Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7YG1

Cryo-EM structure of the C-terminal domain of the human sodium-chloride cotransporter

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002021	biological_process	response to dietary excess
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0006814	biological_process	sodium ion transport
A	0006884	biological_process	cell volume homeostasis
A	0007165	biological_process	signal transduction
A	0008511	molecular_function	sodium:potassium:chloride symporter activity
A	0015081	molecular_function	sodium ion transmembrane transporter activity
A	0015293	molecular_function	symporter activity
A	0015377	molecular_function	chloride:monoatomic cation symporter activity
A	0015378	molecular_function	sodium:chloride symporter activity
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0035725	biological_process	sodium ion transmembrane transport
A	0046873	molecular_function	metal ion transmembrane transporter activity
A	0055064	biological_process	chloride ion homeostasis
A	0055075	biological_process	potassium ion homeostasis
A	0055078	biological_process	sodium ion homeostasis
A	0055085	biological_process	transmembrane transport
A	0070062	cellular_component	extracellular exosome
A	0070294	biological_process	renal sodium ion absorption
A	0071241	biological_process	cellular response to inorganic substance
A	1901702	molecular_function	salt transmembrane transporter activity
A	1902476	biological_process	chloride transmembrane transport
A	1904044	biological_process	response to aldosterone
A	1990573	biological_process	potassium ion import across plasma membrane
B	0000166	molecular_function	nucleotide binding
B	0002021	biological_process	response to dietary excess
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006811	biological_process	monoatomic ion transport
B	0006814	biological_process	sodium ion transport
B	0006884	biological_process	cell volume homeostasis
B	0007165	biological_process	signal transduction
B	0008511	molecular_function	sodium:potassium:chloride symporter activity
B	0015081	molecular_function	sodium ion transmembrane transporter activity
B	0015293	molecular_function	symporter activity
B	0015377	molecular_function	chloride:monoatomic cation symporter activity
B	0015378	molecular_function	sodium:chloride symporter activity
B	0016020	cellular_component	membrane
B	0016324	cellular_component	apical plasma membrane
B	0022857	molecular_function	transmembrane transporter activity
B	0035725	biological_process	sodium ion transmembrane transport
B	0046873	molecular_function	metal ion transmembrane transporter activity
B	0055064	biological_process	chloride ion homeostasis
B	0055075	biological_process	potassium ion homeostasis
B	0055078	biological_process	sodium ion homeostasis
B	0055085	biological_process	transmembrane transport
B	0070062	cellular_component	extracellular exosome
B	0070294	biological_process	renal sodium ion absorption
B	0071241	biological_process	cellular response to inorganic substance
B	1901702	molecular_function	salt transmembrane transporter activity
B	1902476	biological_process	chloride transmembrane transport
B	1904044	biological_process	response to aldosterone
B	1990573	biological_process	potassium ion import across plasma membrane

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1206
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:7Y6I, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR, ECO:0007744\|PDB:8FHT

Chain	Residue	Details
A	MET2-TRP138
B	MET279
B	GLY362-PRO367
B	GLN487-VAL506
B	PRO556-ASN566
B	PRO608-LEU1022
A	ASN195-PRO213
A	MET279
A	GLY362-PRO367
A	GLN487-VAL506
A	PRO556-ASN566
A	PRO608-LEU1022
B	MET2-TRP138
B	ASN195-PRO213

site_id	SWS_FT_FI2
Number of Residues	56
Details	TRANSMEM: Discontinuously helical => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:7Y6I, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR, ECO:0007744\|PDB:8FHT

Chain	Residue	Details
A	VAL139-GLY167
B	VAL139-GLY167

site_id	SWS_FT_FI3
Number of Residues	198
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:7Y6I, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR, ECO:0007744\|PDB:8FHT

Chain	Residue	Details
A	ILE168
B	VAL398-ALA454
B	LEU525-ASN526
B	TRP586
A	ALA251-ASN258
A	PRO307-PHE340
A	VAL398-ALA454
A	LEU525-ASN526
A	TRP586
B	ILE168
B	ALA251-ASN258
B	PRO307-PHE340

site_id	SWS_FT_FI4
Number of Residues	538
Details	TRANSMEM: Helical => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:7Y6I, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR, ECO:0007744\|PDB:8FHT

Chain	Residue	Details
A	VAL169-THR194
A	LYS567-THR585
A	TRP587-LYS607
B	VAL169-THR194
B	GLU214-GLY250
B	ASP259-GLY278
B	GLU280-ILE306
B	PHE341-SER361
B	ALA368-VAL397
B	PRO455-ASP486
B	ARG507-GLU524
A	GLU214-GLY250
B	THR527-SER555
B	LYS567-THR585
B	TRP587-LYS607
A	ASP259-GLY278
A	GLU280-ILE306
A	PHE341-SER361
A	ALA368-VAL397
A	PRO455-ASP486
A	ARG507-GLU524
A	THR527-SER555

site_id	SWS_FT_FI5
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:7Y6I, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR, ECO:0007744\|PDB:8FHT

Chain	Residue	Details
A	ASN149
B	ALA469
A	GLY152
A	THR465
A	SER468
A	ALA469
B	ASN149
B	GLY152
B	THR465
B	SER468

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR

Chain	Residue	Details
A	ILE150
B	ILE150

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ

Chain	Residue	Details
A	ALA228
B	ALA228

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR

Chain	Residue	Details
A	THR235
B	THR235

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHR

Chain	Residue	Details
A	GLY353
B	GLY353

site_id	SWS_FT_FI10
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:36351028, ECO:0000305\|PubMed:36792826

Chain	Residue	Details
A	ILE354
A	LEU355
A	ALA356
A	ALA541
B	ILE354
B	LEU355
B	ALA356
B	ALA541

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN

Chain	Residue	Details
A	ILE360
B	ILE360

site_id	SWS_FT_FI12
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO

Chain	Residue	Details
A	THR649
B	PHE742
B	ASN781
B	VAL782
A	PRO656
A	LEU678
A	PHE742
A	ASN781
A	VAL782
B	THR649
B	PRO656
B	LEU678

site_id	SWS_FT_FI13
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P59158

Chain	Residue	Details
A	SER44
A	SER50
A	SER74
A	GLU127
B	SER44
B	SER50
B	SER74
B	GLU127

site_id	SWS_FT_FI14
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by OXSR1 and STK39 => ECO:0000269\|PubMed:18270262

Chain	Residue	Details
A	THR47
A	THR56
A	THR61
B	THR47
B	THR56
B	THR61

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P59158

Chain	Residue	Details
A	THR51
A	SER125
B	THR51
B	SER125

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphoserine; by OXSR1 and STK39 => ECO:0000305\|PubMed:18270262, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER92
B	SER92

site_id	SWS_FT_FI17
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:36351028, ECO:0007744\|PDB:7Y6I

Chain	Residue	Details
A	ASP407
A	PHE427
B	ASP407
B	PHE427

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