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	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	1902476	biological_process	chloride transmembrane transport
A	1904044	biological_process	response to aldosterone
A	1990573	biological_process	potassium ion import across plasma membrane
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	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	1296
Details	TOPO_DOM: Cytoplasmic => 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	MET2-TRP138
B	VAL479-GLY508
B	SER546-TRP568
B	LEU601-LEU1022
A	ALA191-LEU221
A	GLY362-PRO372
A	VAL479-GLY508
A	SER546-TRP568
A	LEU601-LEU1022
B	MET2-TRP138
B	ALA191-LEU221
B	GLY362-PRO372

site_id	SWS_FT_FI2
Number of Residues	58
Details	TRANSMEM: Discontinuously helical; Name=1 => 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	VAL139-ILE168
B	VAL139-ILE168

site_id	SWS_FT_FI3
Number of Residues	42
Details	TRANSMEM: Helical; Name=2 => 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	VAL169-SER190
B	VAL169-SER190

site_id	SWS_FT_FI4
Number of Residues	44
Details	TRANSMEM: Helical; Name=3 => 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	ILE222-ASP244
B	ILE222-ASP244

site_id	SWS_FT_FI5
Number of Residues	148
Details	TOPO_DOM: Extracellular => 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	LEU245-PRO256
A	SER395-ALA454
A	GLU524-ILE528
B	LEU245-PRO256
B	SER395-ALA454
B	GLU524-ILE528

site_id	SWS_FT_FI6
Number of Residues	48
Details	TRANSMEM: Helical; Name=4 => 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	ILE257-TRP281
B	ILE257-TRP281

site_id	SWS_FT_FI7
Number of Residues	44
Details	TRANSMEM: Helical; Name=5 => 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	GLU282-THR304
B	GLU282-THR304

site_id	SWS_FT_FI8
Number of Residues	68
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:36351028, ECO:0000269\|PubMed:36792826, ECO:0000305, 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	LEU305-THR339
B	LEU305-THR339

site_id	SWS_FT_FI9
Number of Residues	42
Details	TRANSMEM: Discontinuously helical; Name=6 => 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	PHE340-SER361
B	PHE340-SER361

site_id	SWS_FT_FI10
Number of Residues	42
Details	TRANSMEM: Helical; Name=7 => 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	LYS373-GLY394
B	LYS373-GLY394

site_id	SWS_FT_FI11
Number of Residues	46
Details	TRANSMEM: Helical; Name=8 => 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	PRO455-LYS478
B	PRO455-LYS478

site_id	SWS_FT_FI12
Number of Residues	28
Details	TRANSMEM: Helical; Name=9 => 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	TYR509-ALA523
B	TYR509-ALA523

site_id	SWS_FT_FI13
Number of Residues	32
Details	TRANSMEM: Helical; Name=10 => 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	ALA529-PHE545
B	ALA529-PHE545

site_id	SWS_FT_FI14
Number of Residues	38
Details	TRANSMEM: Helical; Name=11 => 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	ALA569-ALA588
B	ALA569-ALA588

site_id	SWS_FT_FI15
Number of Residues	22
Details	TRANSMEM: Helical; Name=12 => 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	ALA589-LEU600
B	ALA589-LEU600

site_id	SWS_FT_FI16
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_FI17
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_FI18
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_FI19
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_FI20
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_FI21
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:36351028, ECO:0000305\|PubMed:36792826, ECO:0007744\|PDB:8FHT

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

site_id	SWS_FT_FI22
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_FI23
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_FI24
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_FI25
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_FI26
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_FI27
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_FI28
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)