8TZO
Structure of human Wnt7a 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 | 0016055 | biological_process | Wnt signaling pathway |
B | 0017147 | molecular_function | Wnt-protein binding |
B | 0030177 | biological_process | positive regulation of Wnt signaling pathway |
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. CKCHGVSGsC |
Chain | Residue | Details |
A | CYS200-CYS209 |
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 | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21423620, ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5 |
Chain | Residue | Details |
C | GLN26 | |
C | LYS62 | |
C | LYS64 | |
C | ASP328 | |
B | ALA493-GLU541 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14211 |
Chain | Residue | Details |
C | TYR109 | |
C | LYS111 | |
C | TYR128 | |
C | ASP135 | |
C | ASP317 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
C | LYS48 | |
C | LYS159 | |
C | LYS209 | |
B | SER453-SER471 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
Chain | Residue | Details |
C | LYS64 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
C | ASN344 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:20652957 |
Chain | Residue | Details |
B | GLN304-MET324 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:20652957 |
Chain | Residue | Details |
B | ILE332-PHE352 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:20652957 |
Chain | Residue | Details |
B | PHE381-PHE401 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:20652957 |
Chain | Residue | Details |
B | PHE432-VAL452 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:20652957 |
Chain | Residue | Details |
B | ALA472-TYR492 |