Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8TZR

Structure of human Wnt3a bound to WLS and CALR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005102	molecular_function	signaling receptor binding
A	0005576	cellular_component	extracellular region
A	0007275	biological_process	multicellular organism development
A	0016055	biological_process	Wnt signaling pathway
B	0000139	cellular_component	Golgi membrane
B	0001707	biological_process	mesoderm formation
B	0005515	molecular_function	protein binding
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005794	cellular_component	Golgi apparatus
B	0005802	cellular_component	trans-Golgi network
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006886	biological_process	intracellular protein transport
B	0009948	biological_process	anterior/posterior axis specification
B	0012505	cellular_component	endomembrane system
B	0016020	cellular_component	membrane
B	0016055	biological_process	Wnt signaling pathway
B	0017147	molecular_function	Wnt-protein binding
B	0030177	biological_process	positive regulation of Wnt signaling pathway
B	0030659	cellular_component	cytoplasmic vesicle membrane
B	0030666	cellular_component	endocytic vesicle membrane
B	0030901	biological_process	midbrain development
B	0030902	biological_process	hindbrain development
B	0031017	biological_process	exocrine pancreas development
B	0031090	cellular_component	organelle membrane
B	0031410	cellular_component	cytoplasmic vesicle
B	0031901	cellular_component	early endosome membrane
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0061355	biological_process	Wnt protein secretion
B	0061357	biological_process	positive regulation of Wnt protein secretion
B	0070062	cellular_component	extracellular exosome
B	0071529	biological_process	cementum mineralization
B	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
C	0005509	molecular_function	calcium ion binding
C	0005783	cellular_component	endoplasmic reticulum
C	0006457	biological_process	protein folding
C	0051082	molecular_function	unfolded protein binding

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KDEL

Chain	Residue	Details
C	LYS414-LEU417

site_id	PS00246
Number of Residues	10
Details	WNT1 Wnt-1 family signature. CKCHGLSGsC

Chain	Residue	Details
A	CYS203-CYS212

site_id	PS00803
Number of Residues	16
Details	CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF

Chain	Residue	Details
C	LYS98-PHE113

site_id	PS00804
Number of Residues	9
Details	CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG

Chain	Residue	Details
C	ILE130-GLY138

site_id	PS00805
Number of Residues	13
Details	CALRETICULIN_REPEAT Calreticulin family repeated motif signature. IkDpDasKPEDWD

Chain	Residue	Details
C	ILE208-ASP220
C	ILE225-ASP237
C	ILE242-ASP254

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Lipidation: {"description":"O-palmitoleoyl serine; by PORCN","evidences":[{"source":"PubMed","id":"20826466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21244856","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24292069","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25731175","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21244856","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	253
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	49
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"20652957","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	131
Details	Region: {"description":"Interaction with Wnt proteins","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	11
Details	Repeat: {"description":"1-1"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	179
Details	Region: {"description":"N-domain"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21423620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27840680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3POS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3POW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LK5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14211","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)