7Q3N

Cryo-EM of the complex between human uromodulin (UMOD)/Tamm-Horsfall protein (THP) and the FimH lectin domain from uropathogenic E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
F	0007155	biological_process	cell adhesion
F	0009289	cellular_component	pilus
U	0000922	cellular_component	spindle pole
U	0005509	molecular_function	calcium ion binding
U	0005515	molecular_function	protein binding
U	0005576	cellular_component	extracellular region
U	0005615	cellular_component	obsolete extracellular space
U	0005783	cellular_component	endoplasmic reticulum
U	0005796	cellular_component	Golgi lumen
U	0005886	cellular_component	plasma membrane
U	0005929	cellular_component	cilium
U	0006968	biological_process	cellular defense response
U	0007157	biological_process	heterophilic cell-cell adhesion
U	0007159	biological_process	leukocyte cell-cell adhesion
U	0008285	biological_process	negative regulation of cell population proliferation
U	0009986	cellular_component	cell surface
U	0010467	biological_process	gene expression
U	0016020	cellular_component	membrane
U	0016323	cellular_component	basolateral plasma membrane
U	0016324	cellular_component	apical plasma membrane
U	0019864	molecular_function	IgG binding
U	0019898	cellular_component	extrinsic component of membrane
U	0044732	cellular_component	mitotic spindle pole body
U	0050801	biological_process	monoatomic ion homeostasis
U	0050829	biological_process	defense response to Gram-negative bacterium
U	0060170	cellular_component	ciliary membrane
U	0070062	cellular_component	extracellular exosome
U	0071692	biological_process	protein localization to extracellular region
U	0072218	biological_process	metanephric ascending thin limb development
U	0072221	biological_process	metanephric distal convoluted tubule development
U	0072233	biological_process	metanephric thick ascending limb development
U	0140367	biological_process	antibacterial innate immune response
U	1990266	biological_process	neutrophil migration

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtpgsFsCvC

Chain	Residue	Details
U	CYS83-CYS94
U	CYS126-CYS137

---

site_id	PS00682
Number of Residues	41
Details	ZP_1 ZP domain signature. VgtmldggDlsrFaLlMtnCYaTPss..NaTdplkyfIIqdr.C

Chain	Residue	Details
U	VAL487-CYS527

---

site_id	PS01186
Number of Residues	14
Details	EGF_2 EGF-like domain signature 2. CtCqeGFtgdglt..C

Chain	Residue	Details
U	CYS50-CYS63
U	CYS92-CYS106
U	CYS135-CYS150

---

site_id	PS01187
Number of Residues	28
Details	EGF_CA Calcium-binding EGF-like domain signature. DlDECaipgahn.......Csanss..CvNtpgsFsC

Chain	Residue	Details
U	ASP65-CYS92
U	ASP108-CYS135

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	42
Details	Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	41
Details	Domain: {"description":"EGF-like 3; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	120
Details	Domain: {"description":"D10C","evidences":[{"source":"PROSITE-ProRule","id":"PRU01408","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35273390","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	21
Details	Region: {"description":"Beta hairpin","evidences":[{"source":"PubMed","id":"35273390","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32616672","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32616672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35273390","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7PFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Q3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26811476","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32616672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35273390","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7PFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Q3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"32616672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35273390","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7PFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Q3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---