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8TZO

Structure of human Wnt7a bound to WLS and CALR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005102molecular_functionsignaling receptor binding
A0005576cellular_componentextracellular region
A0007275biological_processmulticellular organism development
A0016055biological_processWnt signaling pathway
B0000139cellular_componentGolgi membrane
B0001707biological_processmesoderm formation
B0005515molecular_functionprotein binding
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005802cellular_componenttrans-Golgi network
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006886biological_processintracellular protein transport
B0009948biological_processanterior/posterior axis specification
B0012505cellular_componentendomembrane system
B0016055biological_processWnt signaling pathway
B0017147molecular_functionWnt-protein binding
B0030177biological_processpositive regulation of Wnt signaling pathway
B0030666cellular_componentendocytic vesicle membrane
B0030901biological_processmidbrain development
B0030902biological_processhindbrain development
B0031017biological_processexocrine pancreas development
B0031090cellular_componentorganelle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031901cellular_componentearly endosome membrane
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0061355biological_processWnt protein secretion
B0061357biological_processpositive regulation of Wnt protein secretion
B0070062cellular_componentextracellular exosome
B0071529biological_processcementum mineralization
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
C0005509molecular_functioncalcium ion binding
C0005783cellular_componentendoplasmic reticulum
C0006457biological_processprotein folding
C0051082molecular_functionunfolded protein binding
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KDEL
ChainResidueDetails
CLYS414-LEU417

site_idPS00246
Number of Residues10
DetailsWNT1 Wnt-1 family signature. CKCHGVSGsC
ChainResidueDetails
ACYS200-CYS209

site_idPS00803
Number of Residues16
DetailsCALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF
ChainResidueDetails
CLYS98-PHE113

site_idPS00804
Number of Residues9
DetailsCALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG
ChainResidueDetails
CILE130-GLY138

site_idPS00805
Number of Residues13
DetailsCALRETICULIN_REPEAT Calreticulin family repeated motif signature. IkDpDasKPEDWD
ChainResidueDetails
CILE208-ASP220
CILE225-ASP237
CILE242-ASP254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21423620, ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5
ChainResidueDetails
CGLN26
CLYS62
CLYS64
CASP328
BALA493-GLU541

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14211
ChainResidueDetails
CTYR109
CLYS111
CTYR128
CASP135
CASP317

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS48
CLYS159
CLYS209
BSER453-SER471

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
CLYS64

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN344

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:20652957
ChainResidueDetails
BGLN304-MET324

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:20652957
ChainResidueDetails
BILE332-PHE352

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:20652957
ChainResidueDetails
BPHE381-PHE401

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:20652957
ChainResidueDetails
BPHE432-VAL452

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:20652957
ChainResidueDetails
BALA472-TYR492

224004

PDB entries from 2024-08-21

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