
BCYS62-CYS73

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCpfGfeGKnC
ChainResidueDetails
BCYS71-CYS82

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCpfGFegkn....C
ChainResidueDetails
BCYS71-CYS82

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC
ChainResidueDetails
BASP47-CYS71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM
ChainResidueDetails
BASP47
BGLY48
BGLN50
BASP64
BASP65

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6688526
ChainResidueDetails
BASP64
AARG237
AVAL276
AALA294

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.28
ChainResidueDetails
BSER68
AARG232
AGLN259

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591
ChainResidueDetails
BSER53

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:1517205, ECO:0000269|PubMed:25456591
ChainResidueDetails
BSER61

222926

PDB entries from 2024-07-24

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